SCOPe 2.08: Domain d1poxb3: 1pox B:366-593

Lineage for d1poxb3 (1pox B:366-593)

1. Root: SCOPe 2.08

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.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (8 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 [88754] (2 species)

7. Species Lactobacillus plantarum [TaxId:1590] [88755] (2 PDB entries)

8. Domain d1poxb3: 1pox B:366-593 [31796]
   Other proteins in same PDB: d1poxa1, d1poxa2, d1poxb1, d1poxb2
   complexed with fad, gol, mg, na, tpp; mutant

Details for d1poxb3

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 d1poxb3:

Sequence; same for both SEQRES and ATOM records:

>d1poxb3 c.36.1.9 (B:366-593) Pyruvate oxidase {Lactobacillus plantarum [TaxId: 1590]}
kqegplqayqvlravnkiaepdaiysidvgdinlnanrhlkltpsnrhitsnlfatmgvg
ipgaiaaklnyperqvfnlagdggasmtmqdlvtqvqyhlpvinvvftncqygfikdeqe
dtnqndfigvefndidfskiadgvhmqafrvnkieqlpdvfeqakaiaqhepvlidavit
gdrplpaeklrldsamssaadieafkqryeaqdlqplstylkqfgldd

Timeline for d1poxb3:

• d1poxb3 first appeared (with stable ids) in SCOP 1.55
  
• d1poxb3 appears in SCOPe 2.07