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UniProt functional annotation for P9WPZ3 | ||
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| UniProt code: P9WPZ3. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| Function: | |
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. {ECO:0000250}. |
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| Catalytic activity: | |
Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N- acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35; |
| 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; |
| Pathway: | |
Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. |
| Pathway: | |
Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 1/4. |
| Subunit: | |
Heterotetramer of two alpha and two beta chains. {ECO:0000269|PubMed:20184895}. |
| Subcellular location: | |
Cytoplasm {ECO:0000305}. |
| Miscellaneous: | |
Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway. |
| Miscellaneous: | |
Was identified as a high-confidence drug target. |
| Similarity: | |
Belongs to the ArgJ family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.