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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

zwf

Organism
Leuconostoc mesenteroides
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 oxidation of glucose 6-phosphate to 6-phosphogluconolactone. Can utilize either NADP+ or NAD+.UniRule annotation4 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 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

  1. KM=114 µM for glucose 6-phosphate (with NADP)2 Publications
  2. KM=69 µM for glucose 6-phosphate (with NAD)2 Publications
  3. KM=8.0 µM for NADP2 Publications
  4. KM=160 µM for NAD2 Publications

    pH dependencei

    Optimum pH is 5.4-8.9.2 Publications

    <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: pentose phosphate pathway

    This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Glucose-6-phosphate 1-dehydrogenase (zwf), Glucose-6-phosphate 1-dehydrogenase (zwf), Glucose-6-phosphate 1-dehydrogenase (zwf)
    2. no protein annotated in this organism
    3. 6-phosphogluconate dehydrogenase, decarboxylating (gnd)
    This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway 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 sitei47NADPUniRule annotation3 Publications1
    Binding sitei149NADPUniRule annotation1 Publication1
    Binding sitei179Substrate1 Publication1
    Binding sitei183Substrate1 Publication1
    Binding sitei217Substrate1 Publication1
    Binding sitei236Substrate1 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 sitei241Proton acceptorUniRule annotation1 Publication1
    Binding sitei339Substrate1 Publication1
    Binding sitei344Substrate1 Publication1

    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 bindingi13 – 20NADPUniRule annotation3 Publications8
    Nucleotide bindingi86 – 87NADPUniRule annotation3 Publications2

    <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 processCarbohydrate metabolism, Glucose metabolism
    LigandNAD, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-13060

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.363 839

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P11411

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

    More...
    UniPathwayi
    UPA00115;UER00408

    <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:
    Glucose-6-phosphate 1-dehydrogenaseUniRule annotation (EC:1.1.1.3635 Publications)
    Short name:
    G6PDUniRule annotation
    Alternative name(s):
    Glucose-6-phosphate dehydrogenase (NAD(P)(+))Curated
    <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:zwfUniRule annotation
    <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>OrganismiLeuconostoc mesenteroides
    <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 identifieri1245 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeLeuconostoc

    <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>Mutagenesisi15T → A: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi15T → S: Decreases catalytic efficiency toward glucose 6-phosphate (with NAD). 1 Publication1
    Mutagenesisi22K → E: Almost loss of activity. 2 Publications1
    Mutagenesisi22K → Q: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 2 Publications1
    Mutagenesisi22K → R: Decreases catalytic efficiency toward glucose 6-phosphate. 2 Publications1
    Mutagenesisi47R → A: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi48Q → A or E: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi150P → G or V: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi178D → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi179H → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi180Y → F: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi183K → Q or R: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi241H → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi344K → Q or R: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi375D → Q: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi416Y → F: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1741173

    Drug and drug target database

    More...
    DrugBanki
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB04122 beta-D-glucose 6-phosphate
    DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

    <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 methionineiRemoved
    <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_00000681252 – 486Glucose-6-phosphate 1-dehydrogenaseAdd BLAST485

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11411

    <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.2 Publications

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P11411

    <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

    1486
    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
    P11411

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

    More...
    SMRi
    P11411

    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
    P11411

    <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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the glucose-6-phosphate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K00036

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00966 G6PD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001282 G6P_DH
    IPR019796 G6P_DH_AS
    IPR022675 G6P_DH_C
    IPR022674 G6P_DH_NAD-bd
    IPR036291 NAD(P)-bd_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR23429 PTHR23429, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02781 G6PD_C, 1 hit
    PF00479 G6PD_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000110 G6PD, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00079 G6PDHDRGNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00871 zwf, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00069 G6P_DEHYDROGENASE, 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.

    P11411-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL
    60 70 80 90 100
    NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI
    110 120 130 140 150
    EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEKP
    160 170 180 190 200
    FGTSYDTAAE LQNDLENAFD DNQLFRIDHY LGKEMVQNIA ALRFGNPIFD
    210 220 230 240 250
    AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN HTMQIVGWLA
    260 270 280 290 300
    MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP
    310 320 330 340 350
    YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI
    360 370 380 390 400
    VFKAGTFNFG SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL
    410 420 430 440 450
    GWTVSDEDKK NTPEPYERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV
    460 470 480
    YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG
    Length:486
    Mass (Da):54,441
    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:iAA43433F83ED091D
    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 conflicti154 – 156SYD → HYI AA sequence (PubMed:3100332).Curated3
    Sequence conflicti165L → F AA sequence (PubMed:3100332).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
    M64446 Genomic DNA Translation: AAA25265.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A39864

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAA25265

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M64446 Genomic DNA Translation: AAA25265.1
    PIRiA39864

    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
    1DPGX-ray2.00A/B2-486[»]
    1E77X-ray2.69A2-486[»]
    1E7MX-ray2.54A2-486[»]
    1E7YX-ray2.48A2-486[»]
    1H93X-ray2.20A2-486[»]
    1H94X-ray2.50A2-486[»]
    1H9AX-ray2.16A2-486[»]
    1H9BX-ray2.40A2-486[»]
    2DPGX-ray2.50A2-486[»]
    ProteinModelPortaliP11411
    SMRiP11411
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP11411
    ChEMBLiCHEMBL1741173
    DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB04122 beta-D-glucose 6-phosphate
    DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

    Proteomic databases

    PRIDEiP11411

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA25265

    Phylogenomic databases

    KOiK00036

    Enzyme and pathway databases

    UniPathwayi
    UPA00115;UER00408

    BioCyciMetaCyc:MONOMER-13060
    BRENDAi1.1.1.363 839
    SABIO-RKiP11411

    Miscellaneous databases

    EvolutionaryTraceiP11411

    Family and domain databases

    HAMAPiMF_00966 G6PD, 1 hit
    InterProiView protein in InterPro
    IPR001282 G6P_DH
    IPR019796 G6P_DH_AS
    IPR022675 G6P_DH_C
    IPR022674 G6P_DH_NAD-bd
    IPR036291 NAD(P)-bd_dom_sf
    PANTHERiPTHR23429 PTHR23429, 1 hit
    PfamiView protein in Pfam
    PF02781 G6PD_C, 1 hit
    PF00479 G6PD_N, 1 hit
    PIRSFiPIRSF000110 G6PD, 1 hit
    PRINTSiPR00079 G6PDHDRGNASE
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR00871 zwf, 1 hit
    PROSITEiView protein in PROSITE
    PS00069 G6P_DEHYDROGENASE, 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 nameiG6PD_LEUME
    <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: P11411
    <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: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 136 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, 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
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