Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Cofac_haem_bdg domain-containing protein
Schiff-base intermediate with substrate; via pyruvic acid
Schiff-base intermediate with acetaldehyde
Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity
Resolvase/invertase-type recombinase catalytic
2-oxoglutarate carboxylase small subunit
Interaction with polymerase core subunit RpoC
O-(5'-phospho-DNA)-tyrosine intermediate
Proton acceptor; for FBP phosphatase activity
Proton donor/acceptor; for FBP aldolase activity
Schiff-base intermediate with DHAP; for FBP aldolase activity
ADP-ribosylarginine; by dinitrogenase reductase ADP- ribosyltransferase
ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase
Nucleophile; cysteine thiosulfonate intermediate
Arginine biosynthesis bifunctional protein ArgJ alpha chain
Arginine biosynthesis bifunctional protein ArgJ beta chain
L-cysteine S-thiosulfotransferase subunit SoxA
Nitrous oxide reductase accessory protein NosL
Nucleophile; for GTP cyclohydrolase activity
Proton acceptor; for GTP cyclohydrolase activity
Biotin_lipoyl_2 domain-containing protein
Fibronectin type-III domain-containing protein
Important for interaction with partner proteins
Gly-cisPro motif, important for rejection of L-amino acids
Proton acceptor; for processing activity
S-adenosylmethionine decarboxylase alpha chain
S-adenosylmethionine decarboxylase beta chain
Thioredoxin-like_fold domain-containing protein
2-oxoglutarate carboxylase large subunit
Proton acceptor; for glutaminase activity
Almost loss of activity. Does not alter binding of the substrate analog Fe-URO III.
Does not affect didecarboxysiroheme production. Cannot bind the substrate analog Fe-URO III.
Does not affect didecarboxysiroheme production. Does not alter binding of the substrate analog Fe-URO III.
Does not affect didecarboxysiroheme production. Shows a reduced ability to bind the substrate analog Fe-URO III.
Loss of activity. Abolishes binding of the substrate analog Fe-URO III.
Loss of activity. Does not alter binding of the substrate analog Fe-URO III.
Cysteine sulfenic acid (-SOH) intermediate
2-(S-cysteinyl)pyruvic acid O-phosphothioketal