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Q05758 (ILV5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Binds 2 magnesium ions per subunit By similarity.

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

Homodimer By similarity.

Subcellular location

Plastid › chloroplast Probable.

Sequence similarities

Belongs to the ketol-acid reductoisomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6868Chloroplast By similarity
Chain69 – 591523Ketol-acid reductoisomerase, chloroplastic
PRO_0000015629

Regions

Nucleotide binding123 – 1308NADP By similarity
Nucleotide binding156 – 1616NADP By similarity
Nucleotide binding195 – 1995NADP By similarity

Sites

Active site2201 Potential
Metal binding3091Magnesium 1 By similarity
Metal binding3091Magnesium 2 By similarity
Metal binding3131Magnesium 1 By similarity

Experimental info

Sequence conflict2851A → R in CAA48253. Ref.1
Sequence conflict5791A → V in CAA48253. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q05758 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 003C41A69B2C0F4F

FASTA59163,812
        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

« Hide

References

« Hide '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. expand/collapse author list , 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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X68150 mRNA. Translation: CAA48253.1.
X69880 Genomic DNA. Translation: CAA49506.1.
AL137082 Genomic DNA. Translation: CAB68199.1.
CP002686 Genomic DNA. Translation: AEE79804.1.
CP002686 Genomic DNA. Translation: AEE79805.1.
CP002686 Genomic DNA. Translation: AEE79806.1.
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.
IPIIPI00533630.
PIRS30145.
T45681.
RefSeqNP_001078309.1. NM_001084840.1.
NP_001190127.1. NM_001203198.1.
NP_191420.1. NM_115723.3.
UniGeneAt.46637.
At.69012.

3D structure databases

ProteinModelPortalQ05758.
SMRQ05758. Positions 79-587.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ05758.

Proteomic databases

PRIDEQ05758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G58610.1; AT3G58610.1; AT3G58610.
AT3G58610.2; AT3G58610.2; AT3G58610.
AT3G58610.3; AT3G58610.3; AT3G58610.
GeneID825030.
GenomeReviewsGene locus AT3G58610 in contig BA000014_GR.
KEGGath:AT3G58610.
NMPDRfig|3702.1.peg.17203.

Organism-specific databases

GeneFarm4243.
TAIRAt3g58610.

Phylogenomic databases

eggNOGeuNOG04627.
HOGENOMHBG743920.
InParanoidQ05758.
OMAEAYSAAY.
PhylomeDBQ05758.
ProtClustDBCLSN2684737.

Gene expression databases

ArrayExpressQ05758.
GenevestigatorQ05758.
GermOnlineAT3G58610. Arabidopsis thaliana.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013023. AcH_isomrdctse.
IPR000506. AcH_isomrdctse_C.
IPR013328. DH_multihelical.
IPR013116. IlvN.
IPR016206. KetolA_reductoisomerase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KOK00053.
PANTHERPTHR21371. AcH_isomrdctse. 1 hit.
PfamPF01450. IlvC. 2 hits.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFPIRSF000118. Ilv5_plant. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameILV5_ARATH
AccessionPrimary (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: December 14, 2011
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents