ILV5_ARATH
ID ILV5_ARATH Reviewed; 591 AA.
AC Q05758; Q42559;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ketol-acid reductoisomerase, chloroplastic;
DE EC=1.1.1.86;
DE AltName: Full=Acetohydroxy-acid reductoisomerase;
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE Flags: Precursor;
GN OrderedLocusNames=At3g58610; ORFNames=F14P22.200;
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 [MRNA].
RX PubMed=8448371; DOI=10.1007/bf00014556;
RA Curien G., Dumas R., Douce R.;
RT "Nucleotide sequence and characterization of a cDNA encoding the
RT acetohydroxy acid isomeroreductase from Arabidopsis thaliana.";
RL Plant Mol. Biol. 21:717-722(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8379936; DOI=10.1042/bj2940821;
RA Dumas R., Curien G., Derose R.T., Douce R.;
RT "Branched-chain-amino-acid biosynthesis in plants: molecular cloning and
RT characterization of the gene encoding acetohydroxy acid isomeroreductase
RT (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress).";
RL Biochem. J. 294:821-828(1993).
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 [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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-53, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58476; EC=1.1.1.86;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {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; X68150; CAA48253.1; -; mRNA.
DR EMBL; X69880; CAA49506.1; -; Genomic_DNA.
DR EMBL; AL137082; CAB68199.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79804.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79805.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79806.1; -; Genomic_DNA.
DR EMBL; AF324671; AAG40022.1; -; mRNA.
DR EMBL; AF329500; AAG42917.1; -; mRNA.
DR EMBL; AY062094; AAL32973.1; -; mRNA.
DR EMBL; AY065398; AAL38839.1; -; mRNA.
DR EMBL; AY096556; AAM20206.1; -; mRNA.
DR EMBL; BT000669; AAN31816.1; -; mRNA.
DR EMBL; BT000822; AAN33197.1; -; mRNA.
DR PIR; S30145; S30145.
DR PIR; T45681; T45681.
DR RefSeq; NP_001078309.1; NM_001084840.1.
DR RefSeq; NP_001190127.1; NM_001203198.1.
DR RefSeq; NP_191420.1; NM_115723.4.
DR AlphaFoldDB; Q05758; -.
DR SMR; Q05758; -.
DR BioGRID; 10345; 25.
DR STRING; 3702.AT3G58610.3; -.
DR iPTMnet; Q05758; -.
DR PaxDb; Q05758; -.
DR PRIDE; Q05758; -.
DR ProteomicsDB; 250650; -.
DR EnsemblPlants; AT3G58610.1; AT3G58610.1; AT3G58610.
DR EnsemblPlants; AT3G58610.2; AT3G58610.2; AT3G58610.
DR EnsemblPlants; AT3G58610.3; AT3G58610.3; AT3G58610.
DR GeneID; 825030; -.
DR Gramene; AT3G58610.1; AT3G58610.1; AT3G58610.
DR Gramene; AT3G58610.2; AT3G58610.2; AT3G58610.
DR Gramene; AT3G58610.3; AT3G58610.3; AT3G58610.
DR KEGG; ath:AT3G58610; -.
DR Araport; AT3G58610; -.
DR TAIR; locus:2076371; AT3G58610.
DR eggNOG; ENOG502QQBF; Eukaryota.
DR HOGENOM; CLU_033821_5_1_1; -.
DR InParanoid; Q05758; -.
DR OMA; RFTSSSW; -.
DR OrthoDB; 720924at2759; -.
DR PhylomeDB; Q05758; -.
DR BioCyc; ARA:AT3G58610-MON; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR PRO; PR:Q05758; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q05758; baseline and differential.
DR Genevisible; Q05758; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013023; KARI.
DR InterPro; IPR000506; KARI_C.
DR InterPro; IPR013116; KARI_N.
DR InterPro; IPR016206; KetolA_reductoisomerase_plant.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; PTHR21371; 1.
DR Pfam; PF01450; IlvC; 2.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000118; Ilv5_plant; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51851; KARI_C; 2.
DR PROSITE; PS51850; KARI_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast; Magnesium;
KW Metal-binding; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 53..591
FT /note="Ketol-acid reductoisomerase, chloroplastic"
FT /id="PRO_0000015629"
FT DOMAIN 102..300
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 301..449
FT /note="KARI C-terminal knotted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT DOMAIN 450..586
FT /note="KARI C-terminal knotted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /evidence="ECO:0000255"
FT BINDING 123..130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 156..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 195..199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 512
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT MOD_RES 53
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 285
FT /note="A -> R (in Ref. 1; CAA48253)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="A -> V (in Ref. 1; CAA48253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 63812 MW; 003C41A69B2C0F4F CRC64;
MAAATSSIAP SLSCPSPSSS SKTLWSSKAR TLALPNIGFL SSSSKSLRSL TATVAGNGAT
GSSLAARMVS SSAVKAPVSL DFETSVFKKE KVSLAGYEEY IVRGGRDLFK HLPDAFKGIK
QIGVIGWGSQ GPAQAQNLRD SLVEAKSDIV VKIGLRKGSR SFEEARAAGF TEESGTLGDI
WETIAGSDLV LLLISDAAQA DNYEKIFSHM KPNSILGLSH GFLLGHLQSS GLDFPKNISV
VAVCPKGMGP SVRRLYVQGK EINGAGINAS FAVHQDVDGR AADVALGWSV ALGSPFTFAT
TLEQEYRSDI FGERGILLGA VHGIVESLFR RYTENGMSED LAYKNTVECI TGTISRTIST
QGMLAVYNSL SEEGKKDFET AYSASFYPCM EILYECYEDV QSGSEIRSVV LAGRRFYEKE
GLPAFPMGNI DQTRMWKVGE RVRKSRPAGD LGPLYPFTAG VYVALMMAQI EILRKKGHSY
SEIINESVIE SVDSLNPFMH ARGVSFMVDN CSTTARLGSR KWAPRFDYIL TQQALVAVDS
GAAINRDLIS NFFSDPVHGA IEVCAQLRPT VDISVPADAD FVRPELRQSS N
