CPSase_L_D2: Carbamoyl-phosphate synthase L chain, ATP binding domain
| PAG Title | CPSase_L_D2: Carbamoyl-phosphate synthase L chain, ATP binding domain |
| PAG ID | PEX001691 |
| Type | A |
| Source Link |  Pfam |
| Publication Reference | NA |
| PAG Description | Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines 2. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. See Pfam:PF00988. The small chain has a GATase domain in the carboxyl terminus. See Pfam:PF00117. The ATP binding domain (this one) has an ATP-grasp fold. |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 0 |
| Information Content | Poor |
| Other IDs | PF02786 |
| Base PAG ID | PEX001691 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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