ID   ILVB_CORGL              Reviewed;         626 AA.
AC   P42463;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Acetolactate synthase large subunit;
DE            Short=AHAS;
DE            EC=2.2.1.6;
DE   AltName: Full=Acetohydroxy-acid synthase large subunit;
DE            Short=ALS;
GN   Name=ilvB; OrderedLocusNames=Cgl1271, cg1435;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=8366043; DOI=10.1128/jb.175.17.5595-5603.1993;
RA   Keilhauer C., Eggeling L., Sahm H.;
RT   "Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of
RT   the ilvB-ilvN-ilvC operon.";
RL   J. Bacteriol. 175:5595-5603(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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   -!- 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   -!- SUBUNIT: Dimer of large and small chains.
CC   -!- MISCELLANEOUS: Contains 1 molecule of FAD per monomer. The role of this
CC       cofactor is not clear considering that the reaction does not involve
CC       redox chemistry (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; L09232; AAA62429.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98664.1; -; Genomic_DNA.
DR   EMBL; BX927151; CAF19974.1; -; Genomic_DNA.
DR   PIR; A48648; A48648.
DR   RefSeq; NP_600493.1; NC_003450.3.
DR   RefSeq; WP_011014246.1; NC_006958.1.
DR   AlphaFoldDB; P42463; -.
DR   SMR; P42463; -.
DR   STRING; 196627.cg1435; -.
DR   World-2DPAGE; 0001:P42463; -.
DR   KEGG; cgb:cg1435; -.
DR   KEGG; cgl:Cgl1271; -.
DR   PATRIC; fig|196627.13.peg.1248; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_11; -.
DR   OMA; CFGTSGP; -.
DR   BRENDA; 2.2.1.6; 960.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000000582; Chromosome.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02015; TPP_AHAS; 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-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; TIGR00118; acolac_lg; 1.
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..626
FT                   /note="Acetolactate synthase large subunit"
FT                   /id="PRO_0000090787"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..496
FT                   /note="Thiamine pyrophosphate binding"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         73
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         281..302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         324..343
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         494
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   626 AA;  66846 MW;  C425E93F83B8A946 CRC64;
     MNVAASQQPT PATVASRGRS AAPERMTGAK AIVRSLEELN ADIVFGIPGG AVLPVYDPLY
     SSTKVRHVLV RHEQGAGHAA TGYAQVTGRV GVCIATSGPG ATNLVTPIAD ANLDSVPMVA
     ITGQVGSGLL GTDAFQEADI RGITMPVTKH NFMVTNPNDI PQALAEAFHL AITGRPGPVL
     VDIPKDVQNA ELDFVWPPKI DLPGYRPVST PHARQIEQAV KLIGEAKKPV LYVGGGVIKA
     DAHEELRAFA EYTGIPVVTT LMALGTFPES HELHMGMPGM HGTVSAVGAL QRSDLLIAIG
     SRFDDRVTGD VDTFAPDAKI IHADIDPAEI GKIKQVEVPI VGDAREVLAR LLETTKASKA
     ETEDISEWVD YLKGLKARFP RGYDEQPGDL LAPQFVIETL SKEVGPDAIY CAGVGQHQMW
     AAQFVDFEKP RTWLNSGGLG TMGYAVPAAL GAKAGAPDKE VWAIDGDGCF QMTNQELTTA
     AVEGFPIKIA LINNGNLGMV RQWQTLFYEG RYSNTKLRNQ GEYMPDFVTL SEGLGCVAIR
     VTKAEEVLPA IQKAREINDR PVVIDFIVGE DAQVWPMVSA GSSNSDIQYA LGLRPFFDGD
     ESAAEDPADI HEAVSDIDAA VESTEA