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Protein

Ketol-acid reductoisomerase, chloroplastic

Gene

At3g58610

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei220 – 2201Sequence analysis
Metal bindingi309 – 3091Magnesium 1By similarity
Metal bindingi309 – 3091Magnesium 2By similarity
Metal bindingi313 – 3131Magnesium 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi123 – 1308NADPBy similarity
Nucleotide bindingi156 – 1616NADPBy similarity
Nucleotide bindingi195 – 1995NADPBy similarity

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • ketol-acid reductoisomerase activity Source: UniProtKB-EC

GO - Biological processi

  • isoleucine biosynthetic process Source: UniProtKB-UniPathway
  • response to cadmium ion Source: TAIR
  • valine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, NADP

Enzyme and pathway databases

BioCyciARA:AT3G58610-MONOMER.
ARA:GQT-1289-MONOMER.
ARA:GQT-1290-MONOMER.
UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase, chloroplastic (EC:1.1.1.86)
Alternative name(s):
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacyl reductoisomerase
Gene namesi
Ordered Locus Names:At3g58610
ORF Names:F14P22.200
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G58610.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • mitochondrion Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6868ChloroplastBy similarityAdd
BLAST
Chaini69 – 591523Ketol-acid reductoisomerase, chloroplasticPRO_0000015629Add
BLAST

Proteomic databases

PaxDbiQ05758.
PRIDEiQ05758.

Expressioni

Gene expression databases

GenevisibleiQ05758. AT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi10345. 2 interactions.
STRINGi3702.AT3G58610.1.

Structurei

3D structure databases

ProteinModelPortaliQ05758.
SMRiQ05758. Positions 79-587.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IEEV. Eukaryota.
COG0059. LUCA.
HOGENOMiHOG000238129.
InParanoidiQ05758.
KOiK00053.
OMAiGKKQFIE.
PhylomeDBiQ05758.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016206. KetolA_reductoisomerase_plant.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 2 hits.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFiPIRSF000118. Ilv5_plant. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATSSIAP SLSCPSPSSS SKTLWSSKAR TLALPNIGFL SSSSKSLRSL
60 70 80 90 100
TATVAGNGAT GSSLAARMVS SSAVKAPVSL DFETSVFKKE KVSLAGYEEY
110 120 130 140 150
IVRGGRDLFK HLPDAFKGIK QIGVIGWGSQ GPAQAQNLRD SLVEAKSDIV
160 170 180 190 200
VKIGLRKGSR SFEEARAAGF TEESGTLGDI WETIAGSDLV LLLISDAAQA
210 220 230 240 250
DNYEKIFSHM KPNSILGLSH GFLLGHLQSS GLDFPKNISV VAVCPKGMGP
260 270 280 290 300
SVRRLYVQGK EINGAGINAS FAVHQDVDGR AADVALGWSV ALGSPFTFAT
310 320 330 340 350
TLEQEYRSDI FGERGILLGA VHGIVESLFR RYTENGMSED LAYKNTVECI
360 370 380 390 400
TGTISRTIST QGMLAVYNSL SEEGKKDFET AYSASFYPCM EILYECYEDV
410 420 430 440 450
QSGSEIRSVV LAGRRFYEKE GLPAFPMGNI DQTRMWKVGE RVRKSRPAGD
460 470 480 490 500
LGPLYPFTAG VYVALMMAQI EILRKKGHSY SEIINESVIE SVDSLNPFMH
510 520 530 540 550
ARGVSFMVDN CSTTARLGSR KWAPRFDYIL TQQALVAVDS GAAINRDLIS
560 570 580 590
NFFSDPVHGA IEVCAQLRPT VDISVPADAD FVRPELRQSS N
Length:591
Mass (Da):63,812
Last modified:December 1, 2000 - v2
Checksum:i003C41A69B2C0F4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851A → R in CAA48253 (PubMed:8448371).Curated
Sequence conflicti579 – 5791A → V in CAA48253 (PubMed:8448371).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS30145.
T45681.
RefSeqiNP_001078309.1. NM_001084840.1.
NP_001190127.1. NM_001203198.1.
NP_191420.1. NM_115723.3.
UniGeneiAt.46637.
At.480.
At.69012.

Genome annotation databases

EnsemblPlantsiAT3G58610.1; AT3G58610.1; AT3G58610.
AT3G58610.2; AT3G58610.2; AT3G58610.
AT3G58610.3; AT3G58610.3; AT3G58610.
GeneIDi825030.
GrameneiAT3G58610.1; AT3G58610.1; AT3G58610.
AT3G58610.2; AT3G58610.2; AT3G58610.
AT3G58610.3; AT3G58610.3; AT3G58610.
KEGGiath:AT3G58610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS30145.
T45681.
RefSeqiNP_001078309.1. NM_001084840.1.
NP_001190127.1. NM_001203198.1.
NP_191420.1. NM_115723.3.
UniGeneiAt.46637.
At.480.
At.69012.

3D structure databases

ProteinModelPortaliQ05758.
SMRiQ05758. Positions 79-587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10345. 2 interactions.
STRINGi3702.AT3G58610.1.

Proteomic databases

PaxDbiQ05758.
PRIDEiQ05758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G58610.1; AT3G58610.1; AT3G58610.
AT3G58610.2; AT3G58610.2; AT3G58610.
AT3G58610.3; AT3G58610.3; AT3G58610.
GeneIDi825030.
GrameneiAT3G58610.1; AT3G58610.1; AT3G58610.
AT3G58610.2; AT3G58610.2; AT3G58610.
AT3G58610.3; AT3G58610.3; AT3G58610.
KEGGiath:AT3G58610.

Organism-specific databases

TAIRiAT3G58610.

Phylogenomic databases

eggNOGiENOG410IEEV. Eukaryota.
COG0059. LUCA.
HOGENOMiHOG000238129.
InParanoidiQ05758.
KOiK00053.
OMAiGKKQFIE.
PhylomeDBiQ05758.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BioCyciARA:AT3G58610-MONOMER.
ARA:GQT-1289-MONOMER.
ARA:GQT-1290-MONOMER.

Miscellaneous databases

PROiQ05758.

Gene expression databases

GenevisibleiQ05758. AT.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016206. KetolA_reductoisomerase_plant.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 2 hits.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFiPIRSF000118. Ilv5_plant. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiILV5_ARATH
AccessioniPrimary (citable) accession number: Q05758
Secondary accession number(s): Q42559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 1, 2000
Last modified: February 17, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.