SCOP 1.73: Domain d2fwna2: 2fwn A:2-181

Lineage for d2fwna2 (2fwn A:2-181)

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.36.1.5: 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] (8 PDB entries)

8. Domain d2fwna2: 2fwn A:2-181 [134250]
   Other proteins in same PDB: d2fwna1, d2fwna3
   automatically matched to d1bfd_2
   complexed with ca, mg, tdp

Details for d2fwna2

PDB Entry: 2fwn, 1.4 Å

PDB Description: phosphorylation of an active site serine in a thdp-dependent enzyme by phosphonate inactivation

PDB Compounds: (A:) Benzoylformate decarboxylase

SCOP Domain Sequences for d2fwna2:

Sequence; same for both SEQRES and ATOM records:

>d2fwna2 c.36.1.5 (A:2-181) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss

Timeline for d2fwna2:

• d2fwna2 is new in SCOP 1.73
  
• d2fwna2 appears in SCOP 1.75
  
• d2fwna2 appears in the current release, SCOPe 2.08