![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 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] (7 PDB entries) Uniprot P20906 |
![]() | Domain d1q6za2: 1q6z A:2-181 [111656] Other proteins in same PDB: d1q6za1, d1q6za3 complexed with ca, mg, tzd; mutant |
PDB Entry: 1q6z (more details), 1 Å
SCOPe Domain Sequences for d1q6za2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1q6za2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]} asvhgttyellrrqgidtvfgnpgsnalpflkdfpedfryilalqeacvvgiadgyaqas rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
Timeline for d1q6za2: