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Protein

Ketol-acid reductoisomerase, chloroplastic

Gene

Os05g0573700

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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+Note: Binds 2 magnesium ions per subunit.

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 (OsJ_06870), Acetolactate synthase (OsJ_14580), Probable acetolactate synthase 2, chloroplastic (ALS2), Acetolactate synthase 1, chloroplastic (ALS1), Acetolactate synthase (Os02g0510200)
  2. Ketol-acid reductoisomerase (OsJ_02845), Ketol-acid reductoisomerase, chloroplastic (Os05g0573700), Ketol-acid reductoisomerase (Os01g0652600)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
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 (OsJ_06870), Acetolactate synthase (OsJ_14580), Probable acetolactate synthase 2, chloroplastic (ALS2), Acetolactate synthase 1, chloroplastic (ALS1), Acetolactate synthase (Os02g0510200)
  2. Ketol-acid reductoisomerase (OsJ_02845), Ketol-acid reductoisomerase, chloroplastic (Os05g0573700), Ketol-acid reductoisomerase (Os01g0652600)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
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)DescriptionActionsGraphical viewLength
Active sitei208Sequence analysis1
Metal bindingi297Magnesium 11
Metal bindingi297Magnesium 21
Metal bindingi301Magnesium 11

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi111 – 118NADP1 Publication8
Nucleotide bindingi144 – 149NADP1 Publication6
Nucleotide bindingi183 – 187NADP1 Publication5

GO - Molecular functioni

  • ketol-acid reductoisomerase activity Source: UniProtKB-EC
  • magnesium ion binding Source: UniProtKB
  • NADPH binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

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

BRENDAi1.1.1.86. 4460.
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
Protein KARI
Gene namesi
Ordered Locus Names:Os05g0573700, LOC_Os05g49800
ORF Names:OJ1735_C10.18
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
Proteomesi
  • UP000059680 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 52ChloroplastSequence analysisAdd BLAST52
ChainiPRO_000038345853 – 578Ketol-acid reductoisomerase, chloroplasticAdd BLAST526

Proteomic databases

PaxDbiQ65XK0.
PRIDEiQ65XK0.

Expressioni

Gene expression databases

ExpressionAtlasiQ65XK0. baseline and differential.
GenevisibleiQ65XK0. OS.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi39947.LOC_Os05g49800.1.

Structurei

Secondary structure

1578
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi73 – 75Combined sources3
Beta strandi77 – 82Combined sources6
Beta strandi85 – 91Combined sources7
Helixi94 – 99Combined sources6
Helixi100 – 103Combined sources4
Turni104 – 106Combined sources3
Beta strandi108 – 113Combined sources6
Helixi118 – 132Combined sources15
Beta strandi138 – 143Combined sources6
Helixi150 – 155Combined sources6
Turni160 – 163Combined sources4
Beta strandi165 – 167Combined sources3
Helixi168 – 174Combined sources7
Beta strandi176 – 180Combined sources5
Helixi184 – 197Combined sources14
Beta strandi203 – 209Combined sources7
Helixi210 – 217Combined sources8
Beta strandi226 – 235Combined sources10
Helixi237 – 247Combined sources11
Beta strandi257 – 263Combined sources7
Beta strandi265 – 267Combined sources3
Helixi269 – 279Combined sources11
Beta strandi283 – 287Combined sources5
Helixi290 – 302Combined sources13
Turni303 – 306Combined sources4
Helixi307 – 322Combined sources16
Helixi327 – 333Combined sources7
Helixi335 – 339Combined sources5
Helixi341 – 349Combined sources9
Helixi351 – 356Combined sources6
Helixi360 – 390Combined sources31
Helixi392 – 402Combined sources11
Helixi422 – 433Combined sources12
Helixi444 – 463Combined sources20
Helixi468 – 475Combined sources8
Helixi477 – 481Combined sources5
Helixi483 – 490Combined sources8
Helixi492 – 498Combined sources7
Helixi501 – 520Combined sources20
Helixi522 – 527Combined sources6
Helixi534 – 542Combined sources9
Helixi545 – 553Combined sources9
Beta strandi568 – 570Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FR7X-ray1.55A/B54-578[»]
3FR8X-ray2.80A/B54-578[»]
ProteinModelPortaliQ65XK0.
SMRiQ65XK0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ65XK0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IEEV. Eukaryota.
COG0059. LUCA.
InParanoidiQ65XK0.
KOiK00053.
OMAiEDAFKNT.
OrthoDBiEOG093606Q2.

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.

Q65XK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTTLALS HPKTLAAAAA AAPKAPTAPA AVSFPVSHAA CAPLAARRRA
60 70 80 90 100
VTAMVAAPPA VGAAMPSLDF DTSVFNKEKV SLAGHEEYIV RGGRNLFPLL
110 120 130 140 150
PEAFKGIKQI GVIGWGSQGP AQAQNLRDSL AEAKSDIVVK IGLRKGSKSF
160 170 180 190 200
DEARAAGFTE ESGTLGDIWE TVSGSDLVLL LISDAAQADN YEKIFSHMKP
210 220 230 240 250
NSILGLSHGF LLGHLQSAGL DFPKNISVIA VCPKGMGPSV RRLYVQGKEI
260 270 280 290 300
NGAGINSSFA VHQDVDGRAT DVALGWSVAL GSPFTFATTL EQEYKSDIFG
310 320 330 340 350
ERGILLGAVH GIVEALFRRY TEQGMDEEMA YKNTVEGITG IISKTISKKG
360 370 380 390 400
MLEVYNSLTE EGKKEFNKAY SASFYPCMDI LYECYEDVAS GSEIRSVVLA
410 420 430 440 450
GRRFYEKEGL PAFPMGNIDQ TRMWKVGEKV RSTRPENDLG PLHPFTAGVY
460 470 480 490 500
VALMMAQIEV LRKKGHSYSE IINESVIESV DSLNPFMHAR GVAFMVDNCS
510 520 530 540 550
TTARLGSRKW APRFDYILTQ QAFVTVDKDA PINQDLISNF MSDPVHGAIE
560 570
VCAELRPTVD ISVPANADFV RPELRQSS
Length:578
Mass (Da):62,377
Last modified:October 25, 2004 - v1
Checksum:iC81C84F7F03F5506
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173S → F in AK065295 (PubMed:12869764).Curated1
Sequence conflicti183S → L in AK065295 (PubMed:12869764).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC104284 Genomic DNA. Translation: AAU44107.1.
AP008211 Genomic DNA. Translation: BAF18298.1.
AP014961 Genomic DNA. Translation: BAS95451.1.
AK065295 mRNA. No translation available.
RefSeqiXP_015640421.1. XM_015784935.1.
UniGeneiOs.4761.

Genome annotation databases

EnsemblPlantsiOS05T0573700-01; OS05T0573700-01; OS05G0573700.
GeneIDi4339677.
GrameneiOS05T0573700-01; OS05T0573700-01; OS05G0573700.
KEGGiosa:4339677.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC104284 Genomic DNA. Translation: AAU44107.1.
AP008211 Genomic DNA. Translation: BAF18298.1.
AP014961 Genomic DNA. Translation: BAS95451.1.
AK065295 mRNA. No translation available.
RefSeqiXP_015640421.1. XM_015784935.1.
UniGeneiOs.4761.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FR7X-ray1.55A/B54-578[»]
3FR8X-ray2.80A/B54-578[»]
ProteinModelPortaliQ65XK0.
SMRiQ65XK0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os05g49800.1.

Chemistry databases

ChEMBLiCHEMBL2366499.

Proteomic databases

PaxDbiQ65XK0.
PRIDEiQ65XK0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiOS05T0573700-01; OS05T0573700-01; OS05G0573700.
GeneIDi4339677.
GrameneiOS05T0573700-01; OS05T0573700-01; OS05G0573700.
KEGGiosa:4339677.

Phylogenomic databases

eggNOGiENOG410IEEV. Eukaryota.
COG0059. LUCA.
InParanoidiQ65XK0.
KOiK00053.
OMAiEDAFKNT.
OrthoDBiEOG093606Q2.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BRENDAi1.1.1.86. 4460.

Miscellaneous databases

EvolutionaryTraceiQ65XK0.

Gene expression databases

ExpressionAtlasiQ65XK0. baseline and differential.
GenevisibleiQ65XK0. OS.

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...

Entry informationi

Entry nameiILV5_ORYSJ
AccessioniPrimary (citable) accession number: Q65XK0
Secondary accession number(s): A0A0P0WRB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 25, 2004
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  4. 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.