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Protein

Phosphoribosylglycinamide formyltransferase

Gene

purN

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 transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.UniRule annotation2 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 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 N10-(bromoacetyl)-5,8-dideazafolate.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5).1 Publication
  1. KM=77.5 µM for (6R)-N10-formyltetrahydrofolate (at pH 8.5)1 Publication
  2. KM=84.8 µM for (6R)-N10-formyltetrahydrofolate (at pH 7.5)1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route).UniRule annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Phosphoribosylglycinamide formyltransferase (purN)
    This subpathway is part of the pathway IMP biosynthesis via de novo 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 N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    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 sitei6410-formyltetrahydrofolateUniRule annotation1 Publication1
    Binding sitei10610-formyltetrahydrofolateUniRule annotation1 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 sitei108Proton donorUniRule annotation1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei144Raises pKa of active site HisUniRule annotation1 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

    • phosphoribosylglycinamide formyltransferase activity Source: EcoCyc

    GO - Biological processi

    • 'de novo' IMP biosynthetic process Source: GO_Central
    • cellular response to DNA damage stimulus Source: EcoliWiki

    <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 functionTransferase
    Biological processPurine biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

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

    More...
    UniPathwayi
    UPA00074;UER00126

    <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:
    Phosphoribosylglycinamide formyltransferaseUniRule annotation (EC:2.1.2.2UniRule annotation2 Publications)
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylaseUniRule annotation
    GAR transformylaseUniRule annotation
    Short name:
    GARTUniRule annotation
    <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:purN1 PublicationUniRule annotation
    Ordered Locus Names:b2500, JW2485
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10799 purN

    <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

    <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>Mutagenesisi70E → A: Loss of homodimerization. No effect on activity. 1 Publication1
    Mutagenesisi106N → A, D, G or S: Reduces activity about 2000-fold. 1 Publication1
    Mutagenesisi106N → E, H, I, K, L or Y: Loss of activity. 1 Publication1
    Mutagenesisi108H → A, G, M, N, Q or R: Loss of activity. 2 Publications1
    Mutagenesisi108H → E, S or T: Reduces activity about 1000-fold. 1 Publication1
    Mutagenesisi119H → A: No effect. 1 Publication1
    Mutagenesisi121H → Q: Increases Km for 5'-phosphoribosylglycinamide 4-fold. 1 Publication1
    Mutagenesisi135S → A or L: Reduces activity about 1000-fold. 1 Publication1
    Mutagenesisi137H → F or Q: No effect. 1 Publication1
    Mutagenesisi144D → A, E, S or Y: Reduces activity about 1000-fold. 2 Publications1
    Mutagenesisi144D → C, F, H, K, L, N, P, Q, R, T or V: Loss of activity. 2 Publications1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02236 Glycinamide Ribonucleotide
    DB02794 N-[5'-O-Phosphono-Ribofuranosyl]-2-[2-Hydroxy-2-[4-[Glutamic Acid]-N-Carbonylphenyl]-3-[2-Amino-4-Hydroxy-Quinazolin-6-Yl]-Propanylamino]-Acetamide

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000749431 – 212Phosphoribosylglycinamide formyltransferaseAdd BLAST212

    Proteomic databases

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

    More...
    PaxDbi
    P08179

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P08179

    <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

    Monomer. Homodimer below pH 6.8.5 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261440, 10 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P08179, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_2666

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P08179

    <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

    1212
    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
    P08179

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

    More...
    SMRi
    P08179

    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
    P08179

    <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>Regioni11 – 135'-phosphoribosylglycinamide bindingUniRule annotation2 Publications3
    Regioni89 – 9210-formyltetrahydrofolate bindingUniRule annotation2 Publications4
    Regioni140 – 14410-formyltetrahydrofolate binding2 Publications5
    Regioni170 – 1735'-phosphoribosylglycinamide binding2 Publications4

    <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 GART family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108V3E Bacteria
    COG0299 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000033575

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P08179

    KEGG Orthology (KO)

    More...
    KOi
    K11175

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P08179

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd08645 FMT_core_GART, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01930 PurN, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002376 Formyl_transf_N
    IPR036477 Formyl_transf_N_sf
    IPR004607 GART
    IPR001555 GART_AS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00551 Formyl_trans_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53328 SSF53328, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00639 PurN, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00373 GART, 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.

    P08179-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNIVVLISGN GSNLQAIIDA CKTNKIKGTV RAVFSNKADA FGLERARQAG
    60 70 80 90 100
    IATHTLIASA FDSREAYDRE LIHEIDMYAP DVVVLAGFMR ILSPAFVSHY
    110 120 130 140 150
    AGRLLNIHPS LLPKYPGLHT HRQALENGDE EHGTSVHFVT DELDGGPVIL
    160 170 180 190 200
    QAKVPVFAGD SEDDITARVQ TQEHAIYPLV ISWFADGRLK MHENAAWLDG
    210
    QRLPPQGYAA DE
    Length:212
    Mass (Da):23,238
    Last modified:August 1, 1988 - 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:iD38F326BCBA103FB
    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
    M13747 Genomic DNA Translation: AAA83899.1
    U00096 Genomic DNA Translation: AAC75553.1
    AP009048 Genomic DNA Translation: BAA16388.1
    AF293167 Genomic DNA Translation: AAG14584.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A28486 XYECGF

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416995.1, NC_000913.3
    WP_001028612.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75553; AAC75553; b2500
    BAA16388; BAA16388; BAA16388

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946973

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2485
    eco:b2500

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4238

    <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
    M13747 Genomic DNA Translation: AAA83899.1
    U00096 Genomic DNA Translation: AAC75553.1
    AP009048 Genomic DNA Translation: BAA16388.1
    AF293167 Genomic DNA Translation: AAG14584.1
    PIRiA28486 XYECGF
    RefSeqiNP_416995.1, NC_000913.3
    WP_001028612.1, 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
    1C2TX-ray2.10A/B1-212[»]
    1C3EX-ray2.10A/B1-209[»]
    1CDDX-ray2.80A/B1-212[»]
    1CDEX-ray2.50A/B/C/D1-212[»]
    1GARX-ray1.96A/B1-212[»]
    1GRCX-ray3.00A/B1-212[»]
    1JKXX-ray1.60A/B/C/D1-212[»]
    2GARX-ray1.80A1-212[»]
    3GARX-ray1.90A1-212[»]
    ProteinModelPortaliP08179
    SMRiP08179
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261440, 10 interactors
    IntActiP08179, 1 interactor
    STRINGi316385.ECDH10B_2666

    Chemistry databases

    BindingDBiP08179
    DrugBankiDB02236 Glycinamide Ribonucleotide
    DB02794 N-[5'-O-Phosphono-Ribofuranosyl]-2-[2-Hydroxy-2-[4-[Glutamic Acid]-N-Carbonylphenyl]-3-[2-Amino-4-Hydroxy-Quinazolin-6-Yl]-Propanylamino]-Acetamide

    Proteomic databases

    PaxDbiP08179
    PRIDEiP08179

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75553; AAC75553; b2500
    BAA16388; BAA16388; BAA16388
    GeneIDi946973
    KEGGiecj:JW2485
    eco:b2500
    PATRICifig|1411691.4.peg.4238

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0792
    EcoGeneiEG10799 purN

    Phylogenomic databases

    eggNOGiENOG4108V3E Bacteria
    COG0299 LUCA
    HOGENOMiHOG000033575
    InParanoidiP08179
    KOiK11175
    PhylomeDBiP08179

    Enzyme and pathway databases

    UniPathwayi
    UPA00074;UER00126

    BioCyciEcoCyc:GART-MONOMER
    MetaCyc:GART-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP08179

    Protein Ontology

    More...
    PROi
    PR:P08179

    Family and domain databases

    CDDicd08645 FMT_core_GART, 1 hit
    HAMAPiMF_01930 PurN, 1 hit
    InterProiView protein in InterPro
    IPR002376 Formyl_transf_N
    IPR036477 Formyl_transf_N_sf
    IPR004607 GART
    IPR001555 GART_AS
    PfamiView protein in Pfam
    PF00551 Formyl_trans_N, 1 hit
    SUPFAMiSSF53328 SSF53328, 1 hit
    TIGRFAMsiTIGR00639 PurN, 1 hit
    PROSITEiView protein in PROSITE
    PS00373 GART, 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 nameiPUR3_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: P08179
    <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: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: December 5, 2018
    This is version 164 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, Complete proteome, Direct protein sequencing, Reference proteome

    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
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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