SCOPe 2.05: Domain d1poxb2: 1pox B:9-182

Lineage for d1poxb2 (1pox B:9-182)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (9 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] (8 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology
   automatically mapped to Pfam PF02776

6. Protein Pyruvate oxidase [88729] (2 species)

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

8. Domain d1poxb2: 1pox B:9-182 [31795]
   Other proteins in same PDB: d1poxa1, d1poxa3, d1poxb1, d1poxb3
   complexed with fad, gol, mg, na, tpp; mutant

Details for d1poxb2

PDB Entry: 1pox, 2.1 Å

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

PDB Compounds: (B:) Pyruvate oxidase

SCOPe Domain Sequences for d1poxb2:

Sequence; same for both SEQRES and ATOM records:

>d1poxb2 c.36.1.5 (B:9-182) Pyruvate oxidase {Lactobacillus plantarum [TaxId: 1590]}
tnilagaavikvleawgvdhlygipggsinsimdalsaerdrihyiqvrheevgamaaaa
dakltgkigvcfgsagpggthlmnglydaredhvpvlaligqfgttgmnmdtfqemnenp
iyadvadynvtavnaatlphvideairrayahqgvavvqipvdlpwqqisaedw

Timeline for d1poxb2:

• d1poxb2 first appeared (with stable ids) in SCOP 1.55
  
• d1poxb2 appears in SCOPe 2.04
  
• d1poxb2 appears in SCOPe 2.06
  
• d1poxb2 appears in the current release, SCOPe 2.08