Accession | TIGR00857 |
Name | pyrC_multi |
Function | dihydroorotase, multifunctional complex type |
Gene Symbol | pyrC |
Trusted Cutoff | 279.05 |
Domain Trusted Cutoff | 279.05 |
Noise Cutoff | 197.80 |
Domain Noise Cutoff | 197.80 |
Isology Type | subfamily_domain |
EC Number | 3.5.2.3 |
HMM Length | 412 |
Mainrole Category | Purines, pyrimidines, nucleosides, and nucleotides |
Subrole Category | Pyrimidine ribonucleotide biosynthesis |
Gene Ontology Term | GO:0004151: dihydroorotase activity molecular_function |
| GO:0009220: pyrimidine ribonucleotide biosynthetic process biological_process |
Author | Haft DH, Durkin S |
Entry Date | Aug 3 2000 3:23PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present.
The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins.
All proteins described by this HMM should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. |
References | DR PROSITE; PDOC00401; Dihydroorotase signatures
DR HAMAP; MF_01645; 2 of 26 |
Genome Property | GenProp0187: pyrimidine (uridine-5'-phosphate) de novo biosynthesis (HMM) |