SCOP 1.73: Domain d2fn3a3: 2fn3 A:342-525

Lineage for d2fn3a3 (2fn3 A:342-525)

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 d2fn3a3: 2fn3 A:342-525 [133805]
   Other proteins in same PDB: d2fn3a1, d2fn3a2
   automatically matched to d1mcza3
   complexed with ca, mg, tzd; mutant

Details for d2fn3a3

PDB Entry: 2fn3, 1 Å

PDB Description: high resolution structure of s26a mutant of benzoylformate decarboxylase from pseudomonas putida complexed with thiamine thiazolone diphosphate

PDB Compounds: (A:) Benzoylformate decarboxylase

SCOP Domain Sequences for d2fn3a3:

Sequence; same for both SEQRES and ATOM records:

>d2fn3a3 c.36.1.9 (A:342-525) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stvs

Timeline for d2fn3a3:

• d2fn3a3 is new in SCOP 1.73
  
• d2fn3a3 appears in SCOP 1.75
  
• d2fn3a3 appears in the current release, SCOPe 2.08