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UniProtKB - P0A9M2 (HPRT_ECOLI)

Entry version 125 (07 Apr 2021)
Sequence version 1 (19 Jul 2005)
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Protein

Hypoxanthine phosphoribosyltransferase

Gene

hpt

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

Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine.1 Publication

Miscellaneous

E.coli cells express two distinct 6-oxopurine PRTases, with very different specificities for hypoxanthine, guanine, and xanthine. Salvage enzymes allow a more energy efficient synthesis of purine nucleoside monophosphates compared with the de novo pathway. The kinetic analysis suggests that E.coli HPRT is mainly responsible for the synthesis of IMP and that XGPRT primarily salvages guanine and xanthine.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

Mg2+1 Publication

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

Inhibited by the product IMP (PubMed:12070315). Highly inhibited by nucleoside phosphonates, which are product analogs (PubMed:23927482, Ref. 6).3 Publications

<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 59.0 sec(-1) with hypoxanthine as substrate. kcat is 10.2 sec(-1) with guanine as substrate. kcat is 0.008 sec(-1) with xanthine as substrate (at pH 8.5 and 25 degrees Celsius).1 Publication
  1. KM=12.5 µM for hypoxanthine (at pH 8.5 and 25 degrees Celsius)1 Publication
  2. KM=294 µM for guanine (at pH 8.5 and 25 degrees Celsius)1 Publication
  3. KM=25 µM for xanthine (at pH 8.5 and 25 degrees Celsius)1 Publication
  4. KM=192 µM for 5-phospho-alpha-D-ribose 1-diphosphate (at pH 8.5 and 25 degrees Celsius)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: IMP biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes IMP from hypoxanthine.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Hypoxanthine phosphoribosyltransferase (FAZ83_06800), Hypoxanthine phosphoribosyltransferase (hpt)
    This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from hypoxanthine, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi99MagnesiumCombined sources1 Publication1
    <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 sitei99IMP or GMPCombined sources1 Publication1
    Metal bindingi100MagnesiumCombined 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 sitei103Proton acceptor1 Publication1
    Binding sitei131IMP or GMPCombined sources1 Publication1
    Binding sitei159GMP; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei165DiphosphateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi103 – 108IMP or GMPCombined sources1 Publication6

    <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

    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 functionGlycosyltransferase, Transferase
    Biological processPurine salvage
    LigandMagnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

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

    More...    UniPathwayi    		UPA00591;UER00648

    <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:
    Hypoxanthine phosphoribosyltransferase1 Publication (EC:2.4.2.81 Publication)
    Short name:
    HPRT1 Publication
    Alternative name(s):
    6-oxopurine phosphoribosyltransferase1 Publication
    Short name:
    6-oxopurine PRTase1 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:hpt
    Ordered Locus Names:b0125, JW5009
    <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 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

    Keywords - Cellular componenti

    Cytoplasm

    <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    		DB04566, Inosinic Acid

    <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_00001396321 – 178Hypoxanthine phosphoribosyltransferaseAdd BLAST178

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A9M2

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

    More...    PaxDbi    		P0A9M2

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A9M2

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...    SWISS-2DPAGEi    		P0A9M2

    <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

    Homotetramer.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4261679, 26 interactors
    850970, 3 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-47994N

    Protein interaction database and analysis system

    More...    IntActi    		P0A9M2, 5 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0125

    <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

    1178
    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    		P0A9M2

    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    		P0A9M2

    <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

    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>Regioni43 – 44DiphosphateBy similarity2

    <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 purine/pyrimidine phosphoribosyltransferase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0634, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_073615_0_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A9M2

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A9M2

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd06223, PRTases_typeI, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.2020, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR005904, Hxn_phspho_trans
    IPR000836, PRibTrfase_dom
    IPR029057, PRTase-like

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00156, Pribosyltran, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53271, SSF53271, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01203, HGPRTase, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00103, PUR_PYR_PR_TRANSFER, 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.

    P0A9M2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSDMVLVG LLRGSFMFMA 
            60         70         80         90        100
    DLCREVQVSH EVDFMTASSY GSGMSTTRDV KILKDLDEDI RGKDVLIVED 
           110        120        130        140        150
    IIDSGNTLSK VREILSLREP KSLAICTLLD KPSRREVNVP VEFIGFSIPD 
           160        170 
    EFVVGYGIDY AQRYRHLPYI GKVILLDE
    Length:178
    Mass (Da):20,115
    Last modified:July 19, 2005 - 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:iE1A75EB68231DC32
    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
    		U00096 Genomic DNA Translation: AAC73236.2
    AP009048 Genomic DNA Translation: BAB96700.2

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414667.4, NC_000913.3
    WP_000683335.1, NZ_STEB01000010.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73236; AAC73236; b0125
    BAB96700; BAB96700; BAB96700

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		58463620
    946624

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW5009
    eco:b0125

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2157

    <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
    		U00096 Genomic DNA Translation: AAC73236.2
    AP009048 Genomic DNA Translation: BAB96700.2
    RefSeqiNP_414667.4, NC_000913.3
    WP_000683335.1, NZ_STEB01000010.1

    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
    1G9SX-ray2.80A/B1-178[»]
    1G9TX-ray2.80A/B1-178[»]
    1GRVX-ray2.90A/B1-178[»]
    5KNRX-ray2.86A/B1-178[»]
    5KNSX-ray2.79A/B1-178[»]
    5KNTX-ray2.55A/B1-178[»]
    5KNUX-ray2.81A/B1-178[»]
    5KNVX-ray2.86A/B1-178[»]
    5KNXX-ray2.40A/B1-178[»]
    SMRiP0A9M2
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4261679, 26 interactors
    850970, 3 interactors
    DIPiDIP-47994N
    IntActiP0A9M2, 5 interactors
    STRINGi511145.b0125

    Chemistry databases

    DrugBankiDB04566, Inosinic Acid

    2D gel databases

    SWISS-2DPAGEiP0A9M2

    Proteomic databases

    jPOSTiP0A9M2
    PaxDbiP0A9M2
    PRIDEiP0A9M2

    Genome annotation databases

    EnsemblBacteriaiAAC73236; AAC73236; b0125
    BAB96700; BAB96700; BAB96700
    GeneIDi58463620
    946624
    KEGGiecj:JW5009
    eco:b0125
    PATRICifig|1411691.4.peg.2157

    Organism-specific databases

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

    More...    EchoBASEi    		EB4143

    Phylogenomic databases

    eggNOGiCOG0634, Bacteria
    HOGENOMiCLU_073615_0_0_6
    InParanoidiP0A9M2
    PhylomeDBiP0A9M2

    Enzyme and pathway databases

    UniPathwayiUPA00591;UER00648
    BioCyciEcoCyc:HYPOXANPRIBOSYLTRAN-MONOMER
    MetaCyc:HYPOXANPRIBOSYLTRAN-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP0A9M2

    Protein Ontology

    More...    PROi    		PR:P0A9M2

    Family and domain databases

    CDDicd06223, PRTases_typeI, 1 hit
    Gene3Di3.40.50.2020, 1 hit
    InterProiView protein in InterPro
    IPR005904, Hxn_phspho_trans
    IPR000836, PRibTrfase_dom
    IPR029057, PRTase-like
    PfamiView protein in Pfam
    PF00156, Pribosyltran, 1 hit
    SUPFAMiSSF53271, SSF53271, 1 hit
    TIGRFAMsiTIGR01203, HGPRTase, 1 hit
    PROSITEiView protein in PROSITE
    PS00103, PUR_PYR_PR_TRANSFER, 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 nameiHPRT_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: P0A9M2
    Secondary accession number(s): P36766
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: April 7, 2021
    This is version 125 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
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