SCOPe 2.06: Domain d1v5ea3: 1v5e A:364-592

Lineage for d1v5ea3 (1v5e A:364-592)

1. Root: SCOPe 2.06

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 Aerococcus viridans [TaxId:1377] [142207] (2 PDB entries)

8. Domain d1v5ea3: 1v5e A:364-592 [119846]
   Other proteins in same PDB: d1v5ea1, d1v5ea2
   complexed with fad, so4

Details for d1v5ea3

PDB Entry: 1v5e, 1.6 Å

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

PDB Compounds: (A:) Pyruvate oxidase

SCOPe Domain Sequences for d1v5ea3:

Sequence; same for both SEQRES and ATOM records:

>d1v5ea3 c.36.1.9 (A:364-592) Pyruvate oxidase {Aerococcus viridans [TaxId: 1377]}
gdlqfyqvynainnhadedaiysidvgnstqtsirhlhmtpknmwrtsplfatmgiaipg
glgakntypdrqvwniigdgafsmtypdvvtnvrynmpvinvvfsnteyafiknkyedtn
knlfgvdftdvdyakiaeaqgakgftvsriedmdrvmaeavaankaghtvvidckitqdr
pipvetlkldsklysedeikaykeryeaanlvpfreyleaegleskyik

Timeline for d1v5ea3:

• d1v5ea3 first appeared in SCOP 1.73
  
• d1v5ea3 appears in SCOPe 2.05
  
• d1v5ea3 appears in SCOPe 2.07
  
• d1v5ea3 appears in the current release, SCOPe 2.08