Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 69 (31 Jul 2019)
Sequence version 1 (24 Mar 2009)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Ketol-acid reductoisomerase

Gene

At3g58610

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Unreviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase (AXX17_At3g42690), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3), Branched-chain-amino-acid aminotransferase 6 (BCAT6)
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.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase (AXX17_At3g42690), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3), Branched-chain-amino-acid aminotransferase 6 (BCAT6)
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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei220UniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi309Magnesium 1UniRule annotation1
Metal bindingi309Magnesium 2UniRule annotation1
Metal bindingi313Magnesium 1UniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei371SubstratePROSITE-ProRule annotation1
Metal bindingi486Magnesium 2PROSITE-ProRule annotation1
Metal bindingi490Magnesium 2PROSITE-ProRule annotation1
Binding sitei512SubstratePROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation, NADPUniRule annotation

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00047;UER00056
UPA00049;UER00060

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ketol-acid reductoisomeraseUniRule annotation (EC:1.1.1.86UniRule annotation)
Alternative name(s):
Acetohydroxy-acid reductoisomeraseUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:At3g58610Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
B9DH71

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
B9DH71 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

UniRule annotation

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini102 – 300KARI N-terminal RossmannInterPro annotationAdd BLAST199
Domaini301 – 449KARI C-terminal knottedInterPro annotationAdd BLAST149
Domaini450 – 586KARI C-terminal knottedInterPro annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 20DisorderedSequence analysisAdd BLAST20

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IEEV Eukaryota
COG0059 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1040.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR013328 6PGD_dom2
IPR013023 KARI
IPR000506 KARI_C
IPR013116 KARI_N
IPR016206 KetolA_reductoisomerase_plant
IPR036291 NAD(P)-bd_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR21371 PTHR21371, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01450 IlvC, 2 hits
PF07991 IlvN, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000118 Ilv5_plant, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51851 KARI_C, 2 hits
PS51850 KARI_N, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

B9DH71-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAATSSIAP SLSCPSPSSS SKTLWSSKAR TLALPNIGFL SSSSKSLRSL
60 70 80 90 100
TATVAGNGAT GSSLAARMVS SSAVKAPVSL DFETSVFKKE KVSLAGYEVY
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):63,782
Last modified:March 24, 2009 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i68DFCF9E7E24BB34
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK317420 mRNA Translation: BAH20088.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK317420 mRNA Translation: BAH20088.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Proteomic databases

PRIDEiB9DH71

Phylogenomic databases

eggNOGiENOG410IEEV Eukaryota
COG0059 LUCA

Enzyme and pathway databases

UniPathwayiUPA00047;UER00056
UPA00049;UER00060

Gene expression databases

ExpressionAtlasiB9DH71 baseline and differential

Family and domain databases

Gene3Di1.10.1040.10, 1 hit
InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR013328 6PGD_dom2
IPR013023 KARI
IPR000506 KARI_C
IPR013116 KARI_N
IPR016206 KetolA_reductoisomerase_plant
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR21371 PTHR21371, 1 hit
PfamiView protein in Pfam
PF01450 IlvC, 2 hits
PF07991 IlvN, 1 hit
PIRSFiPIRSF000118 Ilv5_plant, 1 hit
SUPFAMiSSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS51851 KARI_C, 2 hits
PS51850 KARI_N, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiB9DH71_ARATH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B9DH71
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: July 31, 2019
This is version 69 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again