SCOPe 2.02: Domain d1ozga2: 1ozg A:6-187

Lineage for d1ozga2 (1ozg A:6-187)

1. Root: SCOPe 2.02

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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 Catabolic acetolactate synthase [102328] (1 species)

7. Species Klebsiella pneumoniae [TaxId:573] [102329] (3 PDB entries)

8. Domain d1ozga2: 1ozg A:6-187 [93828]
   Other proteins in same PDB: d1ozga1, d1ozga3, d1ozgb1, d1ozgb3
   complexed with he3, mg, peg, po4

Details for d1ozga2

PDB Entry: 1ozg, 2.3 Å

PDB Description: The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate

PDB Compounds: (A:) Acetolactate synthase, catabolic

SCOPe Domain Sequences for d1ozga2:

Sequence; same for both SEQRES and ATOM records:

>d1ozga2 c.36.1.5 (A:6-187) Catabolic acetolactate synthase {Klebsiella pneumoniae [TaxId: 573]}
pvrqwahgadlvvsqleaqgvrqvfgipgakidkvfdslldssiriipvrheanaafmaa
avgritgkagvalvtsgpgcsnlitgmatansegdpvvalggavkradkakqvhqsmdtv
amfspvtkyaievtapdalaevvsnafraaeqgrpgsafvslpqdvvdgpvsgkvlpasg
ap

Timeline for d1ozga2:

• d1ozga2 first appeared in SCOP 1.67
  
• d1ozga2 appears in SCOPe 2.01
  
• d1ozga2 appears in SCOPe 2.03
  
• d1ozga2 appears in the current release, SCOPe 2.08