Skip Header

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

UniProtKB - P77455 (PAAZ_ECOLI)

Entry version 150 (10 Feb 2021)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
Add a publicationFeedback
Protein

Bifunctional protein PaaZ

Gene

paaZ

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.3 Publications

<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 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=11 µM for oxepin-CoA (at 22 degrees Celsius and pH 8)1 Publication
  2. KM=56 µM for NADP (at 22 degrees Celsius and pH 8)1 Publication

    pH dependencei

    Optimum pH is 8.1 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: phenylacetate degradation

    This protein is involved in the pathway phenylacetate degradation, which is part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway phenylacetate degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei256By similarity1
    Active sitei295By 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    • phenylacetate catabolic process Source: UniProtKB
    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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:G6708-MONOMER
    MetaCyc:G6708-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.3.2.12, 2026

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

    More...    UniPathwayi    		UPA00930

    <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:
    Bifunctional protein PaaZ
    Including the following 2 domains:
    2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase (EC:3.3.2.12)
    Alternative name(s):
    Oxepin-CoA hydrolase
    3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC:1.2.1.911 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:paaZ
    Synonyms:maoC, ydbN
    Ordered Locus Names:b1387, JW1382
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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
    • UP000000318 <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
    • UP000000625 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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Disruption causes the conversion of phenylacetate (PA) into 2-hydroxyphenylacetate (2-HPA).1 Publication

    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>Mutagenesisi256E → Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA. 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_00000565811 – 681Bifunctional protein PaaZAdd BLAST681

    Proteomic databases

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

    More...    PaxDbi    		P77455

    PRoteomics IDEntifications database

    More...    PRIDEi    		P77455

    <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

    Activated by cAMP receptor protein (CRP) and integration host factor (IHF). Inhibited by PaaX.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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260176, 262 interactors

    Protein interaction database and analysis system

    More...    IntActi    		P77455, 3 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1387

    <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

    1681
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Small Angle Scattering Biological Data Bank

    More...    SASBDBi    		P77455

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

    More...    SMRi    		P77455

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		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>Domaini537 – 648MaoC-likeAdd BLAST112

    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>Regioni1 – 333Aldehyde dehydrogenaseAdd BLAST333

    <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

    In the N-terminal section; belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1012, Bacteria
    COG2030, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_025047_0_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P77455

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P77455

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.309.10, 1 hit
    3.40.605.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR016161, Ald_DH/histidinol_DH
    IPR016163, Ald_DH_C
    IPR016162, Ald_DH_N
    IPR015590, Aldehyde_DH_dom
    IPR029069, HotDog_dom_sf
    IPR002539, MaoC-like_dom
    IPR011966, PaaN-DH

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00171, Aldedh, 1 hit
    PF01575, MaoC_dehydratas, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53720, SSF53720, 1 hit
    SSF54637, SSF54637, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR02278, PaaN-DH, 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.

    P77455-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQQLASFLSG TWQSGRGRSR LIHHAISGEA LWEVTSEGLD MAAARQFAIE 
            60         70         80         90        100
    KGAPALRAMT FIERAAMLKA VAKHLLSEKE RFYALSAQTG ATRADSWVDI 
           110        120        130        140        150
    EGGIGTLFTY ASLGSRELPD DTLWPEDELI PLSKEGGFAA RHLLTSKSGV 
           160        170        180        190        200
    AVHINAFNFP CWGMLEKLAP TWLGGMPAII KPATATAQLT QAMVKSIVDS 
           210        220        230        240        250
    GLVPEGAISL ICGSAGDLLD HLDSQDVVTF TGSAATGQML RVQPNIVAKS 
           260        270        280        290        300
    IPFTMEADSL NCCVLGEDVT PDQPEFALFI REVVREMTTK AGQKCTAIRR 
           310        320        330        340        350
    IIVPQALVNA VSDALVARLQ KVVVGDPAQE GVKMGALVNA EQRADVQEKV 
           360        370        380        390        400
    NILLAAGCEI RLGGQADLSA AGAFFPPTLL YCPQPDETPA VHATEAFGPV 
           410        420        430        440        450
    ATLMPAQNQR HALQLACAGG GSLAGTLVTA DPQIARQFIA DAARTHGRIQ 
           460        470        480        490        500
    ILNEESAKES TGHGSPLPQL VHGGPGRAGG GEELGGLRAV KHYMQRTAVQ 
           510        520        530        540        550
    GSPTMLAAIS KQWVRGAKVE EDRIHPFRKY FEELQPGDSL LTPRRTMTEA 
           560        570        580        590        600
    DIVNFACLSG DHFYAHMDKI AAAESIFGER VVHGYFVLSA AAGLFVDAGV 
           610        620        630        640        650
    GPVIANYGLE SLRFIEPVKP GDTIQVRLTC KRKTLKKQRS AEEKPTGVVE 
           660        670        680 
    WAVEVFNQHQ TPVALYSILT LVARQHGDFV D
    Length:681
    Mass (Da):73,003
    Last modified:February 1, 1997 - 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:iA631B97AA37A1C3E
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti143L → V in strain: W. 1
    Natural varianti440A → T in strain: W. 1
    Natural varianti611S → N in strain: W. 1

    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
    		X97452 Genomic DNA Translation: CAA66089.1
    U00096 Genomic DNA Translation: AAC74469.1
    AP009048 Genomic DNA Translation: BAA14997.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		F64889

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415905.1, NC_000913.3
    WP_001186469.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74469; AAC74469; b1387
    BAA14997; BAA14997; BAA14997

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		57732127
    945954

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW1382
    eco:b1387

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.884

    <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
    		X97452 Genomic DNA Translation: CAA66089.1
    U00096 Genomic DNA Translation: AAC74469.1
    AP009048 Genomic DNA Translation: BAA14997.1
    PIRiF64889
    RefSeqiNP_415905.1, NC_000913.3
    WP_001186469.1, NZ_LN832404.1

    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
    6JQLelectron microscopy2.90A/B/C/D/E/F2-681[»]
    6JQMelectron microscopy3.30A/B/C/D/E/F2-681[»]
    6JQNelectron microscopy3.10A/B/C/D/E/F2-681[»]
    6JQOelectron microscopy3.10A/B/C/D/E/F2-681[»]
    SASBDBiP77455
    SMRiP77455
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260176, 262 interactors
    IntActiP77455, 3 interactors
    STRINGi511145.b1387

    Proteomic databases

    PaxDbiP77455
    PRIDEiP77455

    Genome annotation databases

    EnsemblBacteriaiAAC74469; AAC74469; b1387
    BAA14997; BAA14997; BAA14997
    GeneIDi57732127
    945954
    KEGGiecj:JW1382
    eco:b1387
    PATRICifig|1411691.4.peg.884

    Organism-specific databases

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

    More...    EchoBASEi    		EB3498

    Phylogenomic databases

    eggNOGiCOG1012, Bacteria
    COG2030, Bacteria
    HOGENOMiCLU_025047_0_0_6
    InParanoidiP77455
    PhylomeDBiP77455

    Enzyme and pathway databases

    UniPathwayiUPA00930
    BioCyciEcoCyc:G6708-MONOMER
    MetaCyc:G6708-MONOMER
    BRENDAi3.3.2.12, 2026

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P77455

    Family and domain databases

    Gene3Di3.40.309.10, 1 hit
    3.40.605.10, 1 hit
    InterProiView protein in InterPro
    IPR016161, Ald_DH/histidinol_DH
    IPR016163, Ald_DH_C
    IPR016162, Ald_DH_N
    IPR015590, Aldehyde_DH_dom
    IPR029069, HotDog_dom_sf
    IPR002539, MaoC-like_dom
    IPR011966, PaaN-DH
    PfamiView protein in Pfam
    PF00171, Aldedh, 1 hit
    PF01575, MaoC_dehydratas, 1 hit
    SUPFAMiSSF53720, SSF53720, 1 hit
    SSF54637, SSF54637, 1 hit
    TIGRFAMsiTIGR02278, PaaN-DH, 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 nameiPAAZ_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P77455
    Secondary accession number(s): O53009
    <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: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: February 10, 2021
    This is version 150 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, Reference proteome

    Documents

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