SCOP 1.65: Domain d1powa2: 1pow A:9-182

Lineage for d1powa2 (1pow A:9-182)

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 oxidase [88729] (1 species)

7. Species Lactobacillus plantarum [TaxId:1590] [88730] (2 PDB entries)

8. Domain d1powa2: 1pow A:9-182 [31797]
   Other proteins in same PDB: d1powa1, d1powa3, d1powb1, d1powb3

Details for d1powa2

PDB Entry: 1pow, 2.5 Å

PDB Description: the refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum

SCOP Domain Sequences for d1powa2:

Sequence; same for both SEQRES and ATOM records:

>d1powa2 c.36.1.5 (A:9-182) Pyruvate oxidase {Lactobacillus plantarum}
tnilagaavikvleawgvdhlygipggsinsimdalsaerdrihyiqvrheevgamaaaa
dakltgkigvcfgsagpggthlmnglydaredhvpvlaligqfgttgmnmdtfqemnenp
iyadvadynvtavnaatlphvideairrayahqgvavvqipvdlpwqqipaedw

Timeline for d1powa2:

• d1powa2 first appeared (with stable ids) in SCOP 1.55
  
• d1powa2 appears in SCOP 1.63
  
• d1powa2 appears in SCOP 1.67
  
• d1powa2 appears in the current release, SCOPe 2.08