SCOPe 2.08: Domain d1ozfa3: 1ozf A:367-554

Lineage for d1ozfa3 (1ozf A:367-554)

1. Root: SCOPe 2.08

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 Catabolic acetolactate synthase [102333] (1 species)

7. Species Klebsiella pneumoniae [TaxId:573] [102334] (3 PDB entries)

8. Domain d1ozfa3: 1ozf A:367-554 [93823]
   Other proteins in same PDB: d1ozfa1, d1ozfa2, d1ozfb1, d1ozfb2
   complexed with mg, peg, po4, tpp

Details for d1ozfa3

PDB Entry: 1ozf, 2.3 Å

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

PDB Compounds: (A:) Acetolactate synthase, catabolic

SCOPe Domain Sequences for d1ozfa3:

Sequence; same for both SEQRES and ATOM records:

>d1ozfa3 c.36.1.9 (A:367-554) Catabolic acetolactate synthase {Klebsiella pneumoniae [TaxId: 573]}
nqfalhplrivramqdivnsdvtltvdmgsfhiwiarylytfrarqvmisngqqtmgval
pwaigawlvnperkvvsvsgdggflqssmeletavrlkanvlhliwvdngynmvaiqeek
kyqrlsgvefgpmdfkayaesfgakgfavesaealeptlraamdvdgpavvaipvdyrdn
pllmgqlh

Timeline for d1ozfa3:

• d1ozfa3 first appeared in SCOP 1.67
  
• d1ozfa3 appears in SCOPe 2.07