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The annotation and conditions in this rule are derived from the following entries: P0A7E5 (PYRG_ECOLI), P28595 (PYRG_AZOBR), Q59321 (PYRG_CHLTR), O87761 (PYRG_LACLM), P9WHK7 (PYRG_MYCTU), Q5SIA8 (PYRG_THET8), Q980S6 (PYRG_SACS2)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 239 - 241 aligns to "[KR]-x-[VALI]" in entry P0A7E5
    • Subsequence at position 239 - 241 does not align to "[KR]-x-[VALI]" in entry P0A7E5
    • Subsequence at position 241 - 241 aligns to "[VALI]" in entry P0A7E5
    • Subsequence at position 55 - 55 aligns to "Y" in entry P0A7E5 (individually applies "L-glutamine")
    • Subsequence at position 470 - 470 aligns to "R" in entry P0A7E5 (individually applies "L-glutamine; via amide nitrogen")
    • Subsequence at position 517 - 517 aligns to "E" in entry P0A7E5 (individually applies "")
    • Subsequence at position 14 - 14 aligns to "S" in entry P0A7E5 (individually applies "Allosteric inhibitor CTP; alternate")
    • Subsequence at position @NTER@ - 266 aligns to entry P0A7E5 (individually applies "Amidoligase domain")
    • Subsequence at position 147 - 149 aligns to "D-x-E" in entry P0A7E5 (individually applies "Allosteric inhibitor CTP")
    • Subsequence at position 187 - 192 aligns to "K-[TS]-K-x-x-Q" in entry P0A7E5 (individually applies "UTP; alternate")
    • Subsequence at position 140 - 140 aligns to "E" in entry P0A7E5 (individually applies "Magnesium")
    • Subsequence at position 15 - 20 aligns to "x-x-G-K-G-x" in entry P0A7E5 (individually applies "ATP")
    • Subsequence at position 72 - 72 aligns to "D" in entry P0A7E5 (individually applies "Magnesium")
    • Subsequence at position 403 - 403 aligns to "E" in entry P0A7E5 (individually applies "L-glutamine")
    • Subsequence at position 515 - 515 aligns to "H" in entry P0A7E5 (individually applies "")
    • Subsequence at position 223 - 223 aligns to "[KR]" in entry P0A7E5 (individually applies "UTP; alternate")
    • Subsequence at position 223 - 223 aligns to "[KR]" in entry P0A7E5 (individually applies "Allosteric inhibitor CTP; alternate")
    • Subsequence at position 72 - 72 aligns to "D" in entry P0A7E5 (individually applies "ATP")
    • Subsequence at position 352 - 352 aligns to "[GA]" in entry P0A7E5 (individually applies "L-glutamine; via carbonyl oxygen")
    • Subsequence at position 187 - 192 aligns to "K-[TS]-K-x-x-Q" in entry P0A7E5 (individually applies "Allosteric inhibitor CTP; alternate")
    • Subsequence at position 380 - 383 aligns to "[LMYF]-x-x-[QH]" in entry P0A7E5 (individually applies "L-glutamine binding")
    • Subsequence at position 379 - 379 aligns to "C" in entry P0A7E5 (individually applies "Nucleophile; for glutamine hydrolysis")
    • Subsequence at position 14 - 14 aligns to "S" in entry P0A7E5 (individually applies "UTP; alternate")

... then these annotations are applied i

<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 namei

  • Recommended name:
    CTP synthase (EC:6.3.4.2)
    Alternative name(s):
    Cytidine 5'-triphosphate synthase
    Cytidine triphosphate synthetase
    Short name:
    CTP synthetase
    Short name:
    CTPS
    UTP--ammonia ligase

<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 namei

  • Name:pyrG

<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 ‘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

<p>This subsection of the ‘Function’ section describes relevant information that doesn’t fall into the scope of any other subsections, but is thought to be valuable enough to be cited in UniProtKB.<p><a href='/help/miscellaneous' target='_top'>More...</a></p>Miscellaneousi

  • 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> describes the function(s) of a protein.<p><a href='/help/function' 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.

<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.

<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.

<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

  • Pathwayi: CTP biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP. 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.

<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 sitei

  • ATP (to residues corresponding to position 241)
  • L-glutamine (to residues corresponding to position 55)
  • L-glutamine; via amide nitrogen (to residues corresponding to position 470)
  • Allosteric inhibitor CTP; alternate (to residues corresponding to position 14)
  • L-glutamine (to residues corresponding to position 403)
  • UTP; alternate (to residues corresponding to position 223)
  • Allosteric inhibitor CTP; alternate (to residues corresponding to position 223)
  • ATP (to residues corresponding to position 72)
  • L-glutamine; via carbonyl oxygen (to residues corresponding to position 352)
  • UTP; alternate (to residues corresponding to position 14)

<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 bindingi

  • ATP; via amide nitrogen (to residues corresponding to positions 239 - 241)
  • Allosteric inhibitor CTP (to residues corresponding to positions 147 - 149)
  • UTP; alternate (to residues corresponding to positions 187 - 192)
  • ATP (to residues corresponding to positions 15 - 20)
  • Allosteric inhibitor CTP; alternate (to residues corresponding to positions 187 - 192)

<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 bindingi

  • Magnesium (to residues corresponding to position 140)
  • Magnesium (to residues corresponding to position 72)

<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 sitei

  • (to residues corresponding to position 517)
  • (to residues corresponding to position 515)
  • Nucleophile; for glutamine hydrolysis (to residues corresponding to position 379)

<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>Regioni

  • Amidoligase domain (to residues corresponding to positions @NTER@i - 266)
  • L-glutamine binding (to residues corresponding to positions 380 - 383)

<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

<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 (Gene Ontology) termsi

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