SCOPe 2.07: Domain d1ozfb1: 1ozf B:188-366

Lineage for d1ozfb1 (1ozf B:188-366)

1. Root: SCOPe 2.07

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 d1ozfb1: 1ozf B:188-366 [93824]
   Other proteins in same PDB: d1ozfa2, d1ozfa3, d1ozfb2, d1ozfb3
   complexed with mg, peg, po4, tpp

Details for d1ozfb1

PDB Entry: 1ozf, 2.3 Å

PDB Description: The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors

PDB Compounds: (B:) Acetolactate synthase, catabolic

SCOPe Domain Sequences for d1ozfb1:

Sequence, based on SEQRES records:

>d1ozfb1 c.31.1.3 (B:188-366) Catabolic acetolactate synthase {Klebsiella pneumoniae [TaxId: 573]}
qmgaapddaidqvakliaqaknpifllglmasqpenskalrrlletshipvtstyqaaga
vnqdnfsrfagrvglfnnqagdrllqladlvicigyspveyepamwnsgnatlvhidvlp
ayeernytpdvelvgdiagtlnklaqnidhrlvlspqaaeilrdrqhqrelldrrgaql

Sequence, based on observed residues (ATOM records):

>d1ozfb1 c.31.1.3 (B:188-366) Catabolic acetolactate synthase {Klebsiella pneumoniae [TaxId: 573]}
qmgaapddaidqvakliaqaknpifllglmasqpenskalrrlletshipvtstyqaaga
vnqdnfsrfagrvglfnnqagdrllqladlvicigyspveyepamwnsgnatlvhidvlp
ayeernytpdvelvgdiagtlnklaqnidhrlvlspqaaeilrdrqhqrelldraql

Timeline for d1ozfb1:

• d1ozfb1 first appeared in SCOP 1.67
  
• d1ozfb1 appears in SCOPe 2.06
  
• d1ozfb1 appears in the current release, SCOPe 2.08