![]() | Class c: Alpha and beta proteins (a/b) [51349] (130 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 d1ozhc2: 1ozh C:7-186 [93840] Other proteins in same PDB: d1ozha1, d1ozha3, d1ozhb1, d1ozhb3, d1ozhc1, d1ozhc3, d1ozhd1, d1ozhd3 |
PDB Entry: 1ozh (more details), 2 Å
SCOP Domain Sequences for d1ozhc2:
Sequence, based on SEQRES records: (download)
>d1ozhc2 c.36.1.5 (C:7-186) Catabolic acetolactate synthase {Klebsiella pneumoniae} vrqwahgadlvvsqleaqgvrqvfgipgakidkvfdslldssiriipvrheanaafmaaa vgritgkagvalvtsgpgcsnlitgmatansegdpvvalggavkradkakqvhqsmdtva mfspvtkyaievtapdalaevvsnafraaeqgrpgsafvslpqdvvdgpvsgkvlpasga
>d1ozhc2 c.36.1.5 (C:7-186) Catabolic acetolactate synthase {Klebsiella pneumoniae} vrqwahgadlvvsqleaqgvrqvfgipgakidkvfdslldssiriipvrheanaafmaaa vgritgkagvalvtsgpgcsnlitgmatansegdpvvalggavkradkakmdtvamfspv tkyaievtapdalaevvsnafraaeqgrpgsafvslpqdvvdgpvsgkvlpasga
Timeline for d1ozhc2: