| Accession | TIGR01682 |
| Name | moaD |
| Function | molybdopterin converting factor, subunit 1 |
| Gene Symbol | moaD |
| Trusted Cutoff | 66.15 |
| Domain Trusted Cutoff | 66.15 |
| Noise Cutoff | 57.65 |
| Domain Noise Cutoff | 57.65 |
| Isology Type | equivalog |
| HMM Length | 80 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Molybdopterin |
| Gene Ontology Term | GO:0003824: catalytic activity molecular_function |
| | GO:0006777: Mo-molybdopterin cofactor biosynthetic process biological_process |
| Author | Haft DH |
| Entry Date | Sep 19 2002 3:14PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes MoaD. It excludes archaeal homologs, since many Archaea have two MoaD-like proteins, suggesting two different functions. The Pfam HMM PF02597 describes both the thiamine biosynthesis protein ThiS and this protein, MoaD, a subunit (together with MoaE, Pfam:PF02391) of the molybdopterin converting factor. Both ThiS and MoaD are involved in sulfur transfer reactions. Distribution of this family appears limited to species that also have a member of PF02391, but a number of Archaea have two different members, suggesting functionally distinct subtypes.
The C-terminal Gly-Gly of this model is critical to function. |
| References | DR EXPERIMENTAL; SP|P30748; Escherichia coli
DR EXPERIMENTAL; SP|O96033; Homo sapiens |
| Genome Property | GenProp0466: molybdopterin biosynthesis (HMM) |
