| Accession | TIGR00326 |
| Name | eubact_ribD |
| Function | riboflavin biosynthesis protein RibD |
| Gene Symbol | ribD |
| Trusted Cutoff | 156.35 |
| Domain Trusted Cutoff | 156.35 |
| Noise Cutoff | 152.80 |
| Domain Noise Cutoff | 152.80 |
| Isology Type | equivalog |
| EC Number | 3.5.4.26 1.1.1.193 |
| HMM Length | 343 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Riboflavin, FMN, and FAD |
| Gene Ontology Term | GO:0008703: 5-amino-6-(5-phosphoribosylamino)uracil reductase activity molecular_function |
| | GO:0008835: diaminohydroxyphosphoribosylaminopyrimidine deaminase activity molecular_function |
| | GO:0009231: riboflavin biosynthetic process biological_process |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:07PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the HMM dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. |
| References | DR PROSITE; PDOC00702;
DR PFAM; PF00383; dCMP_cyt_deam;
DR PFAM; PF01872; RibD_C;
DR ECOCYC; EG11321; ribD;
SE TIGR
GA hmmls |
| Genome Property | GenProp0112: riboflavin, FAD and FMN from GTP and ribulose-5-P (HMM) |
| | GenProp0112: riboflavin, FAD and FMN from GTP and ribulose-5-P (HMM) |
