ID   ILVB_PARMW              Reviewed;         617 AA.
AC   Q7U5G1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=SYNW1746;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; BX569693; CAE08261.1; -; Genomic_DNA.
DR   RefSeq; WP_011128606.1; NC_005070.1.
DR   AlphaFoldDB; Q7U5G1; -.
DR   SMR; Q7U5G1; -.
DR   STRING; 84588.SYNW1746; -.
DR   EnsemblBacteria; CAE08261; CAE08261; SYNW1746.
DR   KEGG; syw:SYNW1746; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_3; -.
DR   OMA; CFGTSGP; -.
DR   OrthoDB; 391134at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001422; 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; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN           1..617
FT                   /note="Acetolactate synthase large subunit"
FT                   /id="PRO_0000090806"
FT   REGION          413..492
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         71
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
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         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         490
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   617 AA;  65621 MW;  1DC3EF3BB5086E2F CRC64;
     MTLTSASTVV GGLDANAPQT ISGAAALMDA LRRHGVDTIF GYPGGAILPI YDALHIAESE
     GWVKHILVRH EQAGTHAADA YARATGKVGV CFGTSGPGAT NLVTGIATAQ MDSVPMVVIT
     GQVPRPAIGT DAFQETDIFG ITLPIVKHSW VVRDPADLGS IVAQAFLIAA SGRPGPVLID
     IPKDVGQEQF NYVPVEPGSV IPGGFHQPEP PLDAAVAAAL DLIEQAQRPL LYVGGGAISA
     CAHDSLRMLA ERYQLPVTTT LMGKGAFDEN DALSVGMLGM HGTAYANFAV TECDLLIAVG
     ARFDDRVTGK LDTFAPRARV VHFEIDPAEI GKNRKADVAV LGDLGLSLAR MVEISLQRTA
     EPRTAAWLER INTWKDRYPL TIPPAEGAIY PQEVLLAVRD LAPDAIVTTD VGQHQMWAAQ
     HLRNGPRGWI SSAGLGTMGF GMPAAMGAQV AMPDRQVVCI AGDASILMNI QELGTLAAYG
     LPVKVVIVNN HWQGMVRQWQ ESFYDERYSA SDMLNGMPDF IALARSFGVD GVKITDRELL
     HRDLAAALQS PTPTMIDVHV RRGENCYPMV PPGKSNAQMV GLPSHPELAM GTTRTCSSCG
     AITAHEHRFC PQCGASL