ILVB_METJA
ID ILVB_METJA Reviewed; 591 AA.
AC Q57725;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable 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=MJ0277;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98265.1; -; Genomic_DNA.
DR PIR; F64334; F64334.
DR RefSeq; WP_010869775.1; NC_000909.1.
DR AlphaFoldDB; Q57725; -.
DR SMR; Q57725; -.
DR STRING; 243232.MJ_0277; -.
DR EnsemblBacteria; AAB98265; AAB98265; MJ_0277.
DR GeneID; 1451132; -.
DR KEGG; mja:MJ_0277; -.
DR eggNOG; arCOG01998; Archaea.
DR HOGENOM; CLU_013748_1_3_2; -.
DR InParanoid; Q57725; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 7134at2157; -.
DR PhylomeDB; Q57725; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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..591
FT /note="Probable acetolactate synthase large subunit"
FT /id="PRO_0000090808"
FT REGION 396..476
FT /note="Thiamine pyrophosphate binding"
FT BINDING 47
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 258..279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 301..320
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"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 591 AA; 64493 MW; DB398C926D9B3A9D CRC64;
MKGAEAIIKA LEAEGVKIIF GYPGGAMLPF YDALYDSDLV HILTRHEQAA AHAADGFARA
SGEAGVCVST SGPGATNLVT GIATAYADSS PVIALTGQVP TKLIGNDAFQ EIDALGLFMP
ITKHNFQIKK PEEIPETFRA AFEIATTGRP GPVHIDLPKD VQDGEIDIEK YPIPAKVDLP
GYKPKTVGHP LQIKKAAKLI AESERPVILA GGGVIISGAS EELLRLAEFV KIPVCTTLMG
KGCFPEDHPL ALGMVGMHGT KAANYAVTEC DVLIAIGCRF SDRVTGDIRY FAPEAKIIHI
DIDPAEIGKN VRADIPIVGD AKNVLRDLLA ALIALEIKDK ETWLERIYEL KKLSIPMMDF
DDKPIKPQRF VKDLMEVLNE IDSKLKNTII TTDVGQNQMW MAHFFKTKMP RSFLASGGLG
TMGFGFPAAI GAKVAKPYAN VISITGDGGF LMNSQELATI SEYDIPVVIC IFDNRTLGMV
YQWQNLYYGQ RQSEVHLGES PDFVKLAESY GVKADRIISP DEIKEKLKEA ILSNEPYLLD
IVIDPAEALP MVPPGGRLTN IVQPIRVEPK IKKPQFDEIK KIRDMAAVKE F
