SCOPe 2.08: Domain d1ozga1: 1ozg A:188-366

Lineage for d1ozga1 (1ozg A:188-366)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.31: DHS-like NAD/FAD-binding domain [52466] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; Rossmann-like

4. Superfamily c.31.1: DHS-like NAD/FAD-binding domain [52467] (7 families)
   binds cofactor molecules in the opposite direction than classical Rossmann fold

5. Family c.31.1.3: Pyruvate oxidase and decarboxylase, middle domain [52475] (8 proteins)
   N-terminal domain is Pyr module, and C-terminal domain is PP module of thiamin diphosphate-binding fold

6. Protein Catabolic acetolactate synthase [102288] (1 species)

7. Species Klebsiella pneumoniae [TaxId:573] [102289] (3 PDB entries)

8. Domain d1ozga1: 1ozg A:188-366 [93827]
   Other proteins in same PDB: d1ozga2, d1ozga3, d1ozgb2, d1ozgb3
   complexed with he3, mg, peg, po4

Details for d1ozga1

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 d1ozga1:

Sequence; same for both SEQRES and ATOM records:

>d1ozga1 c.31.1.3 (A:188-366) Catabolic acetolactate synthase {Klebsiella pneumoniae [TaxId: 573]}
qmgaapddaidqvakliaqaknpifllglmasqpenskalrrlletshipvtstyqaaga
vnqdnfsrfagrvglfnnqagdrllqladlvicigyspveyepamwnsgnatlvhidvlp
ayeernytpdvelvgdiagtlnklaqnidhrlvlspqaaeilrdrqhqrelldrrgaql

Timeline for d1ozga1:

• d1ozga1 first appeared in SCOP 1.67
  
• d1ozga1 appears in SCOPe 2.07