ILVB_ARATH
ID ILVB_ARATH Reviewed; 670 AA.
AC P17597; A0A174; Q5FV34; Q8L7Y7; Q94B64;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Acetolactate synthase, chloroplastic;
DE Short=AtALS;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase;
DE AltName: Full=Protein CHLORSULFURON RESISTANT 1;
DE Flags: Precursor;
GN Name=ALS; Synonyms=AHAS, CSR1, TZP5; OrderedLocusNames=At3g48560;
GN ORFNames=T8P19.70;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=16665813; DOI=10.1104/pp.85.4.1110;
RA Mazur B.J., Chui C.F., Smith J.K.;
RT "Isolation and characterization of plant genes coding for acetolactate
RT synthase, the target enzyme for two classes of herbicides.";
RL Plant Physiol. 85:1110-1117(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-653, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=2336405; DOI=10.1093/nar/18.8.2188;
RA Sathasivan K., Haughn G.W., Murai N.;
RT "Nucleotide sequence of a mutant acetolactate synthase gene from an
RT imidazolinone-resistant Arabidopsis thaliana var. Columbia.";
RL Nucleic Acids Res. 18:2188-2188(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Jander G., Baerson S.R., Hudak J.A., Gonzalez K.A., Gruys K.J., Last R.L.;
RT "Saturation mutagenesis in Arabidopsis to determine frequency of herbicide
RT resistance.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang L., Xiang W., Wang X., Wang X., Zhang J., Xi D., Gao A.;
RT "Cloning of Arabidopsis thaliana acetolactate synthase catalytic subunit.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND MUTAGENESIS OF PRO-197.
RC STRAIN=cv. Columbia;
RA Haughn G.W., Smith J.K., Mazur B.J., Somerville C.;
RT "Transformation with a mutant Arabidopsis acetolactate synthase gene
RT renders tobacco resistant to sulfonylurea herbicides.";
RL Mol. Gen. Genet. 211:266-271(1988).
RN [10]
RP FUNCTION.
RX PubMed=16667374; DOI=10.1104/pp.92.4.1081;
RA Haughn G.W., Somerville C.R.;
RT "A mutation causing imidazolinone resistance maps to the csr1 locus of
RT Arabidopsis thaliana.";
RL Plant Physiol. 92:1081-1085(1990).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF SER-653.
RC STRAIN=cv. Columbia;
RX PubMed=16668488; DOI=10.1104/pp.97.3.1044;
RA Sathasivan K., Haughn G.W., Murai N.;
RT "Molecular basis of imidazolinone herbicide resistance in Arabidopsis
RT thaliana var Columbia.";
RL Plant Physiol. 97:1044-1050(1991).
RN [12]
RP 3D-STRUCTURE MODELING, FUNCTION, AND MUTAGENESIS OF MET-124 AND ARG-199.
RX PubMed=8913312; DOI=10.1006/jmbi.1996.0580;
RA Ott K.H., Kwagh J.G., Stockton G.W., Sidorov V., Kakefuda G.;
RT "Rational molecular design and genetic engineering of herbicide resistant
RT crops by structure modeling and site-directed mutagenesis of
RT acetohydroxyacid synthase.";
RL J. Mol. Biol. 263:359-368(1996).
RN [13]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=9355748; DOI=10.1042/bj3270161;
RA Chang A.K., Duggleby R.G.;
RT "Expression, purification and characterization of Arabidopsis thaliana
RT acetohydroxyacid synthase.";
RL Biochem. J. 327:161-169(1997).
RN [14]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF
RP ALA-122; TRP-574 AND SER-653.
RX PubMed=9677339; DOI=10.1042/bj3330765;
RA Chang A.K., Duggleby R.G.;
RT "Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid
RT synthase: characterization of the catalytic properties and sensitivity to
RT inhibitors of four defined mutants.";
RL Biochem. J. 333:765-777(1998).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF SER-653.
RX PubMed=10386618; DOI=10.1016/s0014-5793(99)00668-7;
RA Lee Y.T., Chang A.K., Duggleby R.G.;
RT "Effect of mutagenesis at serine 653 of Arabidopsis thaliana
RT acetohydroxyacid synthase on the sensitivity to imidazolinone and
RT sulfonylurea herbicides.";
RL FEBS Lett. 452:341-345(1999).
RN [16]
RP 3D-STRUCTURE MODELING, AND ACTIVITY REGULATION.
RX PubMed=19342247; DOI=10.1016/j.bmc.2009.03.018;
RA Chen C.N., Lv L.L., Ji F.Q., Chen Q., Xu H., Niu C.W., Xi Z., Yang G.F.;
RT "Design and synthesis of N-2,6-difluorophenyl-5-methoxyl-1,2,4-
RT triazolo[1,5-a]-pyrimidine-2-sulfonamide as acetohydroxyacid synthase
RT inhibitor.";
RL Bioorg. Med. Chem. 17:3011-3017(2009).
RN [17]
RP 3D-STRUCTURE MODELING, AND ACTIVITY REGULATION.
RX PubMed=20598554; DOI=10.1016/j.bmc.2010.06.015;
RA Chen C.N., Chen Q., Liu Y.C., Zhu X.L., Niu C.W., Xi Z., Yang G.F.;
RT "Syntheses and herbicidal activity of new triazolopyrimidine-2-sulfonamides
RT as acetohydroxyacid synthase inhibitor.";
RL Bioorg. Med. Chem. 18:4897-4904(2010).
RN [18]
RP 3D-STRUCTURE MODELING, AND ACTIVITY REGULATION.
RX PubMed=21838297; DOI=10.1021/jf2021607;
RA Wang J., Tan H., Li Y., Ma Y., Li Z., Guddat L.W.;
RT "Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition,
RT herbicidal activity, and computational studies of isatin derivatives.";
RL J. Agric. Food Chem. 59:9892-9900(2011).
RN [19]
RP 3D-STRUCTURE MODELING, AND ACTIVITY REGULATION.
RX PubMed=22905906; DOI=10.1021/jf302206x;
RA Shang J., Wang W.M., Li Y.H., Song H.B., Li Z.M., Wang J.G.;
RT "Synthesis, crystal structure, in vitro acetohydroxyacid synthase
RT inhibition, in vivo herbicidal activity, and 3D-QSAR of new asymmetric aryl
RT disulfides.";
RL J. Agric. Food Chem. 60:8286-8293(2012).
RN [20]
RP DISRUPTION PHENOTYPE.
RX PubMed=22430369; DOI=10.1007/s11248-012-9597-z;
RA Schnell J., Labbe H., Kovinich N., Manabe Y., Miki B.;
RT "Comparability of imazapyr-resistant Arabidopsis created by transgenesis
RT and mutagenesis.";
RL Transgenic Res. 21:1255-1264(2012).
RN [21] {ECO:0007744|PDB:1YBH, ECO:0007744|PDB:1YHY, ECO:0007744|PDB:1YHZ, ECO:0007744|PDB:1YI0, ECO:0007744|PDB:1YI1, ECO:0007744|PDB:1Z8N}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 86-667 IN COMPLEX WITH FAD;
RP MAGNESIUM; THIAMINE PYROPHOSPHATE AND HERBICIDES, OXIDATION AT CYS-340, AND
RP SUBUNIT.
RX PubMed=16407096; DOI=10.1073/pnas.0508701103;
RA McCourt J.A., Pang S.S., King-Scott J., Guddat L.W., Duggleby R.G.;
RT "Herbicide-binding sites revealed in the structure of plant
RT acetohydroxyacid synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:569-573(2006).
RN [22] {ECO:0007744|PDB:3E9Y, ECO:0007744|PDB:3EA4}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 87-670 IN COMPLEX WITH MAGNESIUM
RP AND SULFONYLUREA HERBICIDES, AND OXIDATION AT CYS-340.
RX PubMed=19187232; DOI=10.1111/j.1742-4658.2009.06863.x;
RA Wang J.G., Lee P.K., Dong Y.H., Pang S.S., Duggleby R.G., Li Z.M.,
RA Guddat L.W.;
RT "Crystal structures of two novel sulfonylurea herbicides in complex with
RT Arabidopsis thaliana acetohydroxyacid synthase.";
RL FEBS J. 276:1282-1290(2009).
CC -!- FUNCTION: Catalyzes the formation of acetolactate from pyruvate, the
CC first step in valine and isoleucine biosynthesis.
CC {ECO:0000269|PubMed:10386618, ECO:0000269|PubMed:16665813,
CC ECO:0000269|PubMed:16667374, ECO:0000269|PubMed:16668488,
CC ECO:0000269|PubMed:2336405, ECO:0000269|PubMed:8913312,
CC ECO:0000269|PubMed:9355748, ECO:0000269|PubMed:9677339,
CC ECO:0000269|Ref.9}.
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;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Note=Binds 1 thiamine pyrophosphate per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by asymmetric aryl disulfides,
CC triazolopyrimidine sulfonanilide compounds, isatin derivatives, and
CC sulfonylurea and imidazolinone herbicides. Insensitive to feed-back
CC inhibition by branched-chain amino acids. {ECO:0000269|PubMed:19342247,
CC ECO:0000269|PubMed:20598554, ECO:0000269|PubMed:21838297,
CC ECO:0000269|PubMed:22905906, ECO:0000269|PubMed:9355748}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:9355748,
CC ECO:0000269|PubMed:9677339};
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 or homotetramer. The acetolactate synthase complex
CC contains both large catalytic subunits and small regulatory subunits.
CC {ECO:0000269|PubMed:16407096, ECO:0000269|PubMed:19187232,
CC ECO:0000269|PubMed:9355748}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:22430369}.
CC -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC sulfonylurea resistant plants.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; X51514; CAA35887.1; -; Genomic_DNA.
DR EMBL; AL133315; CAB62345.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78430.1; -; Genomic_DNA.
DR EMBL; AY124092; AAM92569.1; -; Genomic_DNA.
DR EMBL; AY042819; AAK68759.1; -; mRNA.
DR EMBL; BT020540; AAW70386.1; -; mRNA.
DR EMBL; DQ991161; ABJ80681.1; -; mRNA.
DR PIR; S09502; YCMU.
DR RefSeq; NP_190425.1; NM_114714.3.
DR PDB; 1YBH; X-ray; 2.50 A; A=86-667.
DR PDB; 1YHY; X-ray; 2.70 A; A=86-667.
DR PDB; 1YHZ; X-ray; 2.70 A; A=86-667.
DR PDB; 1YI0; X-ray; 2.70 A; A=86-667.
DR PDB; 1YI1; X-ray; 2.90 A; A=86-667.
DR PDB; 1Z8N; X-ray; 2.80 A; A=86-667.
DR PDB; 3E9Y; X-ray; 3.00 A; A=87-670.
DR PDB; 3EA4; X-ray; 2.80 A; A=87-670.
DR PDB; 5K2O; X-ray; 2.87 A; A=86-667.
DR PDB; 5K3S; X-ray; 2.87 A; A=86-667.
DR PDB; 5K6Q; X-ray; 2.95 A; A=86-667.
DR PDB; 5K6R; X-ray; 2.73 A; A=86-667.
DR PDB; 5K6T; X-ray; 2.76 A; A=86-667.
DR PDB; 5WJ1; X-ray; 2.52 A; A=86-667.
DR PDB; 6U9H; EM; 3.80 A; A/B/H/I/L/M/P/Q=86-670.
DR PDB; 6VZ8; EM; 3.45 A; D/E/H/I/L/M/P/Q=86-670.
DR PDBsum; 1YBH; -.
DR PDBsum; 1YHY; -.
DR PDBsum; 1YHZ; -.
DR PDBsum; 1YI0; -.
DR PDBsum; 1YI1; -.
DR PDBsum; 1Z8N; -.
DR PDBsum; 3E9Y; -.
DR PDBsum; 3EA4; -.
DR PDBsum; 5K2O; -.
DR PDBsum; 5K3S; -.
DR PDBsum; 5K6Q; -.
DR PDBsum; 5K6R; -.
DR PDBsum; 5K6T; -.
DR PDBsum; 5WJ1; -.
DR PDBsum; 6U9H; -.
DR PDBsum; 6VZ8; -.
DR AlphaFoldDB; P17597; -.
DR SMR; P17597; -.
DR BioGRID; 9334; 1.
DR DIP; DIP-61092N; -.
DR STRING; 3702.AT3G48560.1; -.
DR BindingDB; P17597; -.
DR ChEMBL; CHEMBL4263; -.
DR MetOSite; P17597; -.
DR PaxDb; P17597; -.
DR PRIDE; P17597; -.
DR ProteomicsDB; 228865; -.
DR EnsemblPlants; AT3G48560.1; AT3G48560.1; AT3G48560.
DR GeneID; 824015; -.
DR Gramene; AT3G48560.1; AT3G48560.1; AT3G48560.
DR KEGG; ath:AT3G48560; -.
DR Araport; AT3G48560; -.
DR TAIR; locus:2114525; AT3G48560.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_1_2_1; -.
DR InParanoid; P17597; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 1132247at2759; -.
DR PhylomeDB; P17597; -.
DR BioCyc; ARA:AT3G48560-MON; -.
DR BRENDA; 2.2.1.6; 399.
DR SABIO-RK; P17597; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR EvolutionaryTrace; P17597; -.
DR PRO; PR:P17597; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P17597; baseline and differential.
DR Genevisible; P17597; AT.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003984; F:acetolactate synthase activity; IDA:TAIR.
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:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IDA:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast; Coiled coil; FAD;
KW Flavoprotein; Genetically modified food; Herbicide resistance; Magnesium;
KW Metal-binding; Oxidation; Plastid; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..670
FT /note="Acetolactate synthase, chloroplastic"
FT /id="PRO_0000035655"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..446
FT /evidence="ECO:0000255"
FT COMPBIAS 1..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 207
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 220
FT /ligand="(R)-imazaquin"
FT /ligand_id="ChEBI:CHEBI:147373"
FT /ligand_note="inhibitor; imidazolinone herbicide"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0007744|PDB:1Z8N"
FT BINDING 246
FT /ligand="(R)-imazaquin"
FT /ligand_id="ChEBI:CHEBI:147373"
FT /ligand_note="inhibitor; imidazolinone herbicide"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0007744|PDB:1Z8N"
FT BINDING 246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 256
FT /ligand="chlorimuron-ethyl"
FT /ligand_id="ChEBI:CHEBI:188144"
FT /ligand_note="inhibitor; sulfonylurea herbicide"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0007744|PDB:1YBH"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 331..332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 349..352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 371..375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 376..377
FT /ligand="chlorimuron-ethyl"
FT /ligand_id="ChEBI:CHEBI:188144"
FT /ligand_note="inhibitor; sulfonylurea herbicide"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0007744|PDB:1YBH"
FT BINDING 395..396
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 414..415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 487..488
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 508..509
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16407096"
FT BINDING 511..513
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 538..540
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232"
FT BINDING 565..570
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 565
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232"
FT BINDING 574
FT /ligand="chlorimuron-ethyl"
FT /ligand_id="ChEBI:CHEBI:188144"
FT /ligand_note="inhibitor; sulfonylurea herbicide"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0007744|PDB:1YBH"
FT BINDING 653
FT /ligand="chlorimuron-ethyl"
FT /ligand_id="ChEBI:CHEBI:188144"
FT /ligand_note="inhibitor; sulfonylurea herbicide"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0007744|PDB:1YBH"
FT MOD_RES 340
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232"
FT MUTAGEN 122
FT /note="A->V: Reduced catalytic activity. Resistant to
FT imidazolinone herbicides but not to sulfonylurea
FT herbicides."
FT /evidence="ECO:0000269|PubMed:9677339"
FT MUTAGEN 124
FT /note="M->E: Reduced catalytic activity. Resistant to
FT imidazolinone herbicides and reduced sensitivity to
FT sulfonylurea herbicides."
FT /evidence="ECO:0000269|PubMed:8913312"
FT MUTAGEN 124
FT /note="M->I: No effect on catalytic activity. Increased
FT resistance to imidazolinone herbicides."
FT /evidence="ECO:0000269|PubMed:8913312"
FT MUTAGEN 197
FT /note="P->S: In csr1-1/GH50; resistant to sulfonylurea but
FT not to imidazolinone herbicides."
FT /evidence="ECO:0000269|Ref.9"
FT MUTAGEN 199
FT /note="R->A,E: No effect on catalytic activity. Resistant
FT to imidazolinone herbicides but not to sulfonylurea
FT herbicides."
FT /evidence="ECO:0000269|PubMed:8913312"
FT MUTAGEN 574
FT /note="W->L: Increased catalytic activity. Resistant to
FT imidazolinone and sulfonylurea herbicides."
FT /evidence="ECO:0000269|PubMed:9677339"
FT MUTAGEN 574
FT /note="W->S: Slightly decreased catalytic activity.
FT Resistant to imidazolinone and sulfonylurea herbicides."
FT /evidence="ECO:0000269|PubMed:9677339"
FT MUTAGEN 653
FT /note="S->A: No effect on catalytic activity or sensitivity
FT to herbicides."
FT /evidence="ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488, ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339"
FT MUTAGEN 653
FT /note="S->F: No effect on catalytic activity. Resistant to
FT imidazolinone herbicides and also slightly sulfonylurea-
FT resistant."
FT /evidence="ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488, ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339"
FT MUTAGEN 653
FT /note="S->N: In csr1-2/GH90; no effect on catalytic
FT activity. Resistant to imidazolinone but not to
FT sulfonylurea herbicides."
FT /evidence="ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488, ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339"
FT MUTAGEN 653
FT /note="S->T: No effect on catalytic activity. Resistant to
FT imidazolinone herbicides but not to sulfonylurea
FT herbicides."
FT /evidence="ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488, ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339"
FT CONFLICT 104
FT /note="V -> A (in Ref. 8; ABJ80681)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="P -> S (in Ref. 8; ABJ80681)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="E -> G (in Ref. 8; ABJ80681)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Y -> H (in Ref. 8; ABJ80681)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="N -> Q (in Ref. 5; AAM92569)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="V -> I (in Ref. 5; AAM92569)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="E -> Q (in Ref. 6; AAK68759)"
FT /evidence="ECO:0000305"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:1YBH"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1YBH"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1YBH"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1YHZ"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1YBH"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:1YBH"
FT TURN 398..402
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 464..475
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 487..494
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 532..537
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 538..543
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 547..553
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 558..564
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 569..578
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:1YBH"
FT HELIX 618..630
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 635..640
FT /evidence="ECO:0007829|PDB:1YBH"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:5WJ1"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:1YBH"
SQ SEQUENCE 670 AA; 72585 MW; DA697A8DD155F160 CRC64;
MAAATTTTTT SSSISFSTKP SPSSSKSPLP ISRFSLPFSL NPNKSSSSSR RRGIKSSSPS
SISAVLNTTT NVTTTPSPTK PTKPETFISR FAPDQPRKGA DILVEALERQ GVETVFAYPG
GASMEIHQAL TRSSSIRNVL PRHEQGGVFA AEGYARSSGK PGICIATSGP GATNLVSGLA
DALLDSVPLV AITGQVPRRM IGTDAFQETP IVEVTRSITK HNYLVMDVED IPRIIEEAFF
LATSGRPGPV LVDVPKDIQQ QLAIPNWEQA MRLPGYMSRM PKPPEDSHLE QIVRLISESK
KPVLYVGGGC LNSSDELGRF VELTGIPVAS TLMGLGSYPC DDELSLHMLG MHGTVYANYA
VEHSDLLLAF GVRFDDRVTG KLEAFASRAK IVHIDIDSAE IGKNKTPHVS VCGDVKLALQ
GMNKVLENRA EELKLDFGVW RNELNVQKQK FPLSFKTFGE AIPPQYAIKV LDELTDGKAI
ISTGVGQHQM WAAQFYNYKK PRQWLSSGGL GAMGFGLPAA IGASVANPDA IVVDIDGDGS
FIMNVQELAT IRVENLPVKV LLLNNQHLGM VMQWEDRFYK ANRAHTFLGD PAQEDEIFPN
MLLFAAACGI PAARVTKKAD LREAIQTMLD TPGPYLLDVI CPHQEHVLPM IPSGGTFNDV
ITEGDGRIKY
