| UniProt functional annotation for Q8P8J2 | |||
| UniProt code: Q8P8J2. |
| Organism: | Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25). | |
| Taxonomy: | Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas. | |
| Function: | Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine. {ECO:0000269|PubMed:16585758}. | |
| Catalytic activity: | Reaction=carbamoyl phosphate + N(2)-acetyl-L-ornithine = H(+) + N(2)- acetyl-L-citrulline + phosphate; Xref=Rhea:RHEA:18609, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57805, ChEBI:CHEBI:58228, ChEBI:CHEBI:58765; EC=2.1.3.9; Evidence={ECO:0000269|PubMed:16585758}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18610; Evidence={ECO:0000305|PubMed:16585758}; | |
| Activity regulation: | Carboxylation at Lys-302 increases the catalytic activity of the enzyme (PubMed:20695527). Is potently inhibited by N(alpha)-acetyl-N(delta)-phosphonoacetyl-L-ornithine (PALAO) (PubMed:16585758). {ECO:0000269|PubMed:16585758, ECO:0000269|PubMed:20695527}. | |
| Biophysicochemical properties: | Kinetic parameters: KM=0.01 mM for carbamoyl phosphate {ECO:0000269|PubMed:16585758}; KM=1.05 mM for N(2)-acetyl-L-ornithine {ECO:0000269|PubMed:16585758}; Vmax=65.28 umol/min/mg enzyme towards N(2)-acetyl-L-ornithine {ECO:0000269|PubMed:16585758}; Vmax=50.68 umol/min/mg enzyme towards carbamoyl phosphate {ECO:0000269|PubMed:16585758}; | |
| Pathway: | Amino-acid biosynthesis; L-arginine biosynthesis. {ECO:0000305|PubMed:16585758}. | |
| Subunit: | Homotrimer. {ECO:0000269|PubMed:15731101, ECO:0000269|PubMed:16741992}. | |
| Subcellular location: | Cytoplasm {ECO:0000305}. | |
| Similarity: | Belongs to the aspartate/ornithine carbamoyltransferase superfamily. AOTCase family. {ECO:0000255|HAMAP-Rule:MF_02234, ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.