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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)DescriptionActionsGraphical viewLength
Active sitei226Sequence analysis1
Metal bindingi315Magnesium 11
Metal bindingi315Magnesium 21
Metal bindingi319Magnesium 11

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi129 – 136NADP2 Publications8
Nucleotide bindingi162 – 167NADP2 Publications6
Nucleotide bindingi201 – 205NADP2 Publications5

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

  • Plastidchloroplast 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 72Chloroplast1 PublicationAdd BLAST72
ChainiPRO_000001563173 – 595Ketol-acid reductoisomerase, chloroplasticAdd BLAST523

Proteomic databases

PRIDEiQ01292.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1595
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi91 – 93Combined sources3
Beta strandi96 – 100Combined sources5
Beta strandi103 – 109Combined sources7
Helixi112 – 117Combined sources6
Helixi118 – 121Combined sources4
Turni122 – 124Combined sources3
Beta strandi126 – 131Combined sources6
Helixi136 – 150Combined sources15
Beta strandi156 – 161Combined sources6
Helixi168 – 173Combined sources6
Helixi178 – 180Combined sources3
Beta strandi183 – 185Combined sources3
Helixi186 – 191Combined sources6
Beta strandi194 – 198Combined sources5
Helixi202 – 215Combined sources14
Beta strandi221 – 227Combined sources7
Helixi228 – 235Combined sources8
Beta strandi244 – 253Combined sources10
Helixi255 – 265Combined sources11
Turni266 – 269Combined sources4
Beta strandi275 – 281Combined sources7
Beta strandi283 – 285Combined sources3
Helixi287 – 297Combined sources11
Beta strandi301 – 305Combined sources5
Helixi308 – 320Combined sources13
Turni321 – 324Combined sources4
Helixi325 – 340Combined sources16
Helixi345 – 350Combined sources6
Helixi353 – 357Combined sources5
Helixi359 – 366Combined sources8
Helixi369 – 374Combined sources6
Helixi378 – 408Combined sources31
Helixi410 – 420Combined sources11
Helixi440 – 450Combined sources11
Helixi462 – 482Combined sources21
Helixi486 – 493Combined sources8
Helixi495 – 499Combined sources5
Helixi502 – 514Combined sources13
Helixi519 – 538Combined sources20
Helixi540 – 545Combined sources6
Helixi552 – 560Combined sources9
Helixi563 – 571Combined sources9
Beta strandi586 – 588Combined sources3
Helixi590 – 592Combined sources3

3D structure databases

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

Proteomic databases

PRIDEiQ01292.

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...

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: November 2, 2016
This is version 111 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.