A0A125RCY0 · A0A125RCY0_9EURY

Function

function

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.

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Activity regulation

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.

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site18CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site18UTP (UniProtKB | ChEBI)
Binding site19-24ATP (UniProtKB | ChEBI)
Binding site59L-glutamine (UniProtKB | ChEBI)
Binding site76ATP (UniProtKB | ChEBI)
Binding site76Mg2+ (UniProtKB | ChEBI)
Binding site146Mg2+ (UniProtKB | ChEBI)
Binding site153-155CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site193-198CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site193-198UTP (UniProtKB | ChEBI)
Binding site229CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site229UTP (UniProtKB | ChEBI)
Binding site247ATP (UniProtKB | ChEBI)
Binding site359L-glutamine (UniProtKB | ChEBI)
Active site386Nucleophile
Active site386Nucleophile; for glutamine hydrolysis
Binding site387-390L-glutamine (UniProtKB | ChEBI)
Binding site409L-glutamine (UniProtKB | ChEBI)
Binding site466L-glutamine (UniProtKB | ChEBI)
Active site511
Active site513

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionglutaminase activity
Molecular Functionmetal ion binding
Biological Process'de novo' CTP biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CTP synthase
  • EC number
  • Alternative names
    • Cytidine 5'-triphosphate synthase
    • Cytidine triphosphate synthetase
      (CTP synthetase
      ; CTPS
      )
    • UTP--ammonia ligase

Gene names

    • Name
      pyrG
    • ORF names
      TL18_05775

Organism names

  • Taxonomic identifier
  • Strain
    • YE315
  • Taxonomic lineage
    Archaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanobrevibacter

Accessions

  • Primary accession
    A0A125RCY0

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-272Amidoligase domain
Domain8-271CTP synthase N-terminal
Domain310-530Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    538
  • Mass (Da)
    60,395
  • Last updated
    2016-04-13 v1
  • Checksum
    A2D2D7AA42B37C3A
MERIFLTKYIIITGGVVSSIGKGITSASMGRILRSYGLKVSAIKIDPYLNWDSGTLNPYQHGEVYVTHDGMETDLDLGHYERFLDVELDGLANITTGKVYESVIAKEREGGYLGECVQVIPHITNRIKEMIRENSESADYDVVLVELGGTVGDIESQPFLEALRQLRNEEGRENVMFVHVTFIPYLNAAGEFKTKPTQHSTKELRSVGINPDVIVCRSQEPIDDALRGKIAHFCDVDYEAVVNTPDAGTIYEVPLVLEEHDIGKFIVNRIGLGIEPDSSKLDEWREIVKSLKINEPVVNIGIVGKYVELEDSYISIRESLLHAAASIGVKANIIFLSSDVEELDQDVMDELDGILIPGGFGERGFEGKLDAVEYAIENDVPLFGICLGMQCMVTQFARINGYPGANSSEFDDNLEFPVIDMMEEQKKIKNMGGTMRLGSYDCKIVEGTKTFDAYGETDIEERHRHRYEVNNDYRDDLQEKGLIISGTSPDNFLVEIVELPDHPWAIGCQFHPEFKSRPNRPHPLFKSFLEAIYEYSKN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010834
EMBL· GenBank· DDBJ
AMD17570.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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