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Protein

Formate-dependent phosphoribosylglycinamide formyltransferase

Gene

purT

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

Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. PurT is also able to cleave acetyl phosphate and carbamoyl phosphate to produce ATP with acetate and carbamate, respectively.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Kcat is 37.6 sec(-1) for transformylase activity (at pH 8). Kcat is 0.309 sec(-1) for acetate kinase activity (at pH 8).1 Publication
  1. KM=10.1 µM for GAR (at pH 8)2 Publications
  2. KM=45 µM for ATP (with formate)1 Publication
  3. KM=77.4 µM for ATP (with acetate at pH 8)2 Publications
  4. KM=319 µM for formate (at pH 8)2 Publications
  5. KM=3.68 mM for acetate (at pH 8)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 (formate route).UniRule annotation2 Publications
    Proteins known to be involved in this subpathway in this organism are:
    1. Formate-dependent phosphoribosylglycinamide formyltransferase (purT)
    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 (formate 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 sitei825'-phosphoribosylglycinamide2 Publications1
    Binding sitei114ATP2 Publications1
    Binding sitei155ATP2 Publications1
    Binding sitei203ATP2 Publications1
    <p>This subsection of the ‘Function’ 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 bindingi267Magnesium2 Publications1
    Metal bindingi279Magnesium2 Publications1
    Binding sitei2865'-phosphoribosylglycinamide2 Publications1
    Binding sitei3555'-phosphoribosylglycinamide2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi160 – 165ATP2 Publications6
    Nucleotide bindingi195 – 198ATP2 Publications4

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionTransferase
    Biological processPurine biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:GARTRANSFORMYL2-MONOMER
    MetaCyc:GARTRANSFORMYL2-MONOMER

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

    More...
    UniPathwayi
    UPA00074;UER00127

    <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:
    Formate-dependent phosphoribosylglycinamide formyltransferase1 Publication
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylase 21 Publication
    Formate-dependent GAR transformylase1 Publication (EC:2.1.2.-2 Publications)
    GAR transformylase 21 Publication
    Short name:
    GART 21 Publication
    Non-folate glycinamide ribonucleotide transformylase1 Publication
    Phosphoribosylglycinamide formyltransferase 21 Publication
    <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:purT1 Publication
    Ordered Locus Names:b1849, JW1838
    <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
    EG11809 purT

    <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>Mutagenesisi162G → I: Strong decrease in the reaction rate for the conversion of formate to FGAR and in the affinity for formate. 3- and 2-fold decrease in the affinity for ATP and GAR, respectively. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03434 3[N-Morpholino]Propane Sulfonic Acid
    DB02236 Glycinamide Ribonucleotide
    DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
    DB02930 Phosphothiophosphoric Acid-Adenylate Ester

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00000749562 – 392Formate-dependent phosphoribosylglycinamide formyltransferaseAdd BLAST391

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei179N6-acetyllysineUniRule annotation1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P33221

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

    More...
    PaxDbi
    P33221

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P33221

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P33221

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.1 Publication2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    ispAP229394EBI-553029,EBI-553011

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260365, 7 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10618N

    Protein interaction database and analysis system

    More...
    IntActi
    P33221, 7 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_1990

    <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

    1392
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1EYZX-ray1.75A/B1-392[»]
    1EZ1X-ray1.75A/B1-392[»]
    1KJ8X-ray1.60A/B2-392[»]
    1KJ9X-ray1.60A/B2-392[»]
    1KJIX-ray1.60A/B2-392[»]
    1KJJX-ray1.75A/B2-392[»]
    1KJQX-ray1.05A/B2-392[»]
    1NFEmodel-A1-392[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P33221

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

    More...
    SMRi
    P33221

    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
    P33221

    <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_and_domains_section">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>Domaini119 – 308ATP-graspUniRule annotationAdd BLAST190

    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>Regioni22 – 235'-phosphoribosylglycinamide binding2 Publications2
    Regioni362 – 3635'-phosphoribosylglycinamide binding2 Publications2

    <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 PurK/PurT family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108HH9 Bacteria
    COG0027 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000072820

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P33221

    KEGG Orthology (KO)

    More...
    KOi
    K08289

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P33221

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1490.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01643 PurT, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011761 ATP-grasp
    IPR003135 ATP-grasp_carboxylate-amine
    IPR013815 ATP_grasp_subdomain_1
    IPR016185 PreATP-grasp_dom_sf
    IPR005862 PurT
    IPR011054 Rudment_hybrid_motif

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02222 ATP-grasp, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51246 SSF51246, 1 hit
    SSF52440 SSF52440, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01142 purT, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50975 ATP_GRASP, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P33221-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM
    60 70 80 90 100
    HVAHRSHVIN MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN
    110 120 130 140 150
    VVPCARATKL TMNREGIRRL AAEELQLPTS TYRFADSESL FREAVADIGY
    160 170 180 190 200
    PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY AQQGGRAGAG RVIVEGVVKF
    210 220 230 240 250
    DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS PLALERAQEI
    260 270 280 290 300
    ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
    310 320 330 340 350
    ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI
    360 370 380 390
    RLFGKPEIDG SRRLGVALAT AESVVDAIER AKHAAGQVKV QG
    Length:392
    Mass (Da):42,434
    Last modified:January 23, 2007 - v3
    <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:i276B3883E7403EA9
    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
    L20897 Genomic DNA Translation: AAA23861.1
    U00096 Genomic DNA Translation: AAC74919.1
    AP009048 Genomic DNA Translation: BAA15657.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A54227

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416363.1, NC_000913.3
    WP_000173484.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74919; AAC74919; b1849
    BAA15657; BAA15657; BAA15657

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946368

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1838
    eco:b1849

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.400

    <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
    L20897 Genomic DNA Translation: AAA23861.1
    U00096 Genomic DNA Translation: AAC74919.1
    AP009048 Genomic DNA Translation: BAA15657.1
    PIRiA54227
    RefSeqiNP_416363.1, NC_000913.3
    WP_000173484.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EYZX-ray1.75A/B1-392[»]
    1EZ1X-ray1.75A/B1-392[»]
    1KJ8X-ray1.60A/B2-392[»]
    1KJ9X-ray1.60A/B2-392[»]
    1KJIX-ray1.60A/B2-392[»]
    1KJJX-ray1.75A/B2-392[»]
    1KJQX-ray1.05A/B2-392[»]
    1NFEmodel-A1-392[»]
    ProteinModelPortaliP33221
    SMRiP33221
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260365, 7 interactors
    DIPiDIP-10618N
    IntActiP33221, 7 interactors
    STRINGi316385.ECDH10B_1990

    Chemistry databases

    DrugBankiDB03434 3[N-Morpholino]Propane Sulfonic Acid
    DB02236 Glycinamide Ribonucleotide
    DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
    DB02930 Phosphothiophosphoric Acid-Adenylate Ester

    PTM databases

    iPTMnetiP33221

    Proteomic databases

    jPOSTiP33221
    PaxDbiP33221
    PRIDEiP33221

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74919; AAC74919; b1849
    BAA15657; BAA15657; BAA15657
    GeneIDi946368
    KEGGiecj:JW1838
    eco:b1849
    PATRICifig|1411691.4.peg.400

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1757
    EcoGeneiEG11809 purT

    Phylogenomic databases

    eggNOGiENOG4108HH9 Bacteria
    COG0027 LUCA
    HOGENOMiHOG000072820
    InParanoidiP33221
    KOiK08289
    PhylomeDBiP33221

    Enzyme and pathway databases

    UniPathwayi
    UPA00074;UER00127

    BioCyciEcoCyc:GARTRANSFORMYL2-MONOMER
    MetaCyc:GARTRANSFORMYL2-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP33221

    Protein Ontology

    More...
    PROi
    PR:P33221

    Family and domain databases

    Gene3Di3.30.1490.20, 1 hit
    HAMAPiMF_01643 PurT, 1 hit
    InterProiView protein in InterPro
    IPR011761 ATP-grasp
    IPR003135 ATP-grasp_carboxylate-amine
    IPR013815 ATP_grasp_subdomain_1
    IPR016185 PreATP-grasp_dom_sf
    IPR005862 PurT
    IPR011054 Rudment_hybrid_motif
    PfamiView protein in Pfam
    PF02222 ATP-grasp, 1 hit
    SUPFAMiSSF51246 SSF51246, 1 hit
    SSF52440 SSF52440, 1 hit
    TIGRFAMsiTIGR01142 purT, 1 hit
    PROSITEiView protein in PROSITE
    PS50975 ATP_GRASP, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    <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 nameiPURT_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: P33221
    <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: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: January 16, 2019
    This is version 175 of the entry and version 3 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. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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