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UniProtKB/Swiss-Prot entry Q05758


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ILV5_ARATH
Primary accession number Q05758
Secondary accession number Q42559
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 68)
Name and origin of the protein
Protein name Ketol-acid reductoisomerase, chloroplastic [Precursor]
Synonyms EC 1.1.1.86
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacil reductoisomerase
Gene name
OrderedLocusNames: At3g58610
ORFNames: F14P22.200
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/BF00014556; PubMed=8448371 [NCBI, ExPASy, EBI, Israel, Japan]
Curien G., Dumas R., Douce R.;
"Nucleotide sequence and characterization of a cDNA encoding the acetohydroxy acid isomeroreductase from Arabidopsis thaliana.";
Plant Mol. Biol. 21:717-722(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8379936 [NCBI, ExPASy, EBI, Israel, Japan]
Dumas R., Curien G., Derose R.T., Douce R.;
"Branched-chain-amino-acid biosynthesis in plants: molecular cloning and characterization of the gene encoding acetohydroxy acid isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress).";
Biochem. J. 294:821-828(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X68150; CAA48253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X69880; CAA49506.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137082; CAB68199.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF324671; AAG40022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF329500; AAG42917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY062094; AAL32973.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065398; AAL38839.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096556; AAM20206.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000669; AAN31816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000822; AAN33197.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S30145; S30145.
T45681; T45681.
RefSeq NP_001078309.1; -.
NP_191420.1; -.
UniGene At.46637
3D structure databases
HSSP Q01292; 1QMG. [HSSP ENTRY / PDB]
SMR Q05758; 79-589.
ModBase Q05758.
Organism-specific databases
GeneFarm 4243; -.
TAIR At3g58610; -.
Gene expression databases
ArrayExpress Q05758; -.
GermOnline AT3G58610; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013023; AcH_isomrdctse.
IPR000506; AcH_isomrdctse_C.
IPR013328; DHase_multihelical.
IPR013116; IlvN.
IPR016206; KetolA_reductoisomerase_pln.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR21371; AcH_isomrdctse; 1.
Pfam PF01450; IlvC; 1.
PF07991; IlvN; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000118; Ilv5_plant; 1.
TIGRFAMs TIGR00465; ilvC; 1.
BLOCKS Q05758.
ProtoNet Q05758.
Genome annotation databases
GeneID 825030; -.
GenomeReviews BA000014_GR; AT3G58610.
KEGG ath:AT3G58610; -.
NMPDR fig|3702.1.peg.17203; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Chloroplast; Complete proteome; Magnesium; NADP; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    67  67     Chloroplast (By similarity). 
CHAIN   68   591  524     Ketol-acid reductoisomerase, chloroplastic. PRO_0000015629
NP_BIND   126   135  10     NADP (Potential). 
ACT_SITE   220   220        Potential. 
CONFLICT   285   285        A -> R (in Ref. 1; CAA48253). 
CONFLICT   579   579        A -> V (in Ref. 1; CAA48253). 
Sequence information
Length: 591 AA [This is the length of the unprocessed precursor] Molecular weight: 63812 Da [This is the MW of the unprocessed precursor] CRC64: 003C41A69B2C0F4F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAATSSIAP SLSCPSPSSS SKTLWSSKAR TLALPNIGFL SSSSKSLRSL TATVAGNGAT 

        70         80         90        100        110        120 
GSSLAARMVS SSAVKAPVSL DFETSVFKKE KVSLAGYEEY IVRGGRDLFK HLPDAFKGIK 

       130        140        150        160        170        180 
QIGVIGWGSQ GPAQAQNLRD SLVEAKSDIV VKIGLRKGSR SFEEARAAGF TEESGTLGDI 

       190        200        210        220        230        240 
WETIAGSDLV LLLISDAAQA DNYEKIFSHM KPNSILGLSH GFLLGHLQSS GLDFPKNISV 

       250        260        270        280        290        300 
VAVCPKGMGP SVRRLYVQGK EINGAGINAS FAVHQDVDGR AADVALGWSV ALGSPFTFAT 

       310        320        330        340        350        360 
TLEQEYRSDI FGERGILLGA VHGIVESLFR RYTENGMSED LAYKNTVECI TGTISRTIST 

       370        380        390        400        410        420 
QGMLAVYNSL SEEGKKDFET AYSASFYPCM EILYECYEDV QSGSEIRSVV LAGRRFYEKE 

       430        440        450        460        470        480 
GLPAFPMGNI DQTRMWKVGE RVRKSRPAGD LGPLYPFTAG VYVALMMAQI EILRKKGHSY 

       490        500        510        520        530        540 
SEIINESVIE SVDSLNPFMH ARGVSFMVDN CSTTARLGSR KWAPRFDYIL TQQALVAVDS 

       550        560        570        580        590 
GAAINRDLIS NFFSDPVHGA IEVCAQLRPT VDISVPADAD FVRPELRQSS N 

Q05758 in FASTA format

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