Skip Header

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

Pyruvate kinase

Gene

pyk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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

Catalyzes the phosphoryl transfer from phosphoenolpyruvate (PEP) to ADP to form pyruvate and ATP (PubMed:3711058, PubMed:15749828). Has a broad specificity for nucleoside diphosphates and can use ADP, GDP, IDP and UDP (PubMed:3711058).2 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

Protein has several cofactor binding sites:
  • Mg2+1 PublicationNote: Can also use manganese or cobalt.1 Publication
  • K+1 PublicationNote: Can also use ammonium ions.1 Publication

<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

Exhibits homotropic positive cooperativity for PEP (PubMed:3711058). Allosterically activated by ribose-5-phosphate, AMP and other nucleoside monophosphates but not by fructose-1,6-bisphosphate (PubMed:3711058).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 3,204 sec(-1) (in the presence of 0.1 mM ribose-5-phosphate).1 Publication
  1. KM=0.186 mM for PEP (in the presence of 0.1 mM ribose-5-phosphate)1 Publication

    pH dependencei

    Optimum pH is 7.2 at 30 degrees Celsius. Optimum pH is 6.8 at 60 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: glycolysis

    This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Curated
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Glyceraldehyde-3-phosphate dehydrogenase (gap)
    2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_1), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
    4. Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno)
    5. Pyruvate kinase (GT94_09925), Pyruvate kinase (GS458_2521), Pyruvate kinase (pyk), Pyruvate kinase (B4114_2369), Pyruvate kinase (AA904_05055), Pyruvate kinase (pyk)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    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 sitei33SubstrateBy similarity1
    <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 bindingi35PotassiumBy similarity1
    Metal bindingi37PotassiumBy similarity1
    Metal bindingi67PotassiumBy similarity1
    Metal bindingi68Potassium; via carbonyl oxygenBy similarity1
    Binding sitei221Substrate; via amide nitrogenBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei221Transition state stabilizerBy similarity1 Publication1
    Metal bindingi223MagnesiumBy similarity1
    Binding sitei246Substrate; via amide nitrogenBy similarity1
    Metal bindingi247MagnesiumBy similarity1
    Binding sitei247Substrate; via amide nitrogenBy similarity1
    Binding sitei279SubstrateBy similarity1

    <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

    <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 functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.1.40 623

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

    More...
    UniPathwayi
    UPA00109;UER00188

    <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:
    Pyruvate kinase1 Publication (EC:2.7.1.402 Publications)
    Short name:
    PKCurated
    Alternative name(s):
    ATP:pyruvate 2-O-phosphotransferase1 Publication
    <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:pyk
    <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>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    <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 identifieri1422 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    <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>Mutagenesisi9C → S: Slight decrease in activity; when associated with S-268. 1 Publication1
    Mutagenesisi221K → C, D, L or R: 10000 to 100000-fold decrease in activity. 1 Publication1
    Mutagenesisi268C → S: Slight decrease in activity; when associated with S-9. 1 Publication1
    Mutagenesisi308D → E: Reduced activity; when associated with Y-416. 1 Publication1
    Mutagenesisi416W → Y: Increased activity. 1 Publication1
    Mutagenesisi425H → A: Decreases affinity for allosteric activators. 1 Publication1
    Mutagenesisi435V → E, K or R: Does not affect kinetic properties. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001120551 – 587Pyruvate kinaseAdd BLAST587

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    The N-terminus is blocked.1 Publication

    <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

    <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

    1587
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q02499

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

    More...
    SMRi
    Q02499

    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
    Q02499

    <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

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Contains an extra C-terminal sequence (ECTS), which contains a highly conserved PEP binding motif.1 Publication

    <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 pyruvate kinase family.Curated
    In the C-terminal section; belongs to the PEP-utilizing enzyme family.Curated

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00288 Pyruvate_Kinase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.40.33.10, 1 hit
    3.40.1380.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008279 PEP-util_enz_mobile_dom
    IPR036637 Phosphohistidine_dom_sf
    IPR001697 Pyr_Knase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR011037 Pyrv_Knase-like_insert_dom_sf
    IPR018209 Pyrv_Knase_AS
    IPR015793 Pyrv_Knase_brl
    IPR015795 Pyrv_Knase_C
    IPR036918 Pyrv_Knase_C_sf
    IPR015806 Pyrv_Knase_insert_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11817 PTHR11817, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF00224 PK, 1 hit
    PF02887 PK_C, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01050 PYRUVTKNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50800 SSF50800, 1 hit
    SSF51621 SSF51621, 1 hit
    SSF52009 SSF52009, 1 hit
    SSF52935 SSF52935, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01064 pyruv_kin, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00110 PYRUVATE_KINASE, 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.

    Q02499-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN
    60 70 80 90 100
    IREAAKRTGR TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG
    110 120 130 140 150
    TPEKISVTYP SLIDDVSVGA KILLDDGLIS LEVNAVDKQA GEIVTTVLNG
    160 170 180 190 200
    GVLKNKKGVN VPGVKVNLPG ITEKDRADIL FGIRQGIDFI AASFVRRASD
    210 220 230 240 250
    VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG LMVARGDLGV
    260 270 280 290 300
    EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA
    310 320 330 340 350
    NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT
    360 370 380 390 400
    KESQTTITDA IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII
    410 420 430 440 450
    AVTSNEAVSR RLALVWGVYT KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD
    460 470 480 490 500
    LVVITAGVPV GETGSTNLMK VHVISDLLAK GQGIGRKSAF GKAVVAKTAE
    510 520 530 540 550
    EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS HAAVVGLSLG
    560 570 580
    IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL
    Length:587
    Mass (Da):62,318
    Last modified:October 1, 1994 - 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:i0794BA1A07BE0D5A
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAA40994 differs from that shown. Reason: Frameshift at position 486.Curated

    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
    D13095 Genomic DNA Translation: BAA02406.1
    X57859 Genomic DNA Translation: CAA40994.1 Frameshift.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S27330
    S29783

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_033014443.1, NZ_LUCR01000070.1

    <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
    D13095 Genomic DNA Translation: BAA02406.1
    X57859 Genomic DNA Translation: CAA40994.1 Frameshift.
    PIRiS27330
    S29783
    RefSeqiWP_033014443.1, NZ_LUCR01000070.1

    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
    2E28X-ray2.40A1-587[»]
    ProteinModelPortaliQ02499
    SMRiQ02499
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayi
    UPA00109;UER00188

    BRENDAi2.7.1.40 623

    Miscellaneous databases

    EvolutionaryTraceiQ02499

    Family and domain databases

    CDDicd00288 Pyruvate_Kinase, 1 hit
    Gene3Di2.40.33.10, 1 hit
    3.40.1380.20, 1 hit
    InterProiView protein in InterPro
    IPR008279 PEP-util_enz_mobile_dom
    IPR036637 Phosphohistidine_dom_sf
    IPR001697 Pyr_Knase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR011037 Pyrv_Knase-like_insert_dom_sf
    IPR018209 Pyrv_Knase_AS
    IPR015793 Pyrv_Knase_brl
    IPR015795 Pyrv_Knase_C
    IPR036918 Pyrv_Knase_C_sf
    IPR015806 Pyrv_Knase_insert_dom_sf
    PANTHERiPTHR11817 PTHR11817, 1 hit
    PfamiView protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF00224 PK, 1 hit
    PF02887 PK_C, 1 hit
    PRINTSiPR01050 PYRUVTKNASE
    SUPFAMiSSF50800 SSF50800, 1 hit
    SSF51621 SSF51621, 1 hit
    SSF52009 SSF52009, 1 hit
    SSF52935 SSF52935, 1 hit
    TIGRFAMsiTIGR01064 pyruv_kin, 1 hit
    PROSITEiView protein in PROSITE
    PS00110 PYRUVATE_KINASE, 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 nameiKPYK_GEOSE
    <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: Q02499
    <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: February 1, 1994
    Last sequence update: October 1, 1994
    Last modified: December 5, 2018
    This is version 121 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

    3D-structure, Direct protein sequencing

    Documents

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