SCOP 1.65: Domain d1pvda2: 1pvd A:2-181

Lineage for d1pvda2 (1pvd A:2-181)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 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] (5 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 Pyruvate decarboxylase [88725] (3 species)

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [88727] (2 PDB entries)

8. Domain d1pvda2: 1pvd A:2-181 [31777]
   Other proteins in same PDB: d1pvda1, d1pvda3, d1pvdb1, d1pvdb3

Details for d1pvda2

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 d1pvda2:

Sequence; same for both SEQRES and ATOM records:

>d1pvda2 c.36.1.5 (A:2-181) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
seitlgkylferlkqvnvntvfglpgdfnlslldkiyevegmrwagnanelnaayaadgy
arikgmsciittfgvgelsalngiagsyaehvgvlhvvgvpsishhtlgngdftvfhrms
anisettamitdiatapaeidrcirttyvtqrpvylglpanlvdlnvpakll

Timeline for d1pvda2:

• d1pvda2 first appeared (with stable ids) in SCOP 1.55
  
• d1pvda2 appears in SCOP 1.63
  
• d1pvda2 appears in SCOP 1.67
  
• d1pvda2 appears in the current release, SCOPe 2.08