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UniProtKB - Q46444 (QHED_COMTE)

Entry version 130 (12 Aug 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Quinohemoprotein alcohol dehydrogenase

Gene

qheDH

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
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 dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Methanol is not a substrate.1 Publication1 Publication

Caution

The oxidation form of Trp-543 is subject of controversy and could be the artifactual result of sample handling.1 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

Protein has several cofactor binding sites:

<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=5 µM for benzyl alcohol1 Publication
  2. KM=5 µM for butan-1-ol1 Publication
  3. KM=5 µM for pentan-1-ol1 Publication
  4. KM=5 µM for octan-1-ol1 Publication
  5. KM=40 µM for octanal1 Publication
  6. KM=60 µM for propan-1-ol1 Publication
  7. KM=100 µM for butyraldehyde1 Publication
  8. KM=200 µM for 6-aminohexan-1-ol1 Publication
  9. KM=280 µM for butan-1,3-diol1 Publication
  10. KM=900 µM for acetaldehyde1 Publication
  11. KM=3 mM for formaldehyde1 Publication
  12. KM=5 mM for ethanol1 Publication

    pH dependencei

    Optimum pH is 7.7.1 Publication

    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 sitei101Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei153Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei198Pyrroloquinoline quinoneCombined sources1 Publication1
    <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 bindingi216CalciumCombined sources1 Publication1
    Binding sitei274Pyrroloquinoline quinoneCombined sources1 Publication1
    Metal bindingi294CalciumCombined sources1 Publication1
    <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 sitei339Proton acceptor1 Publication1
    Metal bindingi339CalciumCombined sources1 Publication1
    Binding sitei366Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei575Pyrroloquinoline quinone; via amide nitrogenCombined sources1 Publication1
    Binding sitei635Heme c (covalent)Combined sources1 Publication1
    Binding sitei638Heme c (covalent)Combined sources1 Publication1
    Metal bindingi639Iron (heme axial ligand); via tele nitrogenCombined sources1 Publication1
    Metal bindingi678Iron (heme axial ligand)Combined sources1 Publication1

    <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

    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
    LigandCalcium, Heme, Iron, Metal-binding, PQQ

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:MONOMER-15520

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.1.9.1, 1590

    <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:
    Quinohemoprotein alcohol dehydrogenase1 Publication (EC:1.1.9.11 Publication)
    Short name:
    QH-ADH1 Publication
    Alternative name(s):
    Alcohol dehydrogenase (azurin)Curated
    PQQ-containing alcohol dehydrogenase1 Publication
    PQQ-dependent ADH1 Publication
    Quinohaemoprotein ethanol dehydrogenase type I1 Publication
    Short name:
    QH-EDHI1 Publication
    <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:qheDH1 Publication
    <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>OrganismiComamonas testosteroni (Pseudomonas testosteroni)
    <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 identifieri285 [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 lineageiBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

    <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

    Complete GO annotation on QuickGO ...

    Keywords - Cellular componenti

    Periplasm

    <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

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB03051, (S)-2-Tetrahydrofuroic acid
    DB03679, 2-Hydroxy-Tryptophan
    DB03317, Ferroheme C
    DB03205, Pyrroloquinoline Quinone

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 312 PublicationsAdd BLAST31
    <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_000002556332 – 708Quinohemoprotein alcohol dehydrogenaseAdd BLAST677

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi147 ↔ 148Combined sources1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    In the crystallographic structures Trp-543 is oxidized to 2'-hydroxytryptophan.1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q46444

    <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

    By ethanol and butanol.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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    1 Publication

    <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

    1708
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...    SMRi    		Q46444

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		Q46444

    <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>Domaini619 – 708Cytochrome cPROSITE-ProRule annotationAdd BLAST90

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni214 – 215Pyrroloquinoline quinone bindingCombined sources1 Publication2
    Regioni425 – 426Pyrroloquinoline quinone bindingCombined sources1 Publication2

    <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 bacterial PQQ dehydrogenase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KEGG Orthology (KO)

    More...    KOi    		K17760

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.760.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR009056, Cyt_c-like_dom
    IPR036909, Cyt_c-like_dom_sf
    IPR018391, PQQ_beta_propeller_repeat
    IPR017512, PQQ_MeOH/EtOH_DH
    IPR002372, PQQ_repeat
    IPR011047, Quinoprotein_ADH-like_supfam
    IPR001479, Quinoprotein_DH_CS

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF13442, Cytochrome_CBB3, 1 hit
    PF13360, PQQ_2, 2 hits

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00564, PQQ, 5 hits

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF46626, SSF46626, 1 hit
    SSF50998, SSF50998, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR03075, PQQ_enz_alc_DH, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00364, BACTERIAL_PQQ_2, 1 hit
    PS51007, CYTC, 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.

    <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 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.

    Q46444-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MERLIDNSHG WPGRMVWLLA ACLGSAAAFA QTGPAAQAAA AVQRVDGDFI 
            60         70         80         90        100
    RANAARTPDW PTIGVDYAET RYSRLDQINA ANVKDLGLAW SYNLESTRGV 
           110        120        130        140        150
    EATPVVVDGI MYVSASWSVV HAIDTRTGNR IWTYDPQIDR STGFKGCCDV 
           160        170        180        190        200
    VNRGVALWKG KVYVGAWDGR LIALDAATGK EVWHQNTFEG QKGSLTITGA 
           210        220        230        240        250
    PRVFKGKVII GKRGAEYGVR GYITAYDAET GERKWRWFSV PGDPSKPFED 
           260        270        280        290        300
    ESMKRAARTW DPSGKWWEAG GGGTMWDSMT FDAELNTMYV GTGNGSPWSH 
           310        320        330        340        350
    KVRSPKGGDN LYLASIVALD PDTGKYKWHY QETPGDNWDY TSTQPMILAD 
           360        370        380        390        400
    IKIAGKPRKV ILHAPKNGFF FVLDRTNGKF ISAKNFVPVN WASGYDKHGK 
           410        420        430        440        450
    PIGIAAARDG SKPQDAVPGP YGAHNWHPMS FNPQTGLVYL PAQNVPVNLM 
           460        470        480        490        500
    DDKKWEFNQA GPGKPQSGTG WNTAKFFNAE PPKSKPFGRL LAWDPVAQKA 
           510        520        530        540        550
    AWSVEHVSPW NGGTLTTAGN VVFQGTADGR LVAYHAATGE KLWEAPTGTG 
           560        570        580        590        600
    VVAAPSTYMV DGRQYVSVAV GWGGVYGLAA RATERQGPGT VYTFVVAGKA 
           610        620        630        640        650
    RMPEFVAQRT GQLLQGVKYD PAKVEAGTML YVANCVFCHG VPGVDRGGNI 
           660        670        680        690        700
    PNLGYMDASY IENLPNFVFK GPAMVRGMPD FTGKLSGDDV ESLKAFIQGT 

    ADAIRPKP
    Length:708
    Mass (Da):76,823
    Last modified:November 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i99AB54BDD6ACCAB3
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		X81880 Genomic DNA Translation: CAA57464.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S62366, S52317

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ag:CAA57464

    <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
    		X81880 Genomic DNA Translation: CAA57464.1
    PIRiS62366, S52317

    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
    1KB0X-ray1.44A32-708[»]
    SMRiQ46444
    ModBaseiSearch...
    PDBe-KBiSearch...

    Chemistry databases

    DrugBankiDB03051, (S)-2-Tetrahydrofuroic acid
    DB03679, 2-Hydroxy-Tryptophan
    DB03317, Ferroheme C
    DB03205, Pyrroloquinoline Quinone

    Proteomic databases

    PRIDEiQ46444

    Genome annotation databases

    KEGGiag:CAA57464

    Phylogenomic databases

    KOiK17760

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15520
    BRENDAi1.1.9.1, 1590

    Miscellaneous databases

    EvolutionaryTraceiQ46444

    Family and domain databases

    Gene3Di1.10.760.10, 1 hit
    InterProiView protein in InterPro
    IPR009056, Cyt_c-like_dom
    IPR036909, Cyt_c-like_dom_sf
    IPR018391, PQQ_beta_propeller_repeat
    IPR017512, PQQ_MeOH/EtOH_DH
    IPR002372, PQQ_repeat
    IPR011047, Quinoprotein_ADH-like_supfam
    IPR001479, Quinoprotein_DH_CS
    PfamiView protein in Pfam
    PF13442, Cytochrome_CBB3, 1 hit
    PF13360, PQQ_2, 2 hits
    SMARTiView protein in SMART
    SM00564, PQQ, 5 hits
    SUPFAMiSSF46626, SSF46626, 1 hit
    SSF50998, SSF50998, 1 hit
    TIGRFAMsiTIGR03075, PQQ_enz_alc_DH, 1 hit
    PROSITEiView protein in PROSITE
    PS00364, BACTERIAL_PQQ_2, 1 hit
    PS51007, CYTC, 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 nameiQHED_COMTE
    <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: Q46444
    <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: January 17, 2003
    Last sequence update: November 1, 1996
    Last modified: August 12, 2020
    This is version 130 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry 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
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