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   16-JUN-2009, entry version 75.
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-hydroxylacil reductoisomerase;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g58610; ORFNames=F14P22.200;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93192533; 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   MEDLINE=93393563; PubMed=8379936;
RA   Dumas R., Curien G., Derose R.T., Douce R.;
RT   "Branched-chain-amino-acid biosynthesis in plants: molecular cloning
RT   and characterization of the gene encoding acetohydroxy acid
RT   isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis
RT   thaliana (thale cress).";
RL   Biochem. J. 294:821-828(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; 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).
CC   -!- CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
CC       = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CC   -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
CC       NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
CC   -!- COFACTOR: Magnesium.
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
CC       from pyruvate: step 2/4.
CC   -!- SUBUNIT: Tetramer of similar but non-identical chains.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
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DR   EMBL; X68150; CAA48253.1; -; mRNA.
DR   EMBL; X69880; CAA49506.1; -; Genomic_DNA.
DR   EMBL; AL137082; CAB68199.1; -; 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   IPI; IPI00533630; -.
DR   PIR; S30145; S30145.
DR   PIR; T45681; T45681.
DR   RefSeq; NP_001078309.1; -.
DR   RefSeq; NP_191420.1; -.
DR   UniGene; At.46637; -.
DR   UniGene; At.69012; -.
DR   HSSP; Q01292; 1QMG.
DR   SMR; Q05758; 79-589.
DR   PRIDE; Q05758; -.
DR   GeneID; 825030; -.
DR   GenomeReviews; BA000014_GR; AT3G58610.
DR   KEGG; ath:AT3G58610; -.
DR   NMPDR; fig|3702.1.peg.17203; -.
DR   GeneFarm; 4243; -.
DR   TAIR; At3g58610; -.
DR   OMA; Q05758; KAYSASF.
DR   BRENDA; 1.1.1.86; 302.
DR   ArrayExpress; Q05758; -.
DR   GermOnline; AT3G58610; Arabidopsis thaliana.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0005618; C:cell wall; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched chain family amino acid biosynthet...; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   InterPro; IPR013023; AcH_isomrdctse.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR016206; KetolA_reductoisomerase_pln.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   PANTHER; PTHR21371; AcH_isomrdctse; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000118; Ilv5_plant; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; Complete proteome; Magnesium; NADP; Oxidoreductase;
KW   Plastid; Transit peptide.
FT   TRANSIT       1     67       Chloroplast (By similarity).
FT   CHAIN        68    591       Ketol-acid reductoisomerase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000015629.
FT   NP_BIND     126    135       NADP (Potential).
FT   ACT_SITE    220    220       Potential.
FT   CONFLICT    285    285       A -> R (in Ref. 1; CAA48253).
FT   CONFLICT    579    579       A -> V (in Ref. 1; CAA48253).
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
//