SCOP 1.71: Domain d1q6za2: 1q6z A:2-181

Lineage for d1q6za2 (1q6z A:2-181)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. 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

4. 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

5. Family c.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (7 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology

6. Protein Benzoylformate decarboxylase [88731] (1 species)

7. Species Pseudomonas putida [TaxId:303] [88732] (5 PDB entries)

8. Domain d1q6za2: 1q6z A:2-181 [111656]
   Other proteins in same PDB: d1q6za1, d1q6za3
   complexed with ca, mg, tdp; mutant

Details for d1q6za2

PDB Entry: 1q6z, 1 Å

PDB Description: high resolution structure of e28a mutant benzoylformate decarboxylase from pseudomonas putida complexed with thiamin thiazolone diphosphate

SCOP Domain Sequences for d1q6za2:

Sequence; same for both SEQRES and ATOM records:

>d1q6za2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida}
asvhgttyellrrqgidtvfgnpgsnalpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss

Timeline for d1q6za2:

• d1q6za2 is new in SCOP 1.71
  
• d1q6za2 appears in SCOP 1.73
  
• d1q6za2 appears in the current release, SCOPe 2.08