ILVB_YEAST
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 03-AUG-2022, entry version 227.
DE RecName: Full=Acetolactate synthase catalytic subunit, mitochondrial {ECO:0000305};
DE EC=2.2.1.6 {ECO:0000269|PubMed:10213630};
DE AltName: Full=Acetohydroxy-acid synthase catalytic subunit {ECO:0000303|PubMed:10213630};
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, PATHWAY, AND SUBCELLULAR LOCATION.
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 -!- FUNCTION: Catalytic subunit of mitochondrial acetolactate synthase,
CC which catalyzes the first of a series of common steps in the
CC biosynthesis of the branched-chain amino acids. Catalyzes the
CC irreversible decarboxylation of pyruvate to a bound hydroxyethyl group
CC that then condenses with either a second pyruvate molecule to form 2-
CC acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-
CC hydroxybutyrate (AHB). The first product is the precursor for valine
CC and leucine biosynthesis, while the second leads to isoleucine.
CC {ECO:0000305|PubMed:10213630}.
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 Evidence={ECO:0000269|PubMed:10213630};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25250;
CC Evidence={ECO:0000269|PubMed:10213630};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + H(+) + pyruvate = (S)-2-ethyl-2-hydroxy-3-
CC oxobutanoate + CO2; Xref=Rhea:RHEA:27654, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:49256; EC=2.2.1.6;
CC Evidence={ECO:0000305|PubMed:10213630};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27655;
CC Evidence={ECO:0000305|PubMed:10213630};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.6 mM for pyruvate (catalytic subunit only)
CC {ECO:0000269|PubMed:10213630};
CC KM=18.1 mM for pyruvate (reconstituted into the acetolactate synthase
CC complex with the regulatory subunit) {ECO:0000269|PubMed:10213630};
CC pH dependence:
CC Optimum pH is 7-7.5. {ECO:0000269|PubMed:10213630};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000305|PubMed:10213630}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000305|PubMed:10213630}.
CC -!- SUBUNIT: Homodimer. The acetolactate synthase complex contains the
CC catalytic subunit ILV2 and the regulatory small subunit ILV6.
CC {ECO:0000269|PubMed:10213630}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10213630}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P07342; -.
DR SMR; P07342; -.
DR BioGRID; 35284; 79.
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; CFGTSGP; -.
DR BioCyc; YEAST:MON3O-29; -.
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; 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 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 REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..579
FT /note="Thiamine pyrophosphate binding"
FT BINDING 139
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12496246"
FT BINDING 355..376
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12496246"
FT BINDING 407..426
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12496246"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 577
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 579
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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
