ID   ILVB_MYCBO              Reviewed;         618 AA.
AC   P0A623; A0A1R3Y2T5; O53250; X2BN34;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   04-NOV-2026, entry version 108.
DE   RecName: Full=Acetolactate synthase;
DE            EC=2.2.1.6;
DE   AltName: Full=ALS;
DE   AltName: Full=Acetohydroxy-acid synthase;
GN   Name=ilvB; OrderedLocusNames=BQ2027_MB3028C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 pyruvate + H(+) = (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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU01652.1; -; Genomic_DNA.
DR   RefSeq; WP_003415168.1; NC_002945.4.
DR   AlphaFoldDB; P0A623; -.
DR   SMR; P0A623; -.
DR   KEGG; mbo:BQ2027_MB3028C; -.
DR   PATRIC; fig|233413.5.peg.3328; -.
DR   OMA; AAAMWCR; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005948; C:acetolactate synthase complex; IEA:TreeGrafter.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02015; TPP_AHAS; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   FunFam; 3.40.50.1220:FF:000008; Acetolactate synthase; 1.
DR   FunFam; 3.40.50.970:FF:000007; Acetolactate synthase; 1.
DR   FunFam; 3.40.50.970:FF:000016; Acetolactate synthase; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR039368; AHAS_TPP.
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_TPP-bd.
DR   NCBIfam; TIGR00118; acolac_lg; 1.
DR   NCBIfam; NF005860; PRK07789.1; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; FAD;
KW   Flavoprotein; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..618
FT                   /note="Acetolactate synthase"
FT                   /id="PRO_0000090801"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..509
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         85
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         293..314
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..355
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         480
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         507
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   618 AA;  66123 MW;  9E0523F4AD6EC6AF CRC64;
     MSAPTKPHSP TFKPEPHSAA NEPKHPAARP KHVALQQLTG AQAVIRSLEE LGVDVIFGIP
     GGAVLPVYDP LFDSKKLRHV LVRHEQGAGH AASGYAHVTG RVGVCMATSG PGATNLVTPL
     ADAQMDSIPV VAITGQVGRG LIGTDAFQEA DISGITMPIT KHNFLVRSGD DIPRVLAEAF
     HIAASGRPGA VLVDIPKDVL QGQCTFSWPP RMELPGYKPN TKPHSRQVRE AAKLIAAARK
     PVLYVGGGVI RGEATEQLRE LAELTGIPVV TTLMARGAFP DSHRQNLGMP GMHGTVAAVA
     ALQRSDLLIA LGTRFDDRVT GKLDSFAPEA KVIHADIDPA EIGKNRHADV PIVGDVKAVI
     TELIAMLRHH HIPGTIEMAD WWAYLNGVRK TYPLSYGPQS DGSLSPEYVI EKLGEIAGPD
     AVFVAGVGQH QMWAAQFIRY EKPRSWLNSG GLGTMGFAIP AAMGAKIALP GTEVWAIDGD
     GCFQMTNQEL ATCAVEGIPV KVALINNGNL GMVRQWQSLF YAERYSQTDL ATHSHRIPDF
     VKLAEALGCV GLRCEREEDV VDVINQARAI NDCPVVIDFI VGADAQVWPM VAAGTSNDEI
     QAARGIRPLF DDITEGHA
//