SCOPe 2.04: Domain d2djia2: 2dji A:3-186

Lineage for d2djia2 (2dji A:3-186)

1. Root: SCOPe 2.04

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 Aerococcus viridans [TaxId:1377] [142203] (2 PDB entries)

8. Domain d2djia2: 2dji A:3-186 [131545]
   Other proteins in same PDB: d2djia1, d2djia3
   automated match to d1v5ea2
   complexed with fad, so4

Details for d2djia2

PDB Entry: 2dji, 1.6 Å

PDB Description: Crystal Structure of Pyruvate Oxidase from Aerococcus viridans containing FAD

PDB Compounds: (A:) Pyruvate oxidase

SCOPe Domain Sequences for d2djia2:

Sequence; same for both SEQRES and ATOM records:

>d2djia2 c.36.1.5 (A:3-186) Pyruvate oxidase {Aerococcus viridans [TaxId: 1377]}
dnkiniglavmkileswgadtiygipsgtlsslmdamgeeennvkflqvkheevgamaav
mqskfggnlgvtvgsggpgashlinglydaamdnipvvailgsrpqrelnmdafqelnqn
pmydhiavynrrvayaeqlpklvdeaarmaiakrgvavlevpgdfakveidndqwyssan
slrk

Timeline for d2djia2:

• d2djia2 first appeared in SCOP 1.73
  
• d2djia2 appears in SCOPe 2.03
  
• d2djia2 appears in SCOPe 2.05
  
• d2djia2 appears in the current release, SCOPe 2.08