ID   ILVB_RAOTE              Reviewed;         559 AA.
AC   Q04524;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Acetolactate synthase, catabolic;
DE            Short=ALS;
DE            EC=2.2.1.6;
GN   Name=budB;
OS   Raoultella terrigena (Klebsiella terrigena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX   NCBI_TaxID=577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VTT-E-74023;
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.
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; L04507; AAA25055.1; -; Genomic_DNA.
DR   PIR; D47069; D47069.
DR   AlphaFoldDB; Q04524; -.
DR   SMR; Q04524; -.
DR   UniPathway; UPA00626; UER00677.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   InterPro; IPR012782; Acetolactate_synth_catblc.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR02418; acolac_catab; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN           1..559
FT                   /note="Acetolactate synthase, catabolic"
FT                   /id="PRO_0000090798"
FT   BINDING         159
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         263..284
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         304..323
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   559 AA;  60153 MW;  C463407DF98B6F3F CRC64;
     MDKPRHERQW AHGADLIVSQ LEAQGVRQVF GIPGAKIDKV FDSLLDSSIR IIPVRHEANA
     AFMAAAVGRI TGKAGVALVT SGPGCSNLIT GMATANSEGD PVVALGGAVK RADKAKLVHQ
     SMDTVAMFSP VTKYAVEVTA SDALAEVVSN AFRAAEQGRP GSAFVSLPQD IVDGPASGST
     LPASRAPQMG AAPDGAVDSV AQAIAAAKNP IFLLGLMASQ PENSRALHRH AGKKPYSGHQ
     HLSGAGAVNQ DNFARFAGRV GLFNNQAGDR LLRQADLIIC IGYSPVEYEP AMWNSGTATL
     VHIDVLPAYE ERNYVPDIEL VGDIAATLEK LAQRIEHRLV LTPQAADILA DRQRQRELLD
     RRGAQLNQFA LHPLRIVRAM QDIVNSDVTL TVDMGSFHIW IARYLYSFRA RQVMISNGQQ
     TMGVALPWAI GAWLVNPQRK VVSVSGDGGF LQSSMELETA VRLHANILHI IWVDNGYNMV
     AIQEQKKYQR LSGVEFGPVD FKVYAEAFGA CGFAVESAEA LEPTLRAAMD VDGPAVVAIP
     VDYRDNPLLM GQLHLSQIL