Class c: Alpha and beta proteins (a/b) [51349] (134 folds) |
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 |
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 |
Family c.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (7 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology |
Protein Catabolic acetolactate synthase [102328] (1 species) |
Species Klebsiella pneumoniae [TaxId:573] [102329] (3 PDB entries) |
Domain d1ozfb2: 1ozf B:5-187 [93825] Other proteins in same PDB: d1ozfa1, d1ozfa3, d1ozfb1, d1ozfb3 complexed with mg, peg, po4, tpp |
PDB Entry: 1ozf (more details), 2.3 Å
SCOP Domain Sequences for d1ozfb2:
Sequence, based on SEQRES records: (download)
>d1ozfb2 c.36.1.5 (B:5-187) Catabolic acetolactate synthase {Klebsiella pneumoniae} ypvrqwahgadlvvsqleaqgvrqvfgipgakidkvfdslldssiriipvrheanaafma aavgritgkagvalvtsgpgcsnlitgmatansegdpvvalggavkradkakqvhqsmdt vamfspvtkyaievtapdalaevvsnafraaeqgrpgsafvslpqdvvdgpvsgkvlpas gap
>d1ozfb2 c.36.1.5 (B:5-187) Catabolic acetolactate synthase {Klebsiella pneumoniae} ypvrqwahgadlvvsqleaqgvrqvfgipgakidkvfdslldssiriipvrheanaafma aavgritgkagvalvtsgpgcsnlitgmatansegdpvvalggavkradkakqsmdtvam fspvtkyaievtapdalaevvsnafraaeqgrpgsafvslpqdvvdgpvsgkvlpap
Timeline for d1ozfb2: