Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P05793 (ILVC_ECOLI)

Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 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 protein 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

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, 3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate (PubMed:15654896).4 Publications

<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 annotation3 PublicationsNote: Binds 2 magnesium ions per subunit.UniRule annotation2 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by N-hydroxy-N-isopropyloxamate (IpOHA).1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). Kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). Kcat is 0.11 min(-1) for reductoisomerase activity with NADH as substrate (PubMed:9015391). Kcat is 5.376 sec(-1) for reductoisomerase activity with 3-hydroxypyruvate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 3.6 sec(-1) for reductoisomerase activity with NADPH as substrate (PubMed:21515217). Kcat is 3.511 sec(-1) for reductoisomerase activity with 3-hydroxy-3-methyl-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 2.231 sec(-1) for reductoisomerase activity with 2-acetolactate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.594 sec(-1) for reductoisomerase activity with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.3 sec(-1) for reductoisomerase activity with NADH as substrate (PubMed:21515217). Kcat is 0.194 sec(-1) for reductoisomerase activity with 2-ketopantoate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.182 sec(-1) for reductoisomerase activity with 2-ketoisovalerate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.167 sec(-1) for reductoisomerase activity with 2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.05 sec(-1) for reductoisomerase activity with 2-ketovalerate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is 0.021 sec(-1) for reductoisomerase activity with pyruvate as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896).3 Publications
  1. KM=0.04 mM for NADPH1 Publication
  2. KM=0.042 mM for NADP1 Publication
  3. KM=0.073 mM for NADPH1 Publication
  4. KM=0.17 mM for 2-ketopantoate (at pH 8 and 37 degrees Celsius)1 Publication
  5. KM=0.206 mM for NADH1 Publication
  6. KM=0.21 mM for 3-hydroxy-2-ketobutyrate (at pH 8 and 37 degrees Celsius)1 Publication
  7. KM=0.25 mM for 2-acetolactate (at pH 8 and 37 degrees Celsius)1 Publication
  8. KM=0.27 mM for 3-hydroxy-3-methyl-2-ketobutyrate (at pH 8 and 37 degrees Celsius)1 Publication
  9. KM=0.42 mM for magnesium (with S2AL and NADPH as substrates)1 Publication
  10. KM=1.08 mM for NADH1 Publication
  11. KM=1.54 mM for pyruvate (at pH 8 and 37 degrees Celsius)1 Publication
  12. KM=2.96 mM for 3-hydroxypyruvate (at pH 8 and 37 degrees Celsius)1 Publication
  13. KM=3.15 mM for 2-ketovalerate (at pH 8 and 37 degrees Celsius)1 Publication
  14. KM=4.56 mM for 2-ketobutyrate (at pH 8 and 37 degrees Celsius)1 Publication
  15. KM=6.91 mM for 2-ketoisovalerate (at pH 8 and 37 degrees Celsius)1 Publication
  1. Vmax=5.421 µmol/min/mg enzyme with 3-hydroxypyruvate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  2. Vmax=3.541 µmol/min/mg enzyme with 3-hydroxy-3-methyl-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  3. Vmax=2.25 µmol/min/mg enzyme with 2-acetolactate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  4. Vmax=0.599 µmol/min/mg enzyme with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  5. Vmax=0.196 µmol/min/mg enzyme with 2-ketopantoate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  6. Vmax=0.184 µmol/min/mg enzyme with 2-ketoisovalerate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  7. Vmax=0.168 µmol/min/mg enzyme with 2-ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  8. Vmax=0.05 µmol/min/mg enzyme with 2-ketovalerate as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  9. Vmax=0.021 µmol/min/mg enzyme with pyruvate as substrate (at pH 8 and 37 degrees Celsius)1 Publication

<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 annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 3 small subunit (ilvH), Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 1 small subunit (ilvN)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
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 annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 3 small subunit (ilvH), Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 1 small subunit (ilvN)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
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 ‘Function’ 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 sitei68NADPUniRule annotation1 Publication1
Binding sitei76NADPUniRule annotation1 Publication1 Publication1
Binding sitei78NADPUniRule annotation1 Publication1
<p>This subsection of the ‘Function’ 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 sitei132UniRule annotation1
Binding sitei158NADP; via amide nitrogenUniRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi217Magnesium 1UniRule annotation1 Publication1
Metal bindingi217Magnesium 2UniRule annotation1 Publication1
Metal bindingi221Magnesium 1UniRule annotation1
Metal bindingi389Magnesium 2UniRule annotation1 Publication1
Metal bindingi393Magnesium 2UniRule annotation1 Publication1
Binding sitei414SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi45 – 48NADPUniRule annotation1 Publication4
Nucleotide bindingi108 – 110NADPUniRule annotation1 Publication3

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: GO_Central
  • isoleucine biosynthetic process Source: EcoCyc
  • protein homotetramerization Source: EcoCyc
  • valine biosynthetic process Source: EcoCyc
View the complete GO annotation on QuickGO ...

<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 functionOxidoreductase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandMagnesium, Metal-binding, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:KETOLREDUCTOISOM-MONOMER
MetaCyc:KETOLREDUCTOISOM-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.86 2026

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 reductoisomerase (NADP(+))1 PublicationUniRule annotation (EC:1.1.1.86UniRule annotation4 Publications)
Short name:
KARI1 PublicationUniRule annotation
Alternative name(s):
Acetohydroxy-acid isomeroreductase1 PublicationUniRule annotation
Short name:
AHIR1 PublicationUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
Ketol-acid reductoisomerase type 21 PublicationUniRule annotation
Ketol-acid reductoisomerase type II1 PublicationUniRule 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
Name:ilvCUniRule annotation
Ordered Locus Names:b3774, JW3747
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10495 ilvC

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi68R → D: Inversion of cofactor specificity from NADPH to NADH; when associated with L-69, V-75 and D-76. 1 Publication1
Mutagenesisi68R → Q: 18-fold decrease of the catalytic efficiency and 3-fold decrease of the affinity for NADPH. 1 Publication1
Mutagenesisi69K → L: Does not significantly alter the affinity for NADPH. Slight increase of the catalytic efficiency. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, V-75 and D-76. 1 Publication1
Mutagenesisi71A → S: 7- and 2.5-fold increase of the reductoisomerase activity with NADH and NADPH, respectively. 1 Publication1
Mutagenesisi75K → Q: 13-fold decrease of the catalytic efficiency and 3-fold increase of the affinity for NADPH. 1 Publication1
Mutagenesisi75K → V: Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and D-76. 1 Publication1
Mutagenesisi76R → D: 3-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH. 1 Publication1
Mutagenesisi76R → D: Strong increase of catalytic efficiency and 2.5-fold increase of the affinity for NADH. 4-fold decrease of the catalytic efficiency and strong decrease of the affinity for NADPH. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and V-75. 1 Publication1
Mutagenesisi76R → Q: 20-fold decrease of the catalytic efficiency and 5-fold decrease of the affinity for NADPH. 1 Publication1
Mutagenesisi78S → D: 12-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH. 1 Publication1
Mutagenesisi110Q → V or A: 12- and 2-fold increase of the reductoisomerase activity with NADH and NADPH, respectively. 1 Publication1
Mutagenesisi132H → K: Loss of reductoisomerase activity. 1 Publication1
Mutagenesisi132H → Q: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 24-fold. 1 Publication1
Mutagenesisi155K → E or Q: Loss of reductoisomerase activity. 1 Publication1
Mutagenesisi155K → R: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 40-fold. 1 Publication1
Mutagenesisi213E → D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 48-fold. 1 Publication1
Mutagenesisi217D → E or N: Loss of reductoisomerase activity. 1 Publication1
Mutagenesisi221E → D or Q: Loss of reductoisomerase activity. 1 Publication1
Mutagenesisi389E → D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 4-fold. 1 Publication1
Mutagenesisi389E → Q: Loss of reductoisomerase activity. 1 Publication1
Mutagenesisi393E → D: Loss of reductoisomerase activity. The reductase activity with HMKB is nearly normal. 1 Publication1
Mutagenesisi414S → A: Loss of reductoisomerase activity. The isomerase activity decreases 15-fold. 1 Publication1
Mutagenesisi414S → T: Loss of reductoisomerase activity. The isomerase activity decreases 24-fold. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2366462

<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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001513092 – 491Ketol-acid reductoisomerase (NADP(+))Add BLAST490

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P05793

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P05793

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P05793

PRoteomics IDEntifications database

More...PRIDEi		P05793

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P05793

<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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

In the presence of acetohydroxybutyrate and acetolactate and by the activator IlvY.2 Publications

<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

Homotetramer.2 Publications

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4263331, 21 interactors

Protein interaction database and analysis system

More...IntActi		P05793, 4 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_3963

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P05793

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRLX-ray2.60A/B/C/D1-491[»]
3ULKX-ray2.30A/B1-491[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P05793

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P05793

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P05793

<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>Domaini15 – 208KARI N-terminal RossmannPROSITE-ProRule annotation1 PublicationAdd BLAST194
Domaini209 – 344KARI C-terminal knotted 1PROSITE-ProRule annotation1 PublicationAdd BLAST136
Domaini345 – 484KARI C-terminal knotted 2PROSITE-ProRule annotation1 PublicationAdd BLAST140

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105C6M Bacteria
COG0059 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000286135

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P05793

KEGG Orthology (KO)

More...KOi		K00053

Database for complete collections of gene phylogenies

More...PhylomeDBi		P05793

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1040.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00435 IlvC, 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
IPR036291 NAD(P)-bd_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR21371 PTHR21371, 2 hits

Pfam protein domain database

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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00465 ilvC, 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>.<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P05793-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANYFNTLNL RQQLAQLGKC RFMGRDEFAD GASYLQGKKV VIVGCGAQGL 
        60         70         80         90        100
NQGLNMRDSG LDISYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD 
       110        120        130        140        150
LVINLTPDKQ HSDVVRTVQP LMKDGAALGY SHGFNIVEVG EQIRKDITVV 
       160        170        180        190        200
MVAPKCPGTE VREEYKRGFG VPTLIAVHPE NDPKGEGMAI AKAWAAATGG 
       210        220        230        240        250
HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL VEEGTDPAYA 
       260        270        280        290        300
EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF 
       310        320        330        340        350
QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE TAPQYEGKIG 
       360        370        380        390        400
EQEYFDKGVL MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT 
       410        420        430        440        450
IARKRLYEMN VVISDTAEYG NYLFSYACVP LLKPFMAELQ PGDLGKAIPE 
       460        470        480        490 
GAVDNGQLRD VNEAIRSHAI EQVGKKLRGY MTDMKRIAVA G
Length:491
Mass (Da):54,069
Last modified:January 23, 2007 - v4
<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:i9CA34BA61C9AEBBA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti251E → K in AAA24029 (PubMed:3003115).Curated1

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
M11689 Genomic DNA Translation: AAA24029.1
M87049 Genomic DNA Translation: AAA67577.1
U00096 Genomic DNA Translation: AAC76779.1
AP009048 Genomic DNA Translation: BAE77523.1

Protein sequence database of the Protein Information Resource

More...PIRi		A65181 ISECKR

NCBI Reference Sequences

More...RefSeqi		NP_418222.1, NC_000913.3
WP_000024939.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76779; AAC76779; b3774
BAE77523; BAE77523; BAE77523

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948286

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3747
eco:b3774

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.3891

<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
M11689 Genomic DNA Translation: AAA24029.1
M87049 Genomic DNA Translation: AAA67577.1
U00096 Genomic DNA Translation: AAC76779.1
AP009048 Genomic DNA Translation: BAE77523.1
PIRiA65181 ISECKR
RefSeqiNP_418222.1, NC_000913.3
WP_000024939.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRLX-ray2.60A/B/C/D1-491[»]
3ULKX-ray2.30A/B1-491[»]
ProteinModelPortaliP05793
SMRiP05793
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263331, 21 interactors
IntActiP05793, 4 interactors
STRINGi316385.ECDH10B_3963

Chemistry databases

BindingDBiP05793
ChEMBLiCHEMBL2366462

2D gel databases

SWISS-2DPAGEiP05793

Proteomic databases

EPDiP05793
jPOSTiP05793
PaxDbiP05793
PRIDEiP05793

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76779; AAC76779; b3774
BAE77523; BAE77523; BAE77523
GeneIDi948286
KEGGiecj:JW3747
eco:b3774
PATRICifig|511145.12.peg.3891

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0490
EcoGeneiEG10495 ilvC

Phylogenomic databases

eggNOGiENOG4105C6M Bacteria
COG0059 LUCA
HOGENOMiHOG000286135
InParanoidiP05793
KOiK00053
PhylomeDBiP05793

Enzyme and pathway databases

UniPathwayi
UPA00047;UER00056

UPA00049;UER00060

BioCyciEcoCyc:KETOLREDUCTOISOM-MONOMER
MetaCyc:KETOLREDUCTOISOM-MONOMER
BRENDAi1.1.1.86 2026

Miscellaneous databases

EvolutionaryTraceiP05793

Protein Ontology

More...PROi		PR:P05793

Family and domain databases

Gene3Di1.10.1040.10, 1 hit
HAMAPiMF_00435 IlvC, 1 hit
InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR013328 6PGD_dom2
IPR013023 KARI
IPR000506 KARI_C
IPR013116 KARI_N
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR21371 PTHR21371, 2 hits
PfamiView protein in Pfam
PF01450 IlvC, 2 hits
PF07991 IlvN, 1 hit
SUPFAMiSSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00465 ilvC, 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...

<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 nameiILVC_ECOLI
<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: P05793
Secondary accession number(s): Q2M883
<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/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 172 of the entry and version 4 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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