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Entry version 34 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
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Protein

CTP synthase

Gene

pyrG

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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. Is essential for M.tuberculosis growth in vitro and ex vivo (PubMed:26097035). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).UniRule annotation1 Publication

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.UniRule annotation

<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 <a href="http://www.uniprot.org/help/function_section">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. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition (By similarity). Is inhibited by the EthA-activated metabolites of compounds 7947882 (5-methyl-N-(4-nitrophenyl)thiophene-2-carboxamide) and 7904688 (3-phenyl-N-[(4-piperidin-1-ylphenyl)carbamothioyl]propanamide), that have been shown to have anti-tubercular activity against M.tuberculosis in its replicating, non-replicating, and intracellular states; active metabolites of 7947882 correspond to the S-dioxide and S-monoxide derivatives (PubMed:26097035). One active metabolite was shown to behave as a competitive inhibitor toward the ATP-binding site of PyrG (PubMed:26097035). Direct inhibition of PyrG decreases CTP levels, leading to disruption of the nucleotide metabolic network, characterized by increased levels of several intermediates in the biosynthesis of pyrimidines and purines (PubMed:26097035).UniRule annotation1 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 22.9 sec(-1).1 Publication
  1. KM=0.18 mM for ATP1 Publication
  2. KM=0.14 mM for UTP1 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: 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)
    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_section">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 sitei20Allosteric inhibitor CTP; alternateBy similarity1 Publication1
    Binding sitei20UTP; alternate1 Publication1
    Binding sitei46ATP1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi78MagnesiumUniRule annotation1
    Binding sitei78ATP1 Publication1
    Metal bindingi152MagnesiumUniRule annotation1
    Binding sitei235Allosteric inhibitor CTP; alternateUniRule annotation1
    Binding sitei235UTP; alternateUniRule annotation1
    Binding sitei253ATP; via amide nitrogen1 Publication1
    Binding sitei366L-glutamine; via carbonyl oxygenUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei393Nucleophile; for glutamine hydrolysisUniRule annotation1 Publication1
    Binding sitei416L-glutamineUniRule annotation1
    Binding sitei477L-glutamine; via amide nitrogenUniRule annotation1
    Active sitei524UniRule annotation1 Publication1
    Active sitei526UniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi21 – 26ATP1 Publication6
    Nucleotide bindingi159 – 161Allosteric inhibitor CTPBy similarity1 Publication3
    Nucleotide bindingi199 – 204Allosteric inhibitor CTP; alternateUniRule annotation6
    Nucleotide bindingi199 – 204UTP; alternateUniRule annotation6

    <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
    MTBH37RV:G185E-5890-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P9WHK7

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

    More...
    UniPathwayi
    UPA00159;UER00277

    <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:
    CTP synthaseUniRule annotation (EC:6.3.4.2UniRule annotation)
    Alternative name(s):
    Cytidine 5'-triphosphate synthaseUniRule annotation
    Cytidine triphosphate synthetaseUniRule annotation
    Short name:
    CTP synthetase1 PublicationUniRule annotation
    Short name:
    CTPSUniRule annotation
    UTP--ammonia ligaseUniRule 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:pyrG
    Ordered Locus Names:Rv1699
    ORF Names:MTCI125.21
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv1699

    <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>Mutagenesisi186V → G: 14-fold reduction in catalytic activity. 10-fold decrease in affinity for ATP but no change in affinity for UTP. Causes resistance to the anti-tubercular compounds 7947882 and 7904688. Catalytic activity cannot be inhibited by the active metabolite of 7947882. 1 Publication1

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001382021 – 586CTP synthaseAdd BLAST586

    Proteomic databases

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

    More...
    PaxDbi
    P9WHK7

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P9WHK7

    <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

    Homotetramer.

    UniRule annotation1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv1699

    <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

    1586
    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
    P9WHK7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_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>Domaini303 – 551Glutamine amidotransferase type-1UniRule annotationAdd BLAST249

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 278Amidoligase domainUniRule annotationAdd BLAST278
    Regioni394 – 397L-glutamine bindingUniRule annotation4

    <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
    ENOG4105C8D Bacteria
    COG0504 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K01937

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    EFNNAYR

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WHK7

    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_length">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_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.

    P9WHK7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRKHPQTATK HLFVSGGVAS SLGKGLTASS LGQLLTARGL HVTMQKLDPY
    60 70 80 90 100
    LNVDPGTMNP FQHGEVFVTE DGAETDLDVG HYERFLDRNL PGSANVTTGQ
    110 120 130 140 150
    VYSTVIAKER RGEYLGDTVQ VIPHITDEIK RRILAMAQPD ADGNRPDVVI
    160 170 180 190 200
    TEIGGTVGDI ESQPFLEAAR QVRHYLGRED VFFLHVSLVP YLAPSGELKT
    210 220 230 240 250
    KPTQHSVAAL RSIGITPDAL ILRCDRDVPE ALKNKIALMC DVDIDGVIST
    260 270 280 290 300
    PDAPSIYDIP KVLHREELDA FVVRRLNLPF RDVDWTEWDD LLRRVHEPHE
    310 320 330 340 350
    TVRIALVGKY VELSDAYLSV AEALRAGGFK HRAKVEICWV ASDGCETTSG
    360 370 380 390 400
    AAAALGDVHG VLIPGGFGIR GIEGKIGAIA YARARGLPVL GLCLGLQCIV
    410 420 430 440 450
    IEAARSVGLT NANSAEFDPD TPDPVIATMP DQEEIVAGEA DLGGTMRLGS
    460 470 480 490 500
    YPAVLEPDSV VAQAYQTTQV SERHRHRYEV NNAYRDKIAE SGLRFSGTSP
    510 520 530 540 550
    DGHLVEFVEY PPDRHPFVVG TQAHPELKSR PTRPHPLFVA FVGAAIDYKA
    560 570 580
    GELLPVEIPE IPEHTPNGSS HRDGVGQPLP EPASRG
    Length:586
    Mass (Da):63,635
    Last modified:April 16, 2014 - 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:iB49F607F9DC47E43
    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
    AL123456 Genomic DNA Translation: CCP44464.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B70503

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_216215.1, NC_000962.3
    WP_003408396.1, NZ_NVQJ01000010.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP44464; CCP44464; Rv1699

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    885048

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv1699
    mtv:RVBD_1699

    <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
    AL123456 Genomic DNA Translation: CCP44464.1
    PIRiB70503
    RefSeqiNP_216215.1, NC_000962.3
    WP_003408396.1, NZ_NVQJ01000010.1

    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
    4ZDIX-ray3.52A/B/C/D/E/F/G/H1-586[»]
    4ZDJX-ray1.99A1-586[»]
    4ZDKX-ray3.49A/B1-586[»]
    SMRiP9WHK7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv1699

    Proteomic databases

    PaxDbiP9WHK7
    PRIDEiP9WHK7

    Genome annotation databases

    EnsemblBacteriaiCCP44464; CCP44464; Rv1699
    GeneIDi885048
    KEGGimtu:Rv1699
    mtv:RVBD_1699

    Organism-specific databases

    TubercuListiRv1699

    Phylogenomic databases

    eggNOGiENOG4105C8D Bacteria
    COG0504 LUCA
    KOiK01937
    OMAiEFNNAYR
    PhylomeDBiP9WHK7

    Enzyme and pathway databases

    UniPathwayiUPA00159;UER00277
    BioCyciMTBH37RV:G185E-5890-MONOMER
    SABIO-RKiP9WHK7

    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

    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 nameiPYRG_MYCTU
    <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: P9WHK7
    Secondary accession number(s): L0TA54, P0A5U2, P96351
    <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: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: September 18, 2019
    This is version 34 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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