Reviewed, UniProtKB/Swiss-Prot Q05758 (ILV5_ARATH)

Names and origin

Protein names

Recommended name:
    Ketol-acid reductoisomerase, chloroplastic
    EC=1.1.1.86
Alternative name(s):
    Acetohydroxy-acid reductoisomerase
    Alpha-keto-beta-hydroxylacil reductoisomerase

Gene names

Ordered Locus Names:	At3g58610
ORF Names:	F14P22.200

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	(R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
Cofactor	Magnesium.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
Subunit structure	Tetramer of similar but non-identical chains.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the ketol-acid reductoisomerase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 67	67	Chloroplast By similarity
	Chain	68 – 591	524	Ketol-acid reductoisomerase, chloroplastic		PRO_0000015629
Regions
	Nucleotide binding	126 – 135	10	NADP Potential
Sites
	Active site	220	1	Potential
Experimental info
	Sequence conflict	285	1	A → R in CAA48253. Ref.1
	Sequence conflict	579	1	A → V in CAA48253. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q05758-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 003C41A69B2C0F4F	FASTA	591	63,812
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and characterization of a cDNA encoding the acetohydroxy acid isomeroreductase from Arabidopsis thaliana." Curien G., Dumas R., Douce R. Plant Mol. Biol. 21:717-722(1993) [PubMed: 8448371] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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)." Dumas R., Curien G., Derose R.T., Douce R. Biochem. J. 294:821-828(1993) [PubMed: 8379936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." 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. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X68150 mRNA. Translation: CAA48253.1. X69880 Genomic DNA. Translation: CAA49506.1. AL137082 Genomic DNA. Translation: CAB68199.1. AF324671 mRNA. Translation: AAG40022.1. AF329500 mRNA. Translation: AAG42917.1. AY062094 mRNA. Translation: AAL32973.1. AY065398 mRNA. Translation: AAL38839.1. AY096556 mRNA. Translation: AAM20206.1. BT000669 mRNA. Translation: AAN31816.1. BT000822 mRNA. Translation: AAN33197.1.
PIR	S30145. T45681.
RefSeq	NP_001078309.1. NP_191420.1.
UniGene	At.46637
3D structure databases
HSSP	HSSP built from PDB template 1QMG based on UniProtKB Q01292.
SMR	Q05758. Positions 79-589.
ModBase	Search...
Genome annotation databases
GeneID	825030.
GenomeReviews	Gene locus AT3G58610 in contig BA000014_GR.
KEGG	ath:AT3G58610.
NMPDR	fig|3702.1.peg.17203.
Organism-specific databases
GeneFarm	4243.
TAIR	At3g58610.
Gene expression databases
ArrayExpress	Q05758.
GermOnline	AT3G58610. Arabidopsis thaliana.
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR21371. AcH_isomrdctse. 1 hit.
Pfam	PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view]
PIRSF	PIRSF000118. Ilv5_plant. 1 hit.
TIGRFAMs	TIGR00465. ilvC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ILV5_ARATH

Accession

Primary (citable) accession number: Q05758
Secondary accession number(s): Q42559

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)