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Reduction and mobilization of iron by a NAD(P)H:flavin oxidoreductase from Escherichia coli
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FUNCTION Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. Seems to reduce the complexed Fe(3+) iron of siderophores to Fe(2+), thus releasing it from the chelator.CATALYTIC ACTIVITY Reduced riboflavin + NAD(P)(+) = riboflavin + NAD(P)H.CATALYTIC ACTIVITY 2 cob(II)alamin + NAD(+) = 2 aquacob(III)alamin + NADH.SUBUNIT Monomer.SIMILARITY Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family.SIMILARITY Contains 1 FAD-binding FR-type domain.CAUTION Was originally (PubMed:1379743) assigned to be ubiB.
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Elongation complex with growing peptide chain
70S:mRNA:peptidyl-tRNA with elongating peptide
The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
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Nicotinamidase deaminates nicotinamide to nicotinate (Frothingham et al. 1996).
Iron is reduced and separates from enterobactin
The IrtA transporter has a flavin reductase domain very much like Fre from E.coli that can probably act as ferrisiderophore reductase to relieve incoming loaded mycobactin from its Fe3+ by reducing it to Fe2+. Furthermore Rv2895c, which co-precipitates with IrtB and therefore is probably part of the transporter complex, has such a domain as well (Farhana et al. 2008).
Peptide transfer from P-site tRNA to the A-site tRNA
At the beginning of this reaction, 1 molecule of '70S:Met-tRNAi:mRNA:aa-tRNA' is present. At the end of this reaction, 1 molecule of 'Elongation complex with growing peptide chain' is present.
Translocation of ribosome by 3 bases in the 3' direction
At the beginning of this reaction, 1 molecule of 'Elongation complex with growing peptide chain' is present. At the end of this reaction, 1 molecule of '70S:mRNA:peptidyl-tRNA with elongating peptide' is present.
Bacterioferritin, like ferritin, is a spherical shell-like protein that takes up 48 ferrous iron ions, and subsequently oxidizes and hydrolyzes them for better storage. (Yang et al, 2000)
The path to perdition is paved with protons
MISCELLANEOUS The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe(2+) binding and oxidation at the ferroxidase center.SIMILARITY Belongs to the bacterioferritin family.SIMILARITY Contains 1 ferritin-like diiron domain.
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Sequential translation of trinucleotide codons for peptide bond formation, translocation, and termination
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Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes
Identification, cloning, and expression of the Escherichia coli pyrazinamidase and nicotinamidase gene, pncA
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beta-Nicotinamide adenine dinucleotide phosphate
Nicotinamide adenine dinucleotide phosphate
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gene ontology term for cellular function
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CATALYTIC ACTIVITY Nicotinamide + H(2)O = nicotinate + NH(3).PATHWAY Cofactor biosynthesis; nicotinate biosynthesis; nicotinate from nicotinamide: step 1/1.SIMILARITY Belongs to the PncA family.
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Steps of mRNA translocation in protein biosynthesis
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