SCOP 1.63: Domain d1powb3: 1pow B:366-593

Lineage for d1powb3 (1pow B:366-593)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 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] (4 families)
   both pyridine (Pyr)- and pyrophosphate (PP)-binding modules have this fold
   conserved core consists of two Pyr and two PP-modules and binds two coenzyme molecules

5. Family c.36.1.1: Pyruvate oxidase and decarboxylase THDP-binding domains [52519] (4 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 [52524] (1 species)

7. Species Lactobacillus plantarum [TaxId:1590] [52525] (2 PDB entries)

8. Domain d1powb3: 1pow B:366-593 [31800]
   Other proteins in same PDB: d1powa1, d1powb1
   complexed with fad, mg, tpp

Details for d1powb3

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 d1powb3:

Sequence; same for both SEQRES and ATOM records:

>d1powb3 c.36.1.1 (B:366-593) Pyruvate oxidase {Lactobacillus plantarum}
kqegplqayqvlravnkiaepdaiysidvgdinlnanrhlkltpsnrhitsnlfatmgvg
ipgaiaaklnyperqvfnlagdggasmtmqdlatqvqyhlpvinvvftncqygfikdeqe
dtnqndfigvefndidfskiadgvhmqafrvnkieqlpdvfeqakaiaqhepvlidavit
gdrplpaeklrldsamssaadieafkqryeaqdlqplstylkqfgldd

Timeline for d1powb3:

• d1powb3 first appeared (with stable ids) in SCOP 1.55
  
• d1powb3 appears in SCOP 1.61
  
• d1powb3 appears in SCOP 1.65
  
• d1powb3 appears in the current release, SCOPe 2.08