SCOP 1.73: Domain d2fwna1: 2fwn A:182-341

Lineage for d2fwna1 (2fwn A:182-341)

1. Root: SCOP 1.73

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

3. Fold c.31: DHS-like NAD/FAD-binding domain [52466] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; Rossmann-like

4. Superfamily c.31.1: DHS-like NAD/FAD-binding domain [52467] (6 families)
   binds cofactor molecules in the opposite direction than classical Rossmann fold

5. Family c.31.1.3: Pyruvate oxidase and decarboxylase, middle domain [52475] (8 proteins)
   N-terminal domain is Pyr module, and C-terminal domain is PP module of thiamin diphosphate-binding fold

6. Protein Benzoylformate decarboxylase [52482] (1 species)

7. Species Pseudomonas putida [TaxId:303] [52483] (8 PDB entries)

8. Domain d2fwna1: 2fwn A:182-341 [134249]
   Other proteins in same PDB: d2fwna2, d2fwna3
   automatically matched to d1bfd_1
   complexed with ca, mg, tdp

Details for d2fwna1

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 d2fwna1:

Sequence; same for both SEQRES and ATOM records:

>d2fwna1 c.31.1.3 (A:182-341) Benzoylformate decarboxylase {Pseudomonas putida [TaxId: 303]}
svrlndqdldilvkalnsasnpaivlgpdvdaananadcvmlaerlkapvwvapsaprcp
fptrhpcfrglmpagiaaisqlleghdvvlvigapvfryhqydpgqylkpgtrlisvtcd
pleaarapmgdaivadigamasalanlveessrqlptaap

Timeline for d2fwna1:

• d2fwna1 is new in SCOP 1.73
  
• d2fwna1 appears in SCOP 1.75
  
• d2fwna1 appears in the current release, SCOPe 2.08