SCOP 1.73: Domain d1v5ea2: 1v5e A:3-186

Lineage for d1v5ea2 (1v5e A:3-186)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 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] (8 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

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

7. Species Aerococcus viridans [TaxId:1377] [142203] (4 PDB entries)

8. Domain d1v5ea2: 1v5e A:3-186 [119845]
   Other proteins in same PDB: d1v5ea1, d1v5ea3
   complexed with fad, so4

Details for d1v5ea2

PDB Entry: 1v5e, 1.6 Å

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

PDB Compounds: (A:) Pyruvate oxidase

SCOP Domain Sequences for d1v5ea2:

Sequence; same for both SEQRES and ATOM records:

>d1v5ea2 c.36.1.5 (A:3-186) Pyruvate oxidase {Aerococcus viridans [TaxId: 1377]}
dnkiniglavmkileswgadtiygipsgtlsslmdamgeeennvkflqvkheevgamaav
mqskfggnlgvtvgsggpgashlinglydaamdnipvvailgsrpqrelnmdafqelnqn
pmydhiavynrrvayaeqlpklvdeaarmaiakrgvavlevpgdfakveidndqwyssan
slrk

Timeline for d1v5ea2:

• d1v5ea2 is new in SCOP 1.73
  
• d1v5ea2 appears in SCOP 1.75
  
• d1v5ea2 appears in the current release, SCOPe 2.08