Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Belongs to the enoyl-CoA hydratase/isomerase family.
Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.
Catalyzes the oxidation of L-aspartate to iminoaspartate.
Belongs to the helicase family. PriA subfamily.
Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Belongs to the PEP-utilizing enzyme family.
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Belongs to the outer membrane factor (OMF) (TC 1.B.17) family.
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Belongs to the ClpX chaperone family. HslU subfamily.
Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Heterooctamer of four alpha and four beta subunits.
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Belongs to the SLC41A transporter family.
Belongs to the bacterial secretin family.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Belongs to the BlaI transcriptional regulatory family.
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the anion channel-forming bestrophin (TC 1.A.46) family.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
A monovalent cation. Ammonium or potassium.
Belongs to the type III pantothenate kinase family.
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Belongs to the glycosyltransferase 87 family.
Belongs to the methyl-accepting chemotaxis (MCP) protein family.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
Belongs to the LysR transcriptional regulatory family.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Belongs to the sigma-70 factor family. ECF subfamily.
Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
Belongs to the small heat shock protein (HSP20) family.
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the iron/manganese superoxide dismutase family.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Belongs to the type IA topoisomerase family.
Belongs to the creatininase superfamily.
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Belongs to the transaldolase family. Type 2 subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the DNA polymerase type-Y family.
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
Interacts transiently with the RNA polymerase catalytic core.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the glycosyl hydrolase 18 family.
Belongs to the zinc-containing alcohol dehydrogenase family.
Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109 subfamily.
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the glutamate 5-kinase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to IF-3.
Belongs to the thiolase-like superfamily. Thiolase family.
Belongs to the histidinol dehydrogenase family.
Belongs to the ATPase epsilon chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the urease beta subunit family.
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
The glycine cleavage system catalyzes the degradation of glycine.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
Part of the 30S ribosomal subunit. Contacts proteins S9 and S11.
Belongs to the class-C beta-lactamase family.
Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Belongs to the KHG/KDPG aldolase family.
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW.
Homodimer; the beta-strands of each monomer intercalate to form a hydrophobic core, while the alpha-helices form wings that extend away from the core.
Belongs to the heat shock protein 90 family.
Molecular chaperone. Has ATPase activity.
Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily.
Belongs to the glycogen phosphorylase family.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
The system is composed of three essential subunits: KdpA, KdpB and KdpC.
Belongs to the ThrE exporter (TC 2.A.79) family.
Belongs to the GTP cyclohydrolase I family.
Belongs to the glycosyl hydrolase 57 family.
To bacterial alkanal monooxygenase alpha and beta chains.
Belongs to the universal stress protein A family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Belongs to the chaperonin (HSP60) family.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Belongs to the radical SAM superfamily. Biotin synthase family.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Belongs to the asparagine synthetase family.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Belongs to the universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.
Belongs to the tRNA pseudouridine synthase TruA family.
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Belongs to the bacterial ribosomal protein bL20 family.
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Belongs to the bacterial ribosomal protein bL21 family.
Part of the 50S ribosomal subunit. Contacts protein L20.
This protein binds to 23S rRNA in the presence of protein L20.
Belongs to the universal ribosomal protein uS17 family.
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs.
Belongs to the aromatic-ring hydroxylase family. TetX subfamily.
Consists of an N-terminal FAD-binding domain with a Rossman fold and a C-terminal substrate-binding domain.
Belongs to the bacterial solute-binding protein SsuA/TauA family.
Belongs to the cytochrome ubiquinol oxidase subunit 1 family.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Belongs to the pantothenate synthetase family.
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
The reaction proceeds by a bi uni uni bi ping pong mechanism.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the complex I 51 kDa subunit family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Belongs to the glycosyltransferase group 1 family.
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Belongs to the pseudouridine synthase RluA family.
Responsible for synthesis of pseudouridine from uracil.
Belongs to the glycosyltransferase 2 family.
Belongs to the universal ribosomal protein uL5 family.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
This is 1 of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Belongs to the metallophosphoesterase superfamily. YfcE family.
Belongs to the acyl coenzyme A hydrolase family.
Belongs to the ABC transporter superfamily. Ycf16 family.
Belongs to the precorrin methyltransferase family.
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
In the C-terminal section; belongs to the cytidylyltransferase family.
In the N-terminal section; belongs to the carbohydrate kinase PfkB family.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Heterotetramer of two alpha and two beta subunits.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the thiolase-like superfamily. FabH family.
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Belongs to the DNA polymerase type-A family.
In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
Belongs to the phD/YefM antitoxin family.
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Heterooligomer composed of large and small subunits.
Belongs to the adenosylhomocysteinase family.
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the AIR carboxylase family. Class I subfamily.
Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.
Belongs to the universal ribosomal protein uL24 family.
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the beta-eliminating lyase family.
Belongs to the carbamoyltransferase HypF family.
Endoribonuclease that initiates mRNA decay.
Belongs to the glutamate synthase family.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.
GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis.
Monomer. Associates with the 50S ribosomal subunit.
In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.
In the central section; belongs to the CRISPR-associated helicase Cas3 family.
Belongs to the complex I 49 kDa subunit family.
NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Essential for recycling GMP and indirectly, cGMP.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes.
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Belongs to the intradiol ring-cleavage dioxygenase family.
Belongs to the GTP-binding SRP family. FtsY subfamily.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.
Belongs to the RbsD / FucU family. RbsD subfamily.
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.
Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.
Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Binds 1 divalent metal cation per subunit.
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Belongs to the glycerate kinase type-1 family.
Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Belongs to the inositol monophosphatase superfamily.
Belongs to the bacterial ribosomal protein bL33 family.
Belongs to the thioester dehydratase family. FabA subfamily.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Belongs to the phosphohexose mutase family.
Heterodimer of an alpha and a beta chain.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Belongs to the ATPase delta chain family.
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
Monomer. Binds directly to the core enzyme of the DNA-dependent RNA polymerase and to nascent RNA.
Participates in both transcription termination and antitermination.
Belongs to the vitamin-B12 dependent methionine synthase family.
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Belongs to the 'phage' integrase family. XerC subfamily.
Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD.
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Belongs to the IS21/IS1162 putative ATP-binding protein family.
Belongs to the glutamine synthetase family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Belongs to the bacterial ribosomal protein bL12 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
Belongs to the mandelate racemase/muconate lactonizing enzyme family.
Belongs to the pseudouridine synthase TruD family.
Belongs to the acyl-CoA dehydrogenase family.
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Belongs to the glycosyl hydrolase 43 family.
Belongs to the xanthine dehydrogenase family.
Belongs to the SecD/SecF family. SecD subfamily.
Belongs to the SecD/SecF family. SecF subfamily.
Forms a complex with SecD. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Forms a complex with SecF. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Belongs to the glycosyl hydrolase 13 family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer.
Belongs to the universal ribosomal protein uS2 family.
Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.
Belongs to the succinate/malate CoA ligase beta subunit family.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Belongs to the MqnA/MqnD family. MqnA subfamily.
Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
Belongs to the ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
Tetramer of two alpha and two beta subunits.
Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
Belongs to the helicase family. RecQ subfamily.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Belongs to the ATPase gamma chain family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Belongs to the bacterial ribosomal protein bL28 family.
Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
Belongs to the membrane-bound acyltransferase family.
Binds to the N-terminal domain of the chaperone ClpA.
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Belongs to the GcvP family. C-terminal subunit subfamily.
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits.
Belongs to the threonine aldolase family.
Once thought to be involved in copper homeostasis, experiments in E.coli have shown this is not the case.
Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.
Belongs to the LeuD family. LeuD type 1 subfamily.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the universal ribosomal protein uL1 family.
Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase.
Belongs to the ABC transporter superfamily. ABCF family. Translational throttle EttA subfamily.
Monomer. Probably contacts ribosomal proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P-site containing tRNA(fMet).
The P-site tRNA interaction motif (PtIM domain) probably interacts with the P-site tRNA(fMet) as well as the 23S rRNA.
The arm domain is inserted in the first ABC transporter domain. Probably contacts ribosomal protein L1.
Belongs to the helicase family. RAD25/XPB subfamily.
Belongs to the ribonucleoside diphosphate reductase class-2 family.
Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition.
Toxic component of a type II toxin-antitoxin (TA) system.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Belongs to the peptide transporter carbon starvation (CstA) (TC 2.A.114) family.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
In the C-terminal section; belongs to the helicase family. RecG subfamily.
In the N-terminal section; belongs to the UvrB family.
Involved in 1,2-propanediol (1,2-PD) degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate.
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Belongs to the protein prenyltransferase subunit beta family.
Belongs to the complex I subunit 2 family.
NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
Belongs to the aldehyde dehydrogenase family.
Belongs to the bacterial solute-binding protein 3 family.
Belongs to the binding-protein-dependent transport system permease family.
A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product.
Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Belongs to the histone deacetylase family.
Homohexameric ring arranged as a trimer of dimers.
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone.
Binds 1 thiamine pyrophosphate per subunit.
Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site.
The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus.
Belongs to the glycosyl hydrolase 130 family.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Belongs to the LDH/MDH superfamily. MDH type 2 family.
Catalyzes the reversible oxidation of malate to oxaloacetate.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Heterotetramer of two alpha and two beta chains.
Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the tRNA(Ile)-lysidine synthase family.
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Belongs to the shikimate dehydrogenase family.
Belongs to the type-I 3-dehydroquinase family.
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Belongs to the bacterial reverse transcriptase family.
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Belongs to the ferritin family. Prokaryotic subfamily.
Belongs to the prokaryotic/mitochondrial release factor family.
Belongs to the RNA methyltransferase RsmE family.
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Belongs to the SIS family. GutQ/KpsF subfamily.
Belongs to the ABC transporter superfamily. ABCF family. Uup subfamily.
Probably plays a role in ribosome assembly or function. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA and has ATPase activity.
Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Belongs to the DNA mismatch repair MutS family.
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Belongs to the complex I subunit 4 family.
Belongs to the DNA gyrase inhibitor YacG family.
Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Belongs to the elongation factor P family.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the conversion of dihydroorotate to orotate.
Belongs to the transcriptional regulatory CopG/NikR family.
Belongs to the bacterial ribosomal protein bL9 family.
Belongs to the Maf family. YceF subfamily.
Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Belongs to the triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.
Belongs to the heme-copper respiratory oxidase family.
Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit.
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
Belongs to the N-acylglucosamine 2-epimerase family.
Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
Belongs to the heat shock protein 70 family.
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18.
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Belongs to the universal ribosomal protein uS8 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S5 and S12.
Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Belongs to the polypeptide deformylase family.
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the POLIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex.
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Belongs to the transaldolase family. Type 1 subfamily.
Belongs to the bacterial microcompartments protein family.
Belongs to the RNA polymerase alpha chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Antitoxin component of a type II toxin-antitoxin (TA) system.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Belongs to the Mg-chelatase subunits D/I family.
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Belongs to the selenium-binding protein family.
Belongs to the glutamyl-tRNA reductase family.
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family.
Belongs to the cytochrome c oxidase subunit 3 family.
Belongs to the group II decarboxylase family.
Belongs to the CRISPR-associated endonuclease Cas1 family.
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
Homodimer, forms a heterotetramer with a Cas2 homodimer.
Belongs to the complex I subunit 5 family.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Belongs to the metallo-dependent hydrolases superfamily.
Belongs to the complex I subunit 6 family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.
Belongs to the complex I 23 kDa subunit family.
Belongs to the bacterial solute-binding protein 2 family.
Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Binds AI-2 and delivers it to the LsrC and LsrD permeases.
The complex is composed of two ATP-binding proteins (LsrA), two transmembrane proteins (LsrC and LsrD) and a solute-binding protein (LsrB).
Belongs to the alpha-acetolactate decarboxylase family.
Catalyzes the ferrous insertion into protoporphyrin IX.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
In the C-terminal section; belongs to the MurCDEF family.
Belongs to the cytochrome ubiquinol oxidase subunit 2 family.
Belongs to the gamma-glutamyltransferase family.
Cleaved by autocatalysis into a large and a small subunit.
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Belongs to the homogentisate dioxygenase family.
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Carbamylation allows a single lysine to coordinate two nickel ions.
Carboxylation allows a single lysine to coordinate two nickel ions.
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Belongs to the urease gamma subunit family.
Belongs to the universal ribosomal protein uL6 family.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Belongs to the anti-sigma-factor antagonist family.
Belongs to the glycosyltransferase 28 family.
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Belongs to the ribonucleoside diphosphate reductase small chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
Belongs to the arylamine N-acetyltransferase family.
Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
Oligomer of 12 subunits arranged in the form of two hexagons.
Belongs to the polyribonucleotide nucleotidyltransferase family.
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Belongs to the uracil-DNA glycosylase (UDG) superfamily. Type 4 (UDGa) family.
Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Belongs to the deoxyhypusine synthase family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Belongs to the universal ribosomal protein uS4 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S5 and S12 plays an important role in translational accuracy.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Belongs to the HAD-like hydrolase superfamily.
Divalent metal ions. Mg(2+) is the most effective.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Belongs to the bacterial ribosomal protein bL35 family.
Belongs to the glycosyl hydrolase 24 family.
Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.
CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Binds between the large and small subunits.
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of vitamin B12.
The basic unit is a heterodimer which dimerizes to form tetramers. The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards.
Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
Homodimer, forms a heterotetramer with a Cas1 homodimer.
Belongs to the ribonucleoside diphosphate reductase large chain family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily.
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Catalyzes the removal of dipeptides from the N-terminus of oligopeptides.
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Interacts with translational regulator CsrA and flagellin(s).
Belongs to the glycosyl hydrolase 32 family.
Belongs to the complex I 30 kDa subunit family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Belongs to the universal ribosomal protein uL22 family.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily.
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the amidase family. GatA subfamily.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
Belongs to the band 7/mec-2 family. HflK subfamily.
HflC and HflK could encode or regulate a protease.
HflC and HflK may interact to form a multimeric complex.
Belongs to the beta-class carbonic anhydrase family.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.
In the C-terminal section; belongs to the Mrp/NBP35 ATP-binding proteins family.
In the N-terminal section; belongs to the MIP18 family.
Belongs to the methyltransferase superfamily. RsmH family.
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Belongs to the complex I 24 kDa subunit family.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Catalyzes the reversible phosphorylation of UMP to UDP.
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Belongs to the glycosyl hydrolase 25 family.
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Belongs to the threonine synthase family.
Belongs to the universal ribosomal protein uL2 family.
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
The C-terminal coiled-coil domain is crucial for aminoacylation activity.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Belongs to the azoreductase type 1 family.
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Belongs to the dethiobiotin synthetase family.
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Belongs to the universal ribosomal protein uL14 family.
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8.
Belongs to the DNA mismatch repair MutL/HexB family.
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Belongs to the peptidase M28 family. M28B subfamily.
Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Belongs to the universal ribosomal protein uL16 family.
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Belongs to the glycosyl hydrolase 33 family.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (CysA), two transmembrane proteins (CysT and CysW) and a solute-binding protein (CysP).
Binds 1 dipyrromethane group covalently.
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
The porphobilinogen subunits are added to the dipyrromethane group.
Divalent metal cations. Prefers magnesium or manganese.
Catalyzes the reversible hydration of fumarate to (S)-malate.
Belongs to the universal ribosomal protein uL4 family.
Forms part of the polypeptide exit tunnel.
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the trans-sulfuration enzymes family.
Belongs to the universal ribosomal protein uL11 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
One or more lysine residues are methylated.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the fatty acid desaturase type 2 family.
Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the methylthiotransferase family. RimO subfamily.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Belongs to the bacterial sugar transferase family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
Belongs to the FtsK/SpoIIIE/SftA family.
Homohexamer. Forms a ring that surrounds DNA.
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Homodimer. Probably interacts with PlsY.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Belongs to the pyruvoyl-dependent arginine decarboxylase family.
Belongs to the pyrroline-5-carboxylate reductase family.
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Belongs to the radical SAM superfamily. MqnE family.
Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate, leading to aminodeoxyfutalosine (AFL), a key intermediate in the formation of menaquinone (MK, vitamin K2) from chorismate.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Involved in DNA repair and RecF pathway recombination.
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Belongs to the P-Pant transferase superfamily. AcpS family.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Plays a role in the regulation of phosphate uptake.
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Na(+) is not transported, but it plays an essential structural role and its presence is essential for fluoride channel function.
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Belongs to the diaminopimelate epimerase family.
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Belongs to the universal ribosomal protein uL10 family.
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the SurE nucleotidase family.
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Belongs to the DcuC/DcuD transporter (TC 2.A.61) family.
Belongs to the dihydrofolate reductase family.
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Homodimer which binds Holliday junction (HJ) DNA. The HJ becomes 2-fold symmetrical on binding to RuvC with unstacked arms; it has a different conformation from HJ DNA in complex with RuvA. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Belongs to the prokaryotic sulfate-binding protein family.
Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Belongs to the bacterial ribosomal protein bS20 family.
Belongs to the cytochrome c oxidase subunit 2 family.
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Belongs to the ATP:guanido phosphotransferase family.
Catalyzes the specific phosphorylation of arginine residues in proteins.
Belongs to the aconitase/IPM isomerase family.
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Belongs to the methylenetetrahydrofolate reductase family.
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Belongs to the universal ribosomal protein uS13 family.
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Belongs to the major facilitator superfamily. TCR/Tet family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Belongs to the PTPS family. QueD subfamily.
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Belongs to the PAPS reductase family. CysH subfamily.
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
In the C-terminal section; belongs to the NRP synthetase family.
Belongs to the DNA glycosylase MPG family.
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Belongs to the helicase family. UvrD subfamily.
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Belongs to the transketolase family. DXPS subfamily.
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
May be involved in the biosynthesis of molybdopterin.
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Belongs to the pseudouridine synthase RsuA family.
Belongs to the PNP/MTAP phosphorylase family.
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Belongs to the polyphosphate kinase 1 (PPK1) family.
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
Belongs to the complex I subunit 1 family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Belongs to the methyltransferase superfamily.
Catalyzes the 3-fold methylation of ornithine lipids. Forms ornithine lipids that are mono-, di-, and trimethylated on the delta-nitrogen of the ornithine head group.
In the N-terminal section; belongs to the cytochrome P450 family.
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Belongs to the PAPS reductase family. CysD subfamily.
Heterodimer composed of CysD, the smaller subunit, and CysN.
With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Belongs to the complex I subunit 4L family.
Binds 1 Mn(2+) or Fe(2+) ion per subunit.
Belongs to the NiCoT transporter (TC 2.A.52) family.
Belongs to the PINc/VapC protein family.
Toxic component of a toxin-antitoxin (TA) system. An RNase.
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
Interacts with the Sec translocase complex via SecD. Specifically interacts with transmembrane segments of nascent integral membrane proteins during membrane integration.
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the bacterial ribosomal protein bS6 family.
Binds together with bS18 to 16S ribosomal RNA.
Belongs to the cytidine and deoxycytidylate deaminase family.
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Belongs to the endoribonuclease YbeY family.
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.
Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Belongs to the universal ribosomal protein uL13 family.
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS.
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines.
Catalyzes the transfer of a formyl group from 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) to produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin (H(4)MPT).
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
Belongs to the SorC transcriptional regulatory family.
Belongs to the acetolactate synthase small subunit family.
Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Belongs to the MsrA Met sulfoxide reductase family.
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import.
Belongs to the methylthiotransferase family. MiaB subfamily.
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Belongs to the OMP decarboxylase family. Type 2 subfamily.
Belongs to the universal ribosomal protein uL3 family.
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Belongs to the 2-oxoacid dehydrogenase family.
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
The active site is a redox-active disulfide bond.
Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Belongs to the bacterial ribosomal protein bS18 family.
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6.
A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalyzes the attachment of glycine to tRNA(Gly).
Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
Belongs to the universal ribosomal protein uS5 family.
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Part of the 30S ribosomal subunit. Contacts proteins S4 and S8.
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S4 and S12 plays an important role in translational accuracy.
Catalyzes the synthesis of GMP from XMP.
Belongs to the homoserine dehydrogenase family.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the universal ribosomal protein uS12 family.
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.
With S4 and S5 plays an important role in translational accuracy.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Belongs to the SAM hydrolase / SAM-dependent halogenase family.
Belongs to the FKBP-type PPIase family. Tig subfamily.
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the Cu-Zn superoxide dismutase family.
Belongs to the neutral ceramidase family.
Belongs to the chorismate synthase family.
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Belongs to the radical SAM superfamily. RlmN family.
Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Could be involved in insertion of integral membrane proteins into the membrane.
Homohexamer. The oligomerization is ATP-dependent.
Homohexamer; The oligomerization is ATP-dependent.
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE.
Belongs to the anhydro-N-acetylmuramic acid kinase family.
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-insensitive subfamily.
Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
Belongs to the GcvP family. N-terminal subunit subfamily.
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.
Part of an energy-coupled inorganic carbon pump.
Belongs to the bacterial solute-binding protein ModA family.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the formate--tetrahydrofolate ligase family.
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Belongs to the Maf family. YhdE subfamily.
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Belongs to the FPP/GGPP synthase family.
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
APS kinase catalyzes the synthesis of activated sulfate.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
In the C-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Belongs to the GHMP kinase family. IspE subfamily.
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
In the C-terminal section; belongs to the OsmX family.
In the N-terminal section; belongs to the binding-protein-dependent transport system permease family.
Belongs to the flotillin-like FloA family.
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Involved in the system for phosphate transport across the cytoplasmic membrane.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the beta sliding clamp family.
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Forms a ring-shaped head-to-tail homodimer around DNA.
Belongs to the methyltransferase superfamily. Arsenite methyltransferase family.
Belongs to the N(4)/N(6)-methyltransferase family.
Belongs to the transferase hexapeptide repeat family.
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Belongs to the band 7/mec-2 family. HflC subfamily.
HflC and HflK could regulate a protease.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Belongs to the thiamine-phosphate synthase family.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Belongs to the universal ribosomal protein uL18 family.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Belongs to the RNA polymerase subunit omega family.
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Belongs to the bacterial ribosomal protein bL36 family.
Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Belongs to the ketol-acid reductoisomerase family.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Belongs to the ABC-2 integral membrane protein family.
E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
The beta-hairpin motif is involved in DNA binding.
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Belongs to the aspartate-semialdehyde dehydrogenase family.
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Homohexamer. Organized in a ring with a central cavity.
Belongs to the GTP cyclohydrolase II family.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
In the N-terminal section; belongs to the DHBP synthase family.
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Belongs to the ATP-dependent AMP-binding enzyme family.
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
Belongs to the bacterial histone-like protein family.
Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family.
Involved in protein export. Participates in an early event of protein translocation.
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Belongs to the MurCDEF family. MurE subfamily.
Belongs to the Mg-chelatase subunits D/I family. ComM subfamily.
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Participates in transcription elongation, termination and antitermination.
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Belongs to the band 7/mec-2 family. Flotillin subfamily.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Interacts transiently with the RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. SDR39U1 subfamily.
Belongs to the anthranilate phosphoribosyltransferase family.
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Involved in the catabolism of quinolinic acid (QA).
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Belongs to the glycosyl hydrolase 2 family.
Belongs to the ribose 5-phosphate isomerase family.
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Belongs to the thioester dehydratase family. FabZ subfamily.
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
Interacts with ribosomal protein uL14 (rplN).
The IMP cyclohydrolase activity resides in the N-terminal region.
Belongs to the bacterial diacylglycerol kinase family.
Belongs to the universal ribosomal protein uL23 family.
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome.
Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Belongs to the RNR ribonuclease family. RNase R subfamily.
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
Belongs to the glycosyl hydrolase 1 family.
Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
Belongs to the peroxiredoxin family. Tpx subfamily.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Belongs to the SAICAR synthetase family.
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
Belongs to the RNA polymerase beta chain family.
2 residues (Tyr-66 and Arg-69) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity.
Belongs to the sirtuin family. Class III subfamily.
NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
In the C-terminal section; belongs to the NAD synthetase family.
Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Belongs to the radical SAM superfamily. MqnC family.
Radical SAM enzyme that catalyzes the cyclization of dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.
Heterodimer of a large and a small subunit.
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Belongs to the thiamine-monophosphate kinase family.
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Catalyzes the epimerization of D-tagaturonate (D-TagA) to D-fructuronate (D-FruA).
Belongs to the RNA methyltransferase TrmD family.
Specifically methylates guanosine-37 in various tRNAs.
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Belongs to the NADH dehydrogenase family.
Belongs to the cytidylate kinase family. Type 1 subfamily.
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
Binds 1 S-adenosyl-L-methionine per subunit.
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
Belongs to the arginase family. Agmatinase subfamily.
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Belongs to the Cob(I)alamin adenosyltransferase family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.
Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the MsrB Met sulfoxide reductase family.
Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Belongs to the GatB/GatE family. GatB subfamily.
Belongs to the pseudouridine-5'-phosphate glycosidase family.
Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Belongs to the universal ribosomal protein uS15 family.
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the helicase family. DnaB subfamily.
Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Belongs to the universal ribosomal protein uL29 family.