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Entry version 133 (07 Oct 2020)
Sequence version 2 (23 Jan 2007)
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Protein

CTP synthase

Gene

pyrG

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 ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.1 Publication2 Publications

Miscellaneous

CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.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 <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

Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate (PubMed:4550559). The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis (PubMed:11336655). Also activated by magnesium; the enzyme requires more Mg2+ for full catalytic activity than required simply to complex the nucleotide substrates (PubMed:8385490). Inhibited by the product CTP, via allosteric rather than competitive inhibition (PubMed:8385490, PubMed:16216072). Also inhibited by divalent metal ions such as copper and zinc (PubMed:8385490). Is potently inhibited by the intermediate analog inhibitor glutamate gamma-semialdehyde (PubMed:11336655).1 Publication3 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 13 sec(-1) with ammonia as substrate. kcat is 6.6 sec(-1) with L-glutamine as substrate (in the presence of 0.25 mM GTP).1 Publication
  1. KM=2.0 mM for ammonia1 Publication
  2. KM=0.30 mM for L-glutamine (in the presence of 0.25 mM GTP)1 Publication

    pH dependencei

    Optimum pH is 8.7.1 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: CTP biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. CTP synthase (pyrG), CTP synthase (pyrG)
    This subpathway is part of the pathway CTP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CTP from UDP, the pathway CTP biosynthesis via de novo pathway and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei14Allosteric inhibitor CTP; alternate1 Publication1
    Binding sitei14UTP; alternate1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi72MagnesiumCombined sources1 Publication1
    Binding sitei72ATPCombined sources1 Publication1
    Metal bindingi140MagnesiumCombined sources1 Publication1
    Binding sitei223Allosteric inhibitor CTP; alternateCombined sources1 Publication1
    Binding sitei223UTP; alternate1 Publication1
    Binding sitei352L-glutamine; via carbonyl oxygenUniRule annotation1
    <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 sitei379Nucleophile; for glutamine hydrolysis2 Publications1
    Binding sitei403L-glutamineUniRule annotation1
    Binding sitei470L-glutamine; via amide nitrogenUniRule annotation1
    Active sitei5151 Publication1
    Active sitei5171 Publication1

    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 bindingi15 – 20ATPCombined sources1 Publication6
    Nucleotide bindingi147 – 149Allosteric inhibitor CTPCombined sources1 Publication3
    Nucleotide bindingi187 – 192Allosteric inhibitor CTP; alternateCombined sources1 Publication6
    Nucleotide bindingi187 – 192UTP; alternate1 Publication6
    Nucleotide bindingi239 – 241ATPCombined sources1 Publication3

    <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 functionLigase
    Biological processPyrimidine biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.3.4.2, 2026

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

    More...
    UniPathwayi
    UPA00159;UER00277

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    C26.964

    <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:
    CTP synthase1 Publication (EC:6.3.4.23 Publications)
    Alternative name(s):
    Cytidine 5'-triphosphate synthase1 Publication
    Cytidine triphosphate synthetase1 Publication
    Short name:
    CTP synthetase1 Publication
    Short name:
    CTPS1 Publication
    UTP--ammonia ligase
    <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:pyrG1 Publication
    Ordered Locus Names:b2780, JW2751
    <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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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

    GO - Cellular componenti

    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

    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>Mutagenesisi349V → S: 30% increase in both glutamine-dependent and ammonia-dependent activities. 1 Publication1
    Mutagenesisi352G → P: Loss of glutamine-dependent activity, but no change in ammonia-dependent activity. 1 Publication1
    Mutagenesisi379C → A or S: Loss of glutamine-dependent activity, but no change in ammonia-dependent activity. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001381832 – 545CTP synthaseAdd BLAST544

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A7E5

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

    More...
    PaxDbi
    P0A7E5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A7E5

    2D gel databases

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

    More...
    SWISS-2DPAGEi
    P0A7E5

    <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

    Homodimer that associates to form homotetramer in the presence of ATP and UTP. The substrate nucleotides ATP and UTP act synergistically to promote oligomerization of CTPS from inactive dimers to active tetramers.

    1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4262298, 5 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10628N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A7E5, 8 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2780

    <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

    1545
    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
    P0A7E5

    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
    P0A7E5

    <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>Domaini291 – 542Glutamine amidotransferase type-1UniRule annotationAdd BLAST252

    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>Regioni2 – 266Amidoligase domain1 PublicationAdd BLAST265
    Regioni380 – 383L-glutamine bindingUniRule annotation4

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Sequence consists of two domains: the C-terminal glutamine amide transfer (GAT) domain catalyzes the hydrolysis of glutamine; the N-terminal synthase domain catalyzes the amination of UTP (PubMed:3514618, PubMed:3298209). Structure shows each subunit consists of three distinct segments: the N-terminal amidoligase (ALase) domain, which mediates oligomerization and contains the ALase active site where ATP and UTP substrates bind, and an interrupted helical interdomain linker segment that connects the ALase domain to the Type I glutamine amidotransferase (GATase) C-terminal domain, which generates ammonia via glutamine hydrolysis (PubMed:15157079). A gated channel that spans 25 Angstroms between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion; the channel is accessible to solvent at the base of a cleft adjoining the glutamine hydrolysis active site, providing an entry point for exogenous ammonia (PubMed:15157079).3 Publications

    <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 CTP synthase family.UniRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0504, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_011675_5_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A7E5

    KEGG Orthology (KO)

    More...
    KOi
    K01937

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A7E5

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01746, GATase1_CTP_Synthase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.880, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01227, PyrG, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029062, Class_I_gatase-like
    IPR004468, CTP_synthase
    IPR017456, CTP_synthase_N
    IPR017926, GATASE
    IPR033828, GATase1_CTP_Synthase
    IPR027417, P-loop_NTPase

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11550, PTHR11550, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF06418, CTP_synth_N, 1 hit
    PF00117, GATase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52317, SSF52317, 1 hit
    SSF52540, SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00337, PyrG, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51273, GATASE_TYPE_1, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A7E5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG
    60 70 80 90 100
    TMSPIQHGEV FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL
    110 120 130 140 150
    RKERRGDYLG ATVQVIPHIT NAIKERVLEG GEGHDVVLVE IGGTVGDIES
    160 170 180 190 200
    LPFLEAIRQM AVEIGREHTL FMHLTLVPYM AASGEVKTKP TQHSVKELLS
    210 220 230 240 250
    IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD VDSIYKIPGL
    260 270 280 290 300
    LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE
    310 320 330 340 350
    LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP
    360 370 380 390 400
    GGFGYRGVEG MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN
    410 420 430 440 450
    STEFVPDCKY PVVALITEWR DENGNVEVRS EKSDLGGTMR LGAQQCQLVD
    460 470 480 490 500
    DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ IEDAGLRVAG RSGDDQLVEI
    510 520 530 540
    IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ KRQAK
    Length:545
    Mass (Da):60,374
    Last modified:January 23, 2007 - v2
    <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:iFBB9E2E18FA355FC
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti338V → L in AAA24485 (PubMed:3514618).Curated1
    Sequence conflicti476M → S in AAA24485 (PubMed:3514618).Curated1

    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
    M12843 mRNA Translation: AAA24485.1
    U29580 Genomic DNA Translation: AAA69290.1
    U00096 Genomic DNA Translation: AAC75822.1
    AP009048 Genomic DNA Translation: BAE76854.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    H65059, SYECTP

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417260.1, NC_000913.3
    WP_000210878.1, NZ_STEB01000030.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75822; AAC75822; b2780
    BAE76854; BAE76854; BAE76854

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    49583355
    946116

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2751
    eco:b2780

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3955

    <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
    M12843 mRNA Translation: AAA24485.1
    U29580 Genomic DNA Translation: AAA69290.1
    U00096 Genomic DNA Translation: AAC75822.1
    AP009048 Genomic DNA Translation: BAE76854.1
    PIRiH65059, SYECTP
    RefSeqiNP_417260.1, NC_000913.3
    WP_000210878.1, NZ_STEB01000030.1

    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
    1S1MX-ray2.30A/B1-545[»]
    2AD5X-ray2.80A/B1-545[»]
    5TKVX-ray2.70A/B1-545[»]
    5U05electron microscopy7.90A/B/C/D1-545[»]
    5U3Celectron microscopy4.60A/B/C/D1-545[»]
    5U6Relectron microscopy5.70A/B/C/D1-545[»]
    SMRiP0A7E5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4262298, 5 interactors
    DIPiDIP-10628N
    IntActiP0A7E5, 8 interactors
    STRINGi511145.b2780

    Protein family/group databases

    MEROPSiC26.964

    2D gel databases

    SWISS-2DPAGEiP0A7E5

    Proteomic databases

    jPOSTiP0A7E5
    PaxDbiP0A7E5
    PRIDEiP0A7E5

    Genome annotation databases

    EnsemblBacteriaiAAC75822; AAC75822; b2780
    BAE76854; BAE76854; BAE76854
    GeneIDi49583355
    946116
    KEGGiecj:JW2751
    eco:b2780
    PATRICifig|1411691.4.peg.3955

    Organism-specific databases

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

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    EchoBASEi
    EB0803

    Phylogenomic databases

    eggNOGiCOG0504, Bacteria
    HOGENOMiCLU_011675_5_0_6
    InParanoidiP0A7E5
    KOiK01937
    PhylomeDBiP0A7E5

    Enzyme and pathway databases

    UniPathwayiUPA00159;UER00277
    BioCyciEcoCyc:CTPSYN-MONOMER
    MetaCyc:CTPSYN-MONOMER
    BRENDAi6.3.4.2, 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A7E5

    Protein Ontology

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    PROi
    PR:P0A7E5

    Family and domain databases

    CDDicd01746, GATase1_CTP_Synthase, 1 hit
    Gene3Di3.40.50.880, 1 hit
    HAMAPiMF_01227, PyrG, 1 hit
    InterProiView protein in InterPro
    IPR029062, Class_I_gatase-like
    IPR004468, CTP_synthase
    IPR017456, CTP_synthase_N
    IPR017926, GATASE
    IPR033828, GATase1_CTP_Synthase
    IPR027417, P-loop_NTPase
    PANTHERiPTHR11550, PTHR11550, 1 hit
    PfamiView protein in Pfam
    PF06418, CTP_synth_N, 1 hit
    PF00117, GATase, 1 hit
    SUPFAMiSSF52317, SSF52317, 1 hit
    SSF52540, SSF52540, 1 hit
    TIGRFAMsiTIGR00337, PyrG, 1 hit
    PROSITEiView protein in PROSITE
    PS51273, GATASE_TYPE_1, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    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 nameiPYRG_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: P0A7E5
    Secondary accession number(s): P08398, Q2MA52
    <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: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 7, 2020
    This is version 133 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
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