SCOP 1.67: Domain d1bfd_3: 1bfd 342-524

Lineage for d1bfd_3 (1bfd 342-524)

1. Root: SCOP 1.67

2. Class c: Alpha and beta proteins (a/b) [51349] (130 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.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (7 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology

6. Protein Benzoylformate decarboxylase [88756] (1 species)

7. Species Pseudomonas putida [TaxId:303] [88757] (2 PDB entries)

8. Domain d1bfd_3: 1bfd 342-524 [31802]
   Other proteins in same PDB: d1bfd_1, d1bfd_2
   complexed with ca, mg, tpp

Details for d1bfd_3

PDB Entry: 1bfd, 1.6 Å

PDB Description: benzoylformate decarboxylase from pseudomonas putida

SCOP Domain Sequences for d1bfd_3:

Sequence; same for both SEQRES and ATOM records:

>d1bfd_3 c.36.1.9 (342-524) Benzoylformate decarboxylase {Pseudomonas putida}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv

Timeline for d1bfd_3:

• d1bfd_3 first appeared (with stable ids) in SCOP 1.55
  
• d1bfd_3 appears in SCOP 1.65
  
• d1bfd_3 appears in SCOP 1.69
  
• d1bfd_3 appears in the current release, SCOPe 2.08, called d1bfda3