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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei208 – 2081Sequence analysis
Metal bindingi297 – 2971Magnesium 1
Metal bindingi297 – 2971Magnesium 2
Metal bindingi301 – 3011Magnesium 1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi111 – 1188NADP1 Publication
Nucleotide bindingi144 – 1496NADP1 Publication
Nucleotide bindingi183 – 1875NADP1 Publication

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

ChEMBLiCHEMBL2366499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252ChloroplastSequence analysisAdd
BLAST
Chaini53 – 578526Ketol-acid reductoisomerase, chloroplasticPRO_0000383458Add
BLAST

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

1
578
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 753Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 917Combined sources
Helixi94 – 996Combined sources
Helixi100 – 1034Combined sources
Turni104 – 1063Combined sources
Beta strandi108 – 1136Combined sources
Helixi118 – 13215Combined sources
Beta strandi138 – 1436Combined sources
Helixi150 – 1556Combined sources
Turni160 – 1634Combined sources
Beta strandi165 – 1673Combined sources
Helixi168 – 1747Combined sources
Beta strandi176 – 1805Combined sources
Helixi184 – 19714Combined sources
Beta strandi203 – 2097Combined sources
Helixi210 – 2178Combined sources
Beta strandi226 – 23510Combined sources
Helixi237 – 24711Combined sources
Beta strandi257 – 2637Combined sources
Beta strandi265 – 2673Combined sources
Helixi269 – 27911Combined sources
Beta strandi283 – 2875Combined sources
Helixi290 – 30213Combined sources
Turni303 – 3064Combined sources
Helixi307 – 32216Combined sources
Helixi327 – 3337Combined sources
Helixi335 – 3395Combined sources
Helixi341 – 3499Combined sources
Helixi351 – 3566Combined sources
Helixi360 – 39031Combined sources
Helixi392 – 40211Combined sources
Helixi422 – 43312Combined sources
Helixi444 – 46320Combined sources
Helixi468 – 4758Combined sources
Helixi477 – 4815Combined sources
Helixi483 – 4908Combined sources
Helixi492 – 4987Combined sources
Helixi501 – 52020Combined sources
Helixi522 – 5276Combined sources
Helixi534 – 5429Combined sources
Helixi545 – 5539Combined sources
Beta strandi568 – 5703Combined sources

3D structure databases

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731S → F in AK065295 (PubMed:12869764).Curated
Sequence conflicti183 – 1831S → L in AK065295 (PubMed:12869764).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3FR7X-ray1.55A/B54-578[»]
3FR8X-ray2.80A/B54-578[»]
ProteinModelPortaliQ65XK0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os05g49800.1.

Chemistry

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.
OMAiNPYMHAR.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nipponbare.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nipponbare.
  3. "The rice annotation project database (RAP-DB): 2008 update."
    The rice annotation project (RAP)
    Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: cv. Nipponbare.
  4. Cited for: GENOME REANNOTATION.
    Strain: cv. Nipponbare.
  5. "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
    The rice full-length cDNA consortium
    Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Nipponbare.
  6. "Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures."
    Leung E.W.W., Guddat L.W.
    J. Mol. Biol. 389:167-182(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 54-578 IN COMPLEX WITH MAGNESIUM IONS AND NADPH, SUBUNIT.

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: June 8, 2016
This is version 84 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.