SCOPe 2.08: Domain d1powa1: 1pow A:183-365

Lineage for d1powa1 (1pow A:183-365)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.31: DHS-like NAD/FAD-binding domain [52466] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; Rossmann-like

4. Superfamily c.31.1: DHS-like NAD/FAD-binding domain [52467] (7 families)
   binds cofactor molecules in the opposite direction than classical Rossmann fold

5. Family c.31.1.3: Pyruvate oxidase and decarboxylase, middle domain [52475] (8 proteins)
   N-terminal domain is Pyr module, and C-terminal domain is PP module of thiamin diphosphate-binding fold

6. Protein Pyruvate oxidase [52476] (2 species)
   binds FAD

7. Species Lactobacillus plantarum [TaxId:1590] [52477] (8 PDB entries)

8. Domain d1powa1: 1pow A:183-365 [31733]
   Other proteins in same PDB: d1powa2, d1powa3, d1powb2, d1powb3
   complexed with fad, mg, tpp; mutant

Details for d1powa1

PDB Entry: 1pow, 2.5 Å

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

PDB Compounds: (A:) Pyruvate oxidase

SCOPe Domain Sequences for d1powa1:

Sequence; same for both SEQRES and ATOM records:

>d1powa1 c.31.1.3 (A:183-365) Pyruvate oxidase {Lactobacillus plantarum [TaxId: 1590]}
yasansyqtpllpepdvqavtrltqtllaaerpliyygigarkagkeleqlsktlkiplm
stypakgivadrypaylgsanrvaqkpanealaqadvvlfvgnnypfaevskafkntryf
lqididpaklgkrhktdiavladaqktlaailaqvserestpwwqanlanvknwraylas
led

Timeline for d1powa1:

• d1powa1 first appeared (with stable ids) in SCOP 1.55
  
• d1powa1 appears in SCOPe 2.07