| 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] (9 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 automatically mapped to Pfam PF02776 |
| Protein Benzoylformate decarboxylase [88731] (1 species) |
| Species Pseudomonas putida [TaxId:303] [88732] (10 PDB entries) Uniprot P20906 |
| Domain d2fn3a2: 2fn3 A:2-181 [133804] Other proteins in same PDB: d2fn3a1, d2fn3a3 automatically matched to d1bfd_2 complexed with ca, mg, tzd; mutant |
PDB Entry: 2fn3 (more details), 1 Å
SCOPe Domain Sequences for d2fn3a2:
Sequence; same for both SEQRES and ATOM records: (download)
>d2fn3a2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
asvhgttyellrrqgidtvfgnpganelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
Timeline for d2fn3a2: