| Total |
100%  |
<100% |
|||
| Functional domains | 509 | 509 | 0 | ||
| UniProtKB | 849 | 849 | 0 | ||
| GI | 1851 | 1851 | 0 | ||
| Structures | 5 | ||||
| Reactions | 1 | ||||
| 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 biosynthesis of the deazapurine base preQ(0), is catalysed by the successive action of four enzymes (GCH I, QueD, QueE and QueC). The pathway includes the conversion of the biosynthetic intermediate, 6-carboxy-5,6,7,8-tetrahydropterin, to a novel intermediate, 7-carboxy-7-deazaguanine (CDG). This family of enzymes have been characterised as QueE with the canonical member being from B. multivorans. They form a discrete cluster of sequences at an E-value of 1e-55 and have a Cx14CxxC [4Fe-4S]-AdoMet binding motif and a pruned down (ab)6 domain architecture in the form of b6/a3. As with the canonical QueE family, this set of enzymes has been shown to be Mg(II) dependent and the SAM moiety is utilised in a catalytic manner.
Dowling DP, Bruender NA, Young AP, McCarty RM, Bandarian V, Drennan CL
Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism
▸ Abstract
Nat Chem Biol 2014;10(2):106-112 | PubMed ID: 24362703
No notes.
Static File Downloads
| File Name | Description | Parameters | Stats |
|---|---|---|---|
| network.fam376.bs60.mek250K.xgmml | One node per sequence network | min bit score = 60 max edge count = 250K |
size = 67M num_edges = 129286 num_nodes = 509 |
| sfld_alignment_fam376.msa | Annotated Sequence Alignment, Stockholm format | 228 sequences size: 66K |
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