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.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (8 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology |
Protein Benzoylformate decarboxylase [88731] (1 species) |
Species Pseudomonas putida [TaxId:303] [88732] (9 PDB entries) Uniprot P20906 |
Domain d2v3wb2: 2v3w B:2-181 [152469] Other proteins in same PDB: d2v3wa1, d2v3wa3, d2v3wb1, d2v3wb3, d2v3wc1, d2v3wc3, d2v3wd1, d2v3wd3 automatically matched to d1bfda2 complexed with mg, so4, tpp; mutant |
PDB Entry: 2v3w (more details), 2.2 Å
SCOP Domain Sequences for d2v3wb2:
Sequence; same for both SEQRES and ATOM records: (download)
>d2v3wb2 c.36.1.5 (B:2-181) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]} asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
Timeline for d2v3wb2: