SCOP 1.67: Domain d1pvda1: 1pvd A:182-360

Lineage for d1pvda1 (1pvd A:182-360)

1. Root: SCOP 1.67

2. Class c: Alpha and beta proteins (a/b) [51349] (130 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] (5 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] (7 proteins)
   N-terminal domain is Pyr module, and C-terminal domain is PP module of thiamin diphosphate-binding fold

6. Protein Pyruvate decarboxylase [52478] (3 species)
   rudiment domain with a variant fold, lacks FAD-binding

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [52480] (2 PDB entries)

8. Domain d1pvda1: 1pvd A:182-360 [31737]
   Other proteins in same PDB: d1pvda2, d1pvda3, d1pvdb2, d1pvdb3

Details for d1pvda1

PDB Entry: 1pvd, 2.3 Å

PDB Description: crystal structure of the thiamin diphosphate dependent enzyme pyruvate decarboxylase from the yeast saccharomyces cerevisiae at 2.3 angstroms resolution

SCOP Domain Sequences for d1pvda1:

Sequence; same for both SEQRES and ATOM records:

>d1pvda1 c.31.1.3 (A:182-360) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
qtpidmslkpndaesekevidtilalvkdaknpviladaccsrhdvkaetkklidltqfp
afvtpmgkgsiseqhpryggvyvgtlskpevkeavesadlilsvgallsdktknivefhs
dhmkirnatfpgvqmkfvlqklltniadaakgykpvavpartpanaavp

Timeline for d1pvda1:

• d1pvda1 first appeared (with stable ids) in SCOP 1.55
  
• d1pvda1 appears in SCOP 1.65
  
• d1pvda1 appears in SCOP 1.69
  
• d1pvda1 appears in the current release, SCOPe 2.08