SCOP 1.73: Domain d1bfda3: 1bfd A:342-524

Lineage for d1bfda3 (1bfd A:342-524)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 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] (8 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] (8 PDB entries)

8. Domain d1bfda3: 1bfd A:342-524 [31802]
   Other proteins in same PDB: d1bfda1, d1bfda2
   complexed with ca, mg, tpp

Details for d1bfda3

PDB Entry: 1bfd, 1.6 Å

PDB Description: benzoylformate decarboxylase from pseudomonas putida

PDB Compounds: (A:) Benzoylformate decarboxylase

SCOP Domain Sequences for d1bfda3:

Sequence; same for both SEQRES and ATOM records:

>d1bfda3 c.36.1.9 (A:342-524) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv

Timeline for d1bfda3:

• d1bfda3 first appeared (with stable ids) in SCOP 1.55, called d1bfd_3
  
• d1bfda3 was called d1bfd_3 in SCOP 1.71
  
• d1bfda3 appears in SCOP 1.75
  
• d1bfda3 appears in the current release, SCOPe 2.08