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UniProt functional annotation for Q5FAK7 | ||
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| UniProt code: Q5FAK7. |
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| Organism: | |
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). |
| Taxonomy: | |
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria. |
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| Catalytic activity: | |
Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000256|ARBA:ARBA00000016, ECO:0000256|HAMAP- Rule:MF_01105}; |
| Pathway: | |
Amino-acid biosynthesis; L-arginine biosynthesis. {ECO:0000256|ARBA:ARBA00004730}. |
| Pathway: | |
Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 1/4. {ECO:0000256|ARBA:ARBA00004925, ECO:0000256|HAMAP-Rule:MF_01105}. |
| Subcellular location: | |
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}. |
| Miscellaneous: | |
In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role. {ECO:0000256|HAMAP-Rule:MF_01105}. |
| Similarity: | |
Belongs to the acetyltransferase family. ArgA subfamily. {ECO:0000256|ARBA:ARBA00009145, ECO:0000256|HAMAP-Rule:MF_01105}. |
Annotations taken from UniProtKB at the EBI.