SCOP 1.65: Domain d1ovmd2: 1ovm D:3-180

Lineage for d1ovmd2 (1ovm D:3-180)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 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] (5 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 Indole-3-pyruvate decarboxylase [89648] (1 species)

7. Species Enterobacter cloacae [TaxId:550] [89649] (1 PDB entry)

8. Domain d1ovmd2: 1ovm D:3-180 [87471]
   Other proteins in same PDB: d1ovma1, d1ovma3, d1ovmb1, d1ovmb3, d1ovmc1, d1ovmc3, d1ovmd1, d1ovmd3
   complexed with mg, tpp

Details for d1ovmd2

PDB Entry: 1ovm, 2.65 Å

PDB Description: Crystal structure of Indolepyruvate decarboxylase from Enterobacter cloacae

SCOP Domain Sequences for d1ovmd2:

Sequence; same for both SEQRES and ATOM records:

>d1ovmd2 c.36.1.5 (D:3-180) Indole-3-pyruvate decarboxylase {Enterobacter cloacae}
tpycvadylldrltdcgadhlfgvpgdynlqfldhvidspdicwvgcanelnasyaadgy
arckgfaallttfgvgelsamngiagsyaehvpvlhivgapgtaaqqrgellhhtlgdge
frhfyhmsepitvaqavlteqnacyeidrvlttmlrerrpgylmlpadvakkaatppv

Timeline for d1ovmd2:

• d1ovmd2 is new in SCOP 1.65
  
• d1ovmd2 appears in SCOP 1.67
  
• d1ovmd2 appears in the current release, SCOPe 2.08