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Entry version 136 (12 Aug 2020)
Sequence version 2 (29 Aug 2001)
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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
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.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 '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 0.8 sec(-1) for reductoisomerase activity with NADPH as substrate (at pH 7). Kcat is 0.1 sec(-1) for reductoisomerase activity with NADH as substrate (at pH 7).1 Publication
  1. KM=13 µM for NADPH (at pH 7)1 Publication
  2. KM=285 µM for NADH (at pH 7)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 large subunit (ilvB), Acetolactate synthase small subunit (ilvH)
    2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
    3. Dihydroxy-acid dehydratase (ilvD)
    4. Branched-chain-amino-acid aminotransferase (bcaT)
    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 large subunit (ilvB), Acetolactate synthase small subunit (ilvH)
    2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
    3. Dihydroxy-acid dehydratase (ilvD)
    4. Branched-chain-amino-acid aminotransferase (bcaT)
    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%5Fsection">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 sitei49NADPUniRule annotation1
    Binding sitei53NADPUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei108UniRule annotation1
    Binding sitei134NADP; via amide nitrogenUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi191Magnesium 1UniRule annotation1
    Metal bindingi191Magnesium 2UniRule annotation1
    Metal bindingi195Magnesium 1UniRule annotation1
    Metal bindingi227Magnesium 2UniRule annotation1
    Metal bindingi231Magnesium 2UniRule annotation1
    Binding sitei252SubstrateUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi26 – 29NADPUniRule annotation4
    Nucleotide bindingi83 – 86NADPUniRule annotation4

    <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 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
    LLAC272623:L0080-MONOMER

    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%5Fand%5Ftaxonomy%5Fsection">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 annotation1 Publication)
    Short name:
    KARI1 PublicationUniRule annotation
    Alternative name(s):
    Acetohydroxy-acid isomeroreductaseUniRule annotation
    Short name:
    AHIRUniRule annotation
    Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
    Ketol-acid reductoisomerase type 11 PublicationUniRule annotation
    Ketol-acid reductoisomerase type I1 PublicationUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:LL1226
    ORF Names:L0080
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri272623 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000002196 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi48V → L: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with P-49, L-52 and D-53. 1 Publication1
    Mutagenesisi49R → P: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with L-48, L-52 and D-53. 1 Publication1
    Mutagenesisi52K → L: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with L-48, P-49 and D-53. 1 Publication1
    Mutagenesisi53S → D: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold increase of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 4-fold increase of the catalytic efficiency for NADH; when associated with L-48, P-49 and L-52. 1 Publication1

    <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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001513181 – 340Ketol-acid reductoisomerase (NADP(+))Add BLAST340

    Proteomic databases

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

    More...
    PaxDbi
    Q02138

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    272623.L0080

    <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

    3D structure databases

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

    More...
    SMRi
    Q02138

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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%5Fand%5Fdomains%5Fsection">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>Domaini3 – 182KARI N-terminal RossmannPROSITE-ProRule annotationAdd BLAST180
    Domaini183 – 328KARI C-terminal knottedPROSITE-ProRule annotationAdd BLAST146

    <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
    COG0059, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_033821_0_1_9

    KEGG Orthology (KO)

    More...
    KOi
    K00053

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RAMFSWL

    Family and domain databases

    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
    IPR013023, KARI
    IPR000506, KARI_C
    IPR013116, KARI_N
    IPR014359, KARI_prok
    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, 1 hit
    PF07991, IlvN, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000116, IlvC_gammaproteo, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48179, SSF48179, 1 hit
    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, 1 hit
    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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    Q02138-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAVTMYYEDD VEVSALAGKQ IAVIGYGSQG HAHAQNLRDS GHNVIIGVRH
    60 70 80 90 100
    GKSFDKAKED GFETFEVGEA VAKADVIMVL APDELQQSIY EEDIKPNLKA
    110 120 130 140 150
    GSALGFAHGF NIHFGYIKVP EDVDVFMVAP KAPGHLVRRT YTEGFGTPAL
    160 170 180 190 200
    FVSHQNASGH AREIAMDWAK GIGCARVGII ETTFKEETEE DLFGEQAVLC
    210 220 230 240 250
    GGLTALVEAG FETLTEAGYA GELAYFEVLH EMKLIVDLMY EGGFTKMRQS
    260 270 280 290 300
    ISNTAEFGDY VTGPRIITDA VKKNMKLVLA DIQSGKFAQD FVDDFKAGRP
    310 320 330 340
    KLTAYREAAK NLEIEKIGAE LRKAMPFTQS GDDDAFKIYQ
    Length:340
    Mass (Da):37,211
    Last modified:August 29, 2001 - v2
    <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:i93E2FF206D7AFF2F
    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 conflicti270A → E in AAB81921 (PubMed:1400210).Curated1
    Sequence conflicti303T → I in AAB81921 (PubMed:1400210).Curated1
    Sequence conflicti321 – 340LRKAM…FKIYQ → HVKQCHSHNLVMTMPLKSIS NFSY in AAB81921 (PubMed:1400210).CuratedAdd BLAST20

    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
    U92974 Genomic DNA Translation: AAB81921.1
    AE005176 Genomic DNA Translation: AAK05324.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B86778
    S35140

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_267382.1, NC_002662.1
    WP_003131136.1, NC_002662.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAK05324; AAK05324; L0080

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    lla:L0080

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|272623.7.peg.1325

    <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
    U92974 Genomic DNA Translation: AAB81921.1
    AE005176 Genomic DNA Translation: AAK05324.1
    PIRiB86778
    S35140
    RefSeqiNP_267382.1, NC_002662.1
    WP_003131136.1, NC_002662.1

    3D structure databases

    SMRiQ02138
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi272623.L0080

    Proteomic databases

    PaxDbiQ02138

    Genome annotation databases

    EnsemblBacteriaiAAK05324; AAK05324; L0080
    KEGGilla:L0080
    PATRICifig|272623.7.peg.1325

    Phylogenomic databases

    eggNOGiCOG0059, Bacteria
    HOGENOMiCLU_033821_0_1_9
    KOiK00053
    OMAiRAMFSWL

    Enzyme and pathway databases

    UniPathwayiUPA00047;UER00056
    UPA00049;UER00060
    BioCyciLLAC272623:L0080-MONOMER

    Family and domain databases

    HAMAPiMF_00435, IlvC, 1 hit
    InterProiView protein in InterPro
    IPR008927, 6-PGluconate_DH-like_C_sf
    IPR013023, KARI
    IPR000506, KARI_C
    IPR013116, KARI_N
    IPR014359, KARI_prok
    IPR036291, NAD(P)-bd_dom_sf
    PANTHERiPTHR21371, PTHR21371, 1 hit
    PfamiView protein in Pfam
    PF01450, IlvC, 1 hit
    PF07991, IlvN, 1 hit
    PIRSFiPIRSF000116, IlvC_gammaproteo, 1 hit
    SUPFAMiSSF48179, SSF48179, 1 hit
    SSF51735, SSF51735, 1 hit
    TIGRFAMsiTIGR00465, ilvC, 1 hit
    PROSITEiView protein in PROSITE
    PS51851, KARI_C, 1 hit
    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 nameiILVC_LACLA
    <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: Q02138
    Secondary accession number(s): Q9CG82
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: August 29, 2001
    Last modified: August 12, 2020
    This is version 136 of the entry and version 2 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

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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