ILVB_KLEAE
ID ILVB_KLEAE Reviewed; 32 AA.
AC Q09129;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Acetolactate synthase, catabolic;
DE Short=ALS;
DE EC=2.2.1.6;
DE Flags: Fragment;
GN Name=budB;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VTT-E-87292;
RX PubMed=8444801; DOI=10.1128/jb.175.5.1392-1404.1993;
RA Blomqvist K., Nikkola M., Lehtovaara P., Suihko M.-L., Airaksinen U.,
RA Straby K.B., Knowles J.K.C., Penttilae M.E.;
RT "Characterization of the genes of the 2,3-butanediol operons from
RT Klebsiella terrigena and Enterobacter aerogenes.";
RL J. Bacteriol. 175:1392-1404(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC butane-2,3-diol from pyruvate: step 1/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Does not seem to require thiamine pyrophosphate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; L04506; AAA56802.1; -; Genomic_DNA.
DR PIR; B47069; B47069.
DR AlphaFoldDB; Q09129; -.
DR SMR; Q09129; -.
DR UniPathway; UPA00626; UER00677.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..>32
FT /note="Acetolactate synthase, catabolic"
FT /id="PRO_0000090796"
FT NON_TER 32
SQ SEQUENCE 32 AA; 3530 MW; 0BA63C108E0878BB CRC64;
MNSEKQSRQW AHGADMVVGQ LEAQGVKQVF GI