Top Level Name
⌊ Superfamily (core) Radical SAM
⌊ Subgroup BATS domain containing
⌊ HMD cofactor maturase (HmdB-like)
⌊ Family HMD cofactor maturase (HmdB-like)
| Total |
100%  |
<100% |
|||
| Functional domains | 39 | 39 | 0 | ||
| UniProtKB | 42 | 42 | 0 | ||
| GI | 113 | 113 | 0 | ||
| Structures | 0 | ||||
| Reactions | 0 | ||||
| Functional domains of this family were last updated on June 10, 2017 | |||||
| New functional domains were last added to this family on June 22, 2014 | |||||
The colocalization of hmdB and hmdC with hmdA (which functions in the reversible reduction of methenyl-tetrahydromethanopterin to methylene-H4MPT and H+) in the genomes of hydrogenotrophic methanogens, coupled with the similar evolutionary histories observed for deduced amino acid sequences for hmdA, hmdB, and hmdC, suggests that the genes are likely involved in a common process. This argument is bolstered by the observation that homologs of HmdB and HmdC were identified only in the genomes of hydrogenotrophic methanogens that contained hmdA. The exact function of HmdB is currently not known, although is is postulated to be involved in the biosynthesis of the HMD cofactor.
McGlynn SE, Boyd ES, Shepard EM, Lange RK, Gerlach R, Broderick JB, Peters JW
Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor
▸ Abstract
J Bacteriol 2010;192(2):595-598 | PubMed ID: 19897660
No notes.
Static File Downloads
| File Name | Description | Parameters | Stats |
|---|---|---|---|
| network.fam330.bs60.mek250K.xgmml | One node per sequence network | min bit score = 60 max edge count = 250K |
size = 440K num_edges = 741 num_nodes = 39 |
| sfld_alignment_fam330.msa | Annotated Sequence Alignment, Stockholm format | 29 sequences size: 15K |