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 12-APR-2017, entry version 163.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC 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
RP 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.,
RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA 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.,
RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA 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
RT thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Portal (Araport);
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA Last R.L.;
RT "Saturation mutagenesis in Arabidopsis to determine frequency of
RT herbicide 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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT 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
RP 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
RT resistant 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, ENZYME REGULATION,
RP AND 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
RT to 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 ENZYME 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.,
RA 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 ENZYME 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-
RT sulfonamides as acetohydroxyacid synthase inhibitor.";
RL Bioorg. Med. Chem. 18:4897-4904(2010).
RN [18]
RP 3D-STRUCTURE MODELING, AND ENZYME 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)
RT inhibition, herbicidal activity, and computational studies of isatin
RT derivatives.";
RL J. Agric. Food Chem. 59:9892-9900(2011).
RN [19]
RP 3D-STRUCTURE MODELING, AND ENZYME 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
RT aryl 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
RT transgenesis and mutagenesis.";
RL Transgenic Res. 21:1255-1264(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 86-667 IN COMPLEX WITH FAD;
RP MAGNESIUM; THIAMINE PYROPHOSPHATE AND HERBICIDES, OXIDATION AT
RP CYS-340, AND 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]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 87-670 IN COMPLEX WITH
RP MAGNESIUM 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
RT with Arabidopsis thaliana acetohydroxyacid synthase.";
RL FEBS J. 276:1282-1290(2009).
CC -!- FUNCTION: Catalyzes the formation of acetolactate from pyruvate,
CC the 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: 2 pyruvate = 2-acetolactate + CO(2).
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 -!- ENZYME REGULATION: Inhibited by asymmetric aryl disulfides,
CC triazolopyrimidine sulfonanilide compounds, isatin derivatives,
CC and sulfonylurea and imidazolinone herbicides. Insensitive to
CC feed-back inhibition by branched-chain amino acids.
CC {ECO:0000269|PubMed:19342247, ECO:0000269|PubMed:20598554,
CC ECO:0000269|PubMed:21838297, ECO:0000269|PubMed:22905906,
CC 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
CC from pyruvate: step 1/4.
CC -!- SUBUNIT: Homodimer or homotetramer. The acetolactate synthase
CC complex contains both large catalytic subunits and small
CC regulatory subunits. {ECO:0000269|PubMed:16407096,
CC ECO:0000269|PubMed:19187232, 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 UniGene; At.22295; -.
DR UniGene; At.72000; -.
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; 5K6R; X-ray; 2.73 A; A=86-667.
DR PDB; 5K6T; X-ray; 2.76 A; A=86-667.
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; 5K6R; -.
DR PDBsum; 5K6T; -.
DR ProteinModelPortal; P17597; -.
DR SMR; P17597; -.
DR BioGrid; 9334; 1.
DR DIP; DIP-61092N; -.
DR STRING; 3702.AT3G48560.1; -.
DR BindingDB; P17597; -.
DR ChEMBL; CHEMBL4263; -.
DR PaxDb; P17597; -.
DR PRIDE; P17597; -.
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 eggNOG; COG0028; LUCA.
DR HOGENOM; HOG000258448; -.
DR InParanoid; P17597; -.
DR KO; K01652; -.
DR OMA; HSWVVRD; -.
DR OrthoDB; EOG0936048A; -.
DR PhylomeDB; P17597; -.
DR BioCyc; ARA:AT3G48560-MONOMER; -.
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 Genevisible; P17597; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0003984; F:acetolactate synthase activity; IDA:TAIR.
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:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1220; -; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
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; Chloroplast; Coiled coil;
KW Complete proteome; FAD; Flavoprotein; Genetically modified food;
KW Herbicide resistance; Magnesium; Metal-binding; Oxidation; Plastid;
KW Reference proteome; Thiamine pyrophosphate; Transferase;
KW Transit peptide.
FT TRANSIT 1 55 Chloroplast. {ECO:0000255}.
FT CHAIN 56 670 Acetolactate synthase, chloroplastic.
FT /FTId=PRO_0000035655.
FT NP_BIND 331 332 FAD. {ECO:0000269|PubMed:16407096}.
FT NP_BIND 349 352 FAD. {ECO:0000269|PubMed:16407096}.
FT NP_BIND 371 375 FAD. {ECO:0000269|PubMed:16407096}.
FT NP_BIND 395 396 FAD. {ECO:0000269|PubMed:16407096}.
FT NP_BIND 414 415 FAD. {ECO:0000269|PubMed:16407096}.
FT NP_BIND 508 509 FAD. {ECO:0000269|PubMed:16407096}.
FT REGION 376 377 Sulfonylurea herbicides binding.
FT REGION 487 488 Thiamine pyrophosphate binding.
FT REGION 511 513 Thiamine pyrophosphate binding.
FT REGION 538 540 Thiamine pyrophosphate binding.
FT REGION 565 570 Thiamine pyrophosphate binding.
FT COILED 414 446 {ECO:0000255}.
FT METAL 538 538 Magnesium. {ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232}.
FT METAL 565 565 Magnesium. {ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232}.
FT METAL 567 567 Magnesium; via carbonyl oxygen.
FT {ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232}.
FT BINDING 144 144 Thiamine pyrophosphate.
FT {ECO:0000269|PubMed:16407096}.
FT BINDING 207 207 Thiamine pyrophosphate.
FT {ECO:0000269|PubMed:16407096}.
FT BINDING 220 220 Imidazolinone herbicides.
FT BINDING 246 246 FAD. {ECO:0000269|PubMed:16407096}.
FT BINDING 246 246 Imidazolinone herbicides; via amide
FT nitrogen.
FT BINDING 256 256 Sulfonylurea herbicides.
FT {ECO:0000269|PubMed:19187232}.
FT BINDING 308 308 FAD; via amide nitrogen.
FT {ECO:0000269|PubMed:16407096}.
FT BINDING 377 377 Imidazolinone and sulfonylurea
FT herbicides.
FT BINDING 574 574 Sulfonylurea herbicides.
FT {ECO:0000269|PubMed:19187232}.
FT BINDING 653 653 Sulfonylurea herbicides.
FT {ECO:0000269|PubMed:19187232}.
FT MOD_RES 340 340 Cysteine sulfinic acid (-SO2H).
FT {ECO:0000269|PubMed:16407096,
FT ECO:0000269|PubMed:19187232}.
FT MUTAGEN 122 122 A->V: Reduced catalytic activity.
FT Resistant to imidazolinone herbicides but
FT not to sulfonylurea herbicides.
FT {ECO:0000269|PubMed:9677339}.
FT MUTAGEN 124 124 M->E: Reduced catalytic activity.
FT Resistant to imidazolinone herbicides and
FT reduced sensitivity to sulfonylurea
FT herbicides. {ECO:0000269|PubMed:8913312}.
FT MUTAGEN 124 124 M->I: No effect on catalytic activity.
FT Increased resistance to imidazolinone
FT herbicides. {ECO:0000269|PubMed:8913312}.
FT MUTAGEN 197 197 P->S: In csr1-1/GH50; resistant to
FT sulfonylurea but not to imidazolinone
FT herbicides. {ECO:0000269|Ref.9}.
FT MUTAGEN 199 199 R->A,E: No effect on catalytic activity.
FT Resistant to imidazolinone herbicides but
FT not to sulfonylurea herbicides.
FT {ECO:0000269|PubMed:8913312}.
FT MUTAGEN 574 574 W->L: Increased catalytic activity.
FT Resistant to imidazolinone and
FT sulfonylurea herbicides.
FT {ECO:0000269|PubMed:9677339}.
FT MUTAGEN 574 574 W->S: Slightly decreased catalytic
FT activity. Resistant to imidazolinone and
FT sulfonylurea herbicides.
FT {ECO:0000269|PubMed:9677339}.
FT MUTAGEN 653 653 S->A: No effect on catalytic activity or
FT sensitivity to herbicides.
FT {ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488,
FT ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339}.
FT MUTAGEN 653 653 S->F: No effect on catalytic activity.
FT Resistant to imidazolinone herbicides and
FT also slightly sulfonylurea-resistant.
FT {ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488,
FT ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339}.
FT MUTAGEN 653 653 S->N: In csr1-2/GH90; no effect on
FT catalytic activity. Resistant to
FT imidazolinone but not to sulfonylurea
FT herbicides. {ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488,
FT ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339}.
FT MUTAGEN 653 653 S->T: No effect on catalytic activity.
FT Resistant to imidazolinone herbicides but
FT not to sulfonylurea herbicides.
FT {ECO:0000269|PubMed:10386618,
FT ECO:0000269|PubMed:16668488,
FT ECO:0000269|PubMed:2336405,
FT ECO:0000269|PubMed:9677339}.
FT CONFLICT 104 104 V -> A (in Ref. 8; ABJ80681).
FT {ECO:0000305}.
FT CONFLICT 161 161 P -> S (in Ref. 8; ABJ80681).
FT {ECO:0000305}.
FT CONFLICT 208 208 E -> G (in Ref. 8; ABJ80681).
FT {ECO:0000305}.
FT CONFLICT 466 466 Y -> H (in Ref. 8; ABJ80681).
FT {ECO:0000305}.
FT CONFLICT 555 555 N -> Q (in Ref. 5; AAM92569).
FT {ECO:0000305}.
FT CONFLICT 560 560 V -> I (in Ref. 5; AAM92569).
FT {ECO:0000305}.
FT CONFLICT 575 575 E -> Q (in Ref. 6; AAK68759).
FT {ECO:0000305}.
FT HELIX 99 108 {ECO:0000244|PDB:1YBH}.
FT TURN 109 111 {ECO:0000244|PDB:1YBH}.
FT STRAND 114 117 {ECO:0000244|PDB:1YBH}.
FT HELIX 121 123 {ECO:0000244|PDB:1YBH}.
FT HELIX 124 132 {ECO:0000244|PDB:1YBH}.
FT HELIX 144 158 {ECO:0000244|PDB:1YBH}.
FT STRAND 162 166 {ECO:0000244|PDB:1YBH}.
FT HELIX 170 173 {ECO:0000244|PDB:1YBH}.
FT HELIX 176 185 {ECO:0000244|PDB:1YBH}.
FT STRAND 189 195 {ECO:0000244|PDB:1YBH}.
FT HELIX 198 200 {ECO:0000244|PDB:1YBH}.
FT TURN 201 204 {ECO:0000244|PDB:1YBH}.
FT HELIX 211 215 {ECO:0000244|PDB:1YBH}.
FT HELIX 216 218 {ECO:0000244|PDB:1YBH}.
FT STRAND 219 224 {ECO:0000244|PDB:1YBH}.
FT HELIX 228 230 {ECO:0000244|PDB:1YBH}.
FT HELIX 231 243 {ECO:0000244|PDB:1YBH}.
FT STRAND 244 246 {ECO:0000244|PDB:1YBH}.
FT STRAND 249 255 {ECO:0000244|PDB:1YBH}.
FT HELIX 256 260 {ECO:0000244|PDB:1YBH}.
FT HELIX 274 279 {ECO:0000244|PDB:1YBH}.
FT HELIX 286 298 {ECO:0000244|PDB:1YBH}.
FT STRAND 300 306 {ECO:0000244|PDB:1YBH}.
FT HELIX 308 310 {ECO:0000244|PDB:1YBH}.
FT HELIX 314 324 {ECO:0000244|PDB:1YBH}.
FT STRAND 328 330 {ECO:0000244|PDB:1YBH}.
FT TURN 332 336 {ECO:0000244|PDB:1YBH}.
FT STRAND 340 342 {ECO:0000244|PDB:1YHZ}.
FT STRAND 345 348 {ECO:0000244|PDB:1YBH}.
FT HELIX 355 363 {ECO:0000244|PDB:1YBH}.
FT STRAND 365 371 {ECO:0000244|PDB:1YBH}.
FT HELIX 376 379 {ECO:0000244|PDB:1YBH}.
FT HELIX 382 384 {ECO:0000244|PDB:1YBH}.
FT TURN 385 388 {ECO:0000244|PDB:1YBH}.
FT STRAND 389 396 {ECO:0000244|PDB:1YBH}.
FT TURN 398 402 {ECO:0000244|PDB:1YBH}.
FT STRAND 403 405 {ECO:0000244|PDB:1YBH}.
FT STRAND 408 413 {ECO:0000244|PDB:1YBH}.
FT HELIX 415 428 {ECO:0000244|PDB:1YBH}.
FT HELIX 430 433 {ECO:0000244|PDB:1YBH}.
FT HELIX 438 450 {ECO:0000244|PDB:1YBH}.
FT HELIX 464 475 {ECO:0000244|PDB:1YBH}.
FT STRAND 480 483 {ECO:0000244|PDB:1YBH}.
FT HELIX 487 494 {ECO:0000244|PDB:1YBH}.
FT STRAND 503 505 {ECO:0000244|PDB:1YBH}.
FT HELIX 516 526 {ECO:0000244|PDB:1YBH}.
FT STRAND 532 537 {ECO:0000244|PDB:1YBH}.
FT HELIX 538 543 {ECO:0000244|PDB:1YBH}.
FT HELIX 544 546 {ECO:0000244|PDB:1YBH}.
FT HELIX 547 553 {ECO:0000244|PDB:1YBH}.
FT STRAND 558 564 {ECO:0000244|PDB:1YBH}.
FT HELIX 569 578 {ECO:0000244|PDB:1YBH}.
FT HELIX 591 593 {ECO:0000244|PDB:1YBH}.
FT HELIX 601 607 {ECO:0000244|PDB:1YBH}.
FT STRAND 612 615 {ECO:0000244|PDB:1YBH}.
FT HELIX 618 630 {ECO:0000244|PDB:1YBH}.
FT STRAND 631 633 {ECO:0000244|PDB:1YBH}.
FT STRAND 635 640 {ECO:0000244|PDB:1YBH}.
FT STRAND 648 650 {ECO:0000244|PDB:1YHZ}.
FT HELIX 657 659 {ECO:0000244|PDB:1YBH}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 290 420 ipfam:TPP_enzyme_M [T]
FT MYHIT 484 639 ipfam:TPP_enzyme_C [T]
FT MYHIT 98 261 ipfam:TPP_enzyme_N [T]
FT MYHIT 521 540 ipat:TPP_ENZYMES [T]
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
//
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