SCOP 1.67: Domain d1qpbb3: 1qpb B:361-556

Lineage for d1qpbb3 (1qpb B:361-556)

1. Root: SCOP 1.67

2. Class c: Alpha and beta proteins (a/b) [51349] (130 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] (7 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 [88750] (3 species)

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [88752] (2 PDB entries)

8. Domain d1qpbb3: 1qpb B:361-556 [31784]
   Other proteins in same PDB: d1qpba1, d1qpba2, d1qpbb1, d1qpbb2

Details for d1qpbb3

PDB Entry: 1qpb, 2.4 Å

PDB Description: pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide

SCOP Domain Sequences for d1qpbb3:

Sequence; same for both SEQRES and ATOM records:

>d1qpbb3 c.36.1.9 (B:361-556) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
astplkqewmwnqlgnflqegdvviaetgtsafginqttfpnntygisqvlwgsigfttg
atlgaafaaeeidpkkrvilfigdgslqltvqeistmirwglkpylfvlnndgytiekli
hgpkaqyneiqgwdhlsllptfgakdyethrvattgewdkltqdksfndnskirmievml
pvfdapqnlveqaklt

Timeline for d1qpbb3:

• d1qpbb3 first appeared (with stable ids) in SCOP 1.55
  
• d1qpbb3 appears in SCOP 1.65
  
• d1qpbb3 appears in SCOP 1.69
  
• d1qpbb3 appears in the current release, SCOPe 2.08