SCOPe 2.02: Domain d1pi3a2: 1pi3 A:2-181

Lineage for d1pi3a2 (1pi3 A:2-181)

1. Root: SCOPe 2.02

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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] (8 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] (9 PDB entries)
   Uniprot P20906

8. Domain d1pi3a2: 1pi3 A:2-181 [111634]
   Other proteins in same PDB: d1pi3a1, d1pi3a3
   complexed with ca, mg, tzd; mutant

Details for d1pi3a2

PDB Entry: 1pi3, 1.2 Å

PDB Description: e28q mutant benzoylformate decarboxylase from pseudomonas putida

PDB Compounds: (A:) Benzoylformate decarboxylase

SCOPe Domain Sequences for d1pi3a2:

Sequence; same for both SEQRES and ATOM records:

>d1pi3a2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
asvhgttyellrrqgidtvfgnpgsnqlpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss

Timeline for d1pi3a2:

• d1pi3a2 first appeared in SCOP 1.71
  
• d1pi3a2 appears in SCOPe 2.01
  
• d1pi3a2 appears in SCOPe 2.03
  
• d1pi3a2 appears in the current release, SCOPe 2.08