| Accession | TIGR00097 |
| Name | HMP-P_kinase |
| Function | hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase |
| Gene Symbol | thiD |
| Trusted Cutoff | 204.95 |
| Domain Trusted Cutoff | 204.95 |
| Noise Cutoff | 79.35 |
| Domain Noise Cutoff | 79.35 |
| Isology Type | equivalog_domain |
| EC Number | 2.7.1.49 2.7.4.7 |
| HMM Length | 254 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Thiamine |
| Gene Ontology Term | GO:0008972: phosphomethylpyrimidine kinase activity molecular_function |
| | GO:0009228: thiamine biosynthetic process biological_process |
| Author | Haft DH, Richardson DL, Anolik RT |
| Entry Date | Apr 20 1999 2:03PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. |
| References | RN [1]
RM PMID:10075431
RT Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase.
RA Mizote T, Tsuda M, Smith DD, Nakayama H, Nakazawa T
RL Microbiology. 1999 Feb;145 ( Pt 2):495-501. |
| Genome Property | GenProp0253: thiamine: hydroxymethylpyrimidine pyrophosphate from aminoimidazole ribotide (HMM) |
