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Protein

Ketol-acid reductoisomerase, chloroplastic

Gene

AHRI

Organism
Spinacia oleracea (Spinach)
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 (SOVF_080310)
  2. Ketol-acid reductoisomerase, chloroplastic (AHRI), Ketol-acid reductoisomerase (SOVF_017360)
  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 (SOVF_080310)
  2. Ketol-acid reductoisomerase, chloroplastic (AHRI), Ketol-acid reductoisomerase (SOVF_017360)
  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 sitei226 – 2261Sequence analysis
Metal bindingi315 – 3151Magnesium 1
Metal bindingi315 – 3151Magnesium 2
Metal bindingi319 – 3191Magnesium 1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi129 – 1368NADP2 Publications
Nucleotide bindingi162 – 1676NADP2 Publications
Nucleotide bindingi201 – 2055NADP2 Publications

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. 5812.
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
Name:AHRI
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

  • Plastidchloroplast 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7272Chloroplast1 PublicationAdd
BLAST
Chaini73 – 595523Ketol-acid reductoisomerase, chloroplasticPRO_0000015631Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1
595
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi91 – 933Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi103 – 1097Combined sources
Helixi112 – 1176Combined sources
Helixi118 – 1214Combined sources
Turni122 – 1243Combined sources
Beta strandi126 – 1316Combined sources
Helixi136 – 15015Combined sources
Beta strandi156 – 1616Combined sources
Helixi168 – 1736Combined sources
Helixi178 – 1803Combined sources
Beta strandi183 – 1853Combined sources
Helixi186 – 1916Combined sources
Beta strandi194 – 1985Combined sources
Helixi202 – 21514Combined sources
Beta strandi221 – 2277Combined sources
Helixi228 – 2358Combined sources
Beta strandi244 – 25310Combined sources
Helixi255 – 26511Combined sources
Turni266 – 2694Combined sources
Beta strandi275 – 2817Combined sources
Beta strandi283 – 2853Combined sources
Helixi287 – 29711Combined sources
Beta strandi301 – 3055Combined sources
Helixi308 – 32013Combined sources
Turni321 – 3244Combined sources
Helixi325 – 34016Combined sources
Helixi345 – 3506Combined sources
Helixi353 – 3575Combined sources
Helixi359 – 3668Combined sources
Helixi369 – 3746Combined sources
Helixi378 – 40831Combined sources
Helixi410 – 42011Combined sources
Helixi440 – 45011Combined sources
Helixi462 – 48221Combined sources
Helixi486 – 4938Combined sources
Helixi495 – 4995Combined sources
Helixi502 – 51413Combined sources
Helixi519 – 53820Combined sources
Helixi540 – 5456Combined sources
Helixi552 – 5609Combined sources
Helixi563 – 5719Combined sources
Beta strandi586 – 5883Combined sources
Helixi590 – 5923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QMGX-ray1.60A/B/C/D72-595[»]
1YVEX-ray1.65I/J/K/L72-595[»]
ProteinModelPortaliQ01292.
SMRiQ01292. Positions 82-595.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01292.

Family & Domainsi

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

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.

Q01292-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAATTFS LSSSSSTSAA ASKALKQSPK PSALNLGFLG SSSTIKACRS
60 70 80 90 100
LKAARVLPSG ANGGGSALSA QMVSAPSINT PSATTFDFDS SVFKKEKVTL
110 120 130 140 150
SGHDEYIVRG GRNLFPLLPD AFKGIKQIGV IGWGSQAPAQ AQNLKDSLTE
160 170 180 190 200
AKSDVVVKIG LRKGSNSFAE ARAAGFSEEN GTLGDMWETI SGSDLVLLLI
210 220 230 240 250
SDSAQADNYE KVFSHMKPNS ILGLSHGFLL GHLQSLGQDF PKNISVIAVC
260 270 280 290 300
PKGMGPSVRR LYVQGKEVNG AGINSSFAVH QDVDGRATDV ALGWSIALGS
310 320 330 340 350
PFTFATTLEQ EYKSDIFGER GILLGAVHGI VECLFRRYTE SGMSEDLAYK
360 370 380 390 400
NTVECITGVI SKTISTKGML ALYNSLSEEG KKDFQAAYSA SYYPSMDILY
410 420 430 440 450
ECYEDVASGS EIRSVVLAGR RFYEKEGLPA FPMGKIDQTR MWKVGEKVRS
460 470 480 490 500
VRPAGDLGPL YPFTAGVYVA LMMAQIEILR KKGHSYSEII NESVIEAVDS
510 520 530 540 550
LNPFMHARGV SFMVDNCSTT ARLGSRKWAP RFDYILSQQA LVAVDNGAPI
560 570 580 590
NQDLISNFLS DPVHEAIGVC AQLRPSVDIS VTADADFVRP ELRQA
Length:595
Mass (Da):63,754
Last modified:April 1, 1993 - v1
Checksum:iB0EE9055097CFBA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57073 mRNA. Translation: CAA40356.1.
PIRiS17180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57073 mRNA. Translation: CAA40356.1.
PIRiS17180.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QMGX-ray1.60A/B/C/D72-595[»]
1YVEX-ray1.65I/J/K/L72-595[»]
ProteinModelPortaliQ01292.
SMRiQ01292. Positions 82-595.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BRENDAi1.1.1.86. 5812.

Miscellaneous databases

EvolutionaryTraceiQ01292.

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

  1. "Isolation, characterization and sequence analysis of a full-length cDNA clone encoding acetohydroxy acid reductoisomerase from spinach chloroplasts."
    Dumas R., Lebrun M., Douce R.
    Biochem. J. 277:469-475(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-88, SUBCELLULAR LOCATION.
    Tissue: Leaf.
  2. "The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65-A resolution."
    Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., Pebay-Peyroula E.
    EMBO J. 16:3405-3415(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 72-595 IN COMPLEX WITH NADPH AND MAGNESIUM IONS, SUBUNIT.
  3. "Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose."
    Thomazeau K., Dumas R., Halgand F., Forest E., Douce R., Biou V.
    Acta Crystallogr. D 56:389-397(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 72-595 IN COMPLEX WITH NADPH AND MAGNESIUM IONS, SUBUNIT.

Entry informationi

Entry nameiILV5_SPIOL
AccessioniPrimary (citable) accession number: Q01292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 9, 2015
This is version 107 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, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.