| Accession | TIGR01161 |
| Name | purK |
| Function | phosphoribosylaminoimidazole carboxylase, ATPase subunit |
| Gene Symbol | purK |
| Trusted Cutoff | 318.40 |
| Domain Trusted Cutoff | 318.40 |
| Noise Cutoff | 197.10 |
| Domain Noise Cutoff | 197.10 |
| Isology Type | equivalog_domain |
| EC Number | 4.1.1.21 |
| HMM Length | 362 |
| Mainrole Category | Purines, pyrimidines, nucleosides, and nucleotides |
| Subrole Category | Purine ribonucleotide biosynthesis |
| Gene Ontology Term | GO:0004638: phosphoribosylaminoimidazole carboxylase activity molecular_function |
| | GO:0009152: purine ribonucleotide biosynthetic process biological_process |
| | GO:0009320: phosphoribosylaminoimidazole carboxylase complex cellular_component |
| | GO:0016887: ATPase activity molecular_function |
| Author | Haft DH |
| Entry Date | Feb 6 2001 11:21AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. |
| References | DR SWISSPROT; P09029; PURK_ECOLI
DR ECOCYC; EG10796; purK
RM 10569930
RT Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily.
RA Thoden JB, Kappock TJ, Stubbe J, Holden HM
RL Biochemistry 1999 Nov 23;38(47):15480-92 |
| Genome Property | GenProp0110: purine (inosine-5'-phosphate) biosynthesis from ribose-5-phosphate (HMM) |
