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Database: UniProt
Entry: P07342
LinkDB: P07342
Original site: P07342 
ID   ILVB_YEAST              Reviewed;         687 AA.
AC   P07342; D6VZT1;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   02-JUN-2021, entry version 223.
DE   RecName: Full=Acetolactate synthase catalytic subunit, mitochondrial;
DE            EC=2.2.1.6;
DE   AltName: Full=Acetohydroxy-acid synthase catalytic subunit;
DE            Short=AHAS;
DE            Short=ALS;
DE   Flags: Precursor;
GN   Name=ILV2; Synonyms=SMR1; OrderedLocusNames=YMR108W; ORFNames=YM9718.07;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989783; DOI=10.1093/nar/13.11.4011;
RA   Falco S.C., Dumas K.S., Livak K.J.;
RT   "Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate
RT   synthase.";
RL   Nucleic Acids Res. 13:4011-4027(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   RECONSTITUTION OF THE ACETOLACTATE SYNTHASE COMPLEX, AND ACTIVITY
RP   REGULATION.
RX   PubMed=10213630; DOI=10.1021/bi983013m;
RA   Pang S.S., Duggleby R.G.;
RT   "Expression, purification, characterization, and reconstitution of the
RT   large and small subunits of yeast acetohydroxyacid synthase.";
RL   Biochemistry 38:5222-5231(1999).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 58-687.
RX   PubMed=11902841; DOI=10.1006/jmbi.2001.5419;
RA   Pang S.S., Duggleby R.G., Guddat L.W.;
RT   "Crystal structure of yeast acetohydroxyacid synthase: a target for
RT   herbicidal inhibitors.";
RL   J. Mol. Biol. 317:249-262(2002).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-687 IN COMPLEX WITH FAD;
RP   HERBICIDE AND THIAMINE DIPHOSPHATE.
RX   PubMed=12496246; DOI=10.1074/jbc.m211648200;
RA   Pang S.S., Guddat L.W., Duggleby R.G.;
RT   "Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid
RT   synthase.";
RL   J. Biol. Chem. 278:7639-7644(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   -!- ACTIVITY REGULATION: The regulatory subunit ILV6 stimulates enzymatic
CC       activity seven- to tenfold and confers sensitivity to inhibition by
CC       valine and activation by ATP. {ECO:0000269|PubMed:10213630}.
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: Homodimer. The acetolactate synthase complex contains the
CC       catalytic regulatory subunit ILV2 and the regulatory small subunit
CC       ILV6. {ECO:0000269|PubMed:12496246}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
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.
CC   -!- MISCELLANEOUS: Present with 31900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; X02549; CAA26400.1; -; Genomic_DNA.
DR   EMBL; Z49702; CAA89744.1; -; Genomic_DNA.
DR   EMBL; AY692995; AAT93014.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10005.1; -; Genomic_DNA.
DR   PIR; A23808; YCBYI.
DR   RefSeq; NP_013826.1; NM_001182608.1.
DR   PDB; 1JSC; X-ray; 2.60 A; A/B=58-687.
DR   PDB; 1N0H; X-ray; 2.80 A; A/B=58-687.
DR   PDB; 1T9A; X-ray; 2.59 A; A/B=58-687.
DR   PDB; 1T9B; X-ray; 2.20 A; A/B=58-687.
DR   PDB; 1T9C; X-ray; 2.34 A; A/B=58-687.
DR   PDB; 1T9D; X-ray; 2.30 A; A/B/C/D=58-687.
DR   PDB; 5FEM; X-ray; 2.17 A; A/B=58-687.
DR   PDB; 5IMS; X-ray; 1.98 A; A/B=58-687.
DR   PDB; 5WKC; X-ray; 2.33 A; A/B/D/E=58-687.
DR   PDB; 6BD3; X-ray; 2.28 A; A/B=58-687.
DR   PDB; 6BD9; X-ray; 1.98 A; A/B=58-687.
DR   PDB; 6U9D; X-ray; 3.19 A; A/B/E/F/I/J/M/N/Q/R/U/V=58-687.
DR   PDBsum; 1JSC; -.
DR   PDBsum; 1N0H; -.
DR   PDBsum; 1T9A; -.
DR   PDBsum; 1T9B; -.
DR   PDBsum; 1T9C; -.
DR   PDBsum; 1T9D; -.
DR   PDBsum; 5FEM; -.
DR   PDBsum; 5IMS; -.
DR   PDBsum; 5WKC; -.
DR   PDBsum; 6BD3; -.
DR   PDBsum; 6BD9; -.
DR   PDBsum; 6U9D; -.
DR   SMR; P07342; -.
DR   BioGRID; 35284; 53.
DR   ComplexPortal; CPX-3034; Acetolactate synthase complex.
DR   DIP; DIP-1104N; -.
DR   IntAct; P07342; 73.
DR   MINT; P07342; -.
DR   STRING; 4932.YMR108W; -.
DR   BindingDB; P07342; -.
DR   ChEMBL; CHEMBL1075095; -.
DR   CarbonylDB; P07342; -.
DR   iPTMnet; P07342; -.
DR   MaxQB; P07342; -.
DR   PaxDb; P07342; -.
DR   PRIDE; P07342; -.
DR   EnsemblFungi; YMR108W_mRNA; YMR108W; YMR108W.
DR   GeneID; 855135; -.
DR   KEGG; sce:YMR108W; -.
DR   SGD; S000004714; ILV2.
DR   VEuPathDB; FungiDB:YMR108W; -.
DR   eggNOG; KOG4166; Eukaryota.
DR   GeneTree; ENSGT00940000176650; -.
DR   HOGENOM; CLU_013748_1_2_1; -.
DR   InParanoid; P07342; -.
DR   OMA; MRSYNPV; -.
DR   BRENDA; 2.2.1.6; 984.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   EvolutionaryTrace; P07342; -.
DR   PRO; PR:P07342; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P07342; protein.
DR   GO; GO:0005948; C:acetolactate synthase complex; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0003984; F:acetolactate synthase activity; IDA:SGD.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:SGD.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR   CDD; cd02015; TPP_AHAS; 1.
DR   DisProt; DP00398; -.
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; IPR011766; TPP_enzyme-bd_C.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Magnesium; Metal-binding;
KW   Mitochondrion; Reference proteome; Thiamine pyrophosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..90
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           91..687
FT                   /note="Acetolactate synthase catalytic subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000035664"
FT   NP_BIND         355..376
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:12496246"
FT   NP_BIND         407..426
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:12496246"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..579
FT                   /note="Thiamine pyrophosphate binding"
FT   METAL           550
FT                   /note="Magnesium"
FT   METAL           577
FT                   /note="Magnesium"
FT   METAL           579
FT                   /note="Magnesium; via carbonyl oxygen"
FT   BINDING         139
FT                   /note="Thiamine pyrophosphate"
FT   BINDING         241
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:12496246"
FT   TURN            88..91
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           94..104
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           119..127
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           139..153
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           171..180
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          184..190
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   TURN            196..199
FT                   /evidence="ECO:0007829|PDB:5IMS"
FT   HELIX           206..209
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          214..219
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           226..237
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           251..255
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           264..267
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           281..298
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          300..306
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           308..312
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           316..327
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           335..337
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          348..351
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           358..366
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          368..374
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           379..382
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           385..387
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           390..397
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          402..408
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          420..425
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           427..435
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           445..457
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          467..469
FT                   /evidence="ECO:0007829|PDB:1JSC"
FT   HELIX           473..486
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          491..495
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           499..507
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          512..514
FT                   /evidence="ECO:0007829|PDB:5IMS"
FT   HELIX           528..538
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          542..549
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           550..556
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           557..559
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           560..566
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          571..576
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          582..587
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          589..591
FT                   /evidence="ECO:0007829|PDB:5IMS"
FT   STRAND          594..596
FT                   /evidence="ECO:0007829|PDB:5IMS"
FT   HELIX           605..612
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          614..619
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           622..624
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   HELIX           625..634
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          639..645
FT                   /evidence="ECO:0007829|PDB:6BD9"
FT   STRAND          652..654
FT                   /evidence="ECO:0007829|PDB:5FEM"
FT   HELIX           669..682
FT                   /evidence="ECO:0007829|PDB:5FEM"
FT   TURN            683..685
FT                   /evidence="ECO:0007829|PDB:5FEM"
SQ   SEQUENCE   687 AA;  74937 MW;  B03C4D0F38AA1362 CRC64;
     MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP ASKRPEPAPS
     FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE MMSRQNVDTV FGYPGGAILP
     VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA RASGKPGVVL VTSGPGATNV VTPMADAFAD
     GIPMVVFTGQ VPTSAIGTDA FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG
     RPGPVLVDLP KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK
     KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD MLGMHGCATA
     NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR GGIIHFEVSP KNINKVVQTQ
     IAVEGDATTN LGKMMSKIFP VKERSEWFAQ INKWKKEYPY AYMEETPGSK IKPQTVIKKL
     SKVANDTGRH VIVTTGVGQH QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP
     ESLVIDIDGD ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ
     LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP VLPMVAGGSG
     LDEFINFDPE VERQQTELRH KRTGGKH
//
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