Class c: Alpha and beta proteins (a/b) [51349] (147 folds) |
Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily) 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465 |
Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 families) there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules |
Family c.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (8 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology |
Protein Benzoylformate decarboxylase [88756] (1 species) |
Species Pseudomonas putida [TaxId:303] [88757] (9 PDB entries) Uniprot P20906 |
Domain d2v3wd3: 2v3w D:342-525 [152476] Other proteins in same PDB: d2v3wa1, d2v3wa2, d2v3wb1, d2v3wb2, d2v3wc1, d2v3wc2, d2v3wd1, d2v3wd2 automatically matched to d1mcza3 complexed with mg, so4, tpp; mutant |
PDB Entry: 2v3w (more details), 2.2 Å
SCOP Domain Sequences for d2v3wd3:
Sequence; same for both SEQRES and ATOM records: (download)
>d2v3wd3 c.36.1.9 (D:342-525) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]} epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygaa rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev stvs
Timeline for d2v3wd3: