A0A1B1TEZ1 · A0A1B1TEZ1_9ARCH

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 site31CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site31UTP (UniProtKB | ChEBI)
Binding site32-37ATP (UniProtKB | ChEBI)
Binding site89ATP (UniProtKB | ChEBI)
Binding site89Mg2+ (UniProtKB | ChEBI)
Binding site165Mg2+ (UniProtKB | ChEBI)
Binding site172-174CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site212-217CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site212-217UTP (UniProtKB | ChEBI)
Binding site248CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site248UTP (UniProtKB | ChEBI)
Binding site266ATP (UniProtKB | ChEBI)
Binding site389L-glutamine (UniProtKB | ChEBI)
Active site416Nucleophile
Active site416Nucleophile; for glutamine hydrolysis
Binding site417-420L-glutamine (UniProtKB | ChEBI)
Binding site440L-glutamine (UniProtKB | ChEBI)
Binding site498L-glutamine (UniProtKB | ChEBI)
Active site543
Active site545

GO annotations

AspectTerm
Cellular Componentcytoophidium
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionglutaminase activity
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Biological Process'de novo' CTP biosynthetic process
Biological Processglutamine metabolic process
Biological Processpyrimidine nucleobase biosynthetic 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

Organism names

Accessions

  • Primary accession
    A0A1B1TEZ1

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-291Amidoligase domain
Domain21-290CTP synthase N-terminal
Domain329-562Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    569
  • Mass (Da)
    63,035
  • Last updated
    2016-11-02 v1
  • Checksum
    E88A57DEEF6ECDE6
MNIANVDMSSISRSNPVDYMKYVVVTGGVLSGLGKGVTASSIGVLLKSAGLRVTAVKIDPYLNSDAGTMSPFEHGEVFVLDDGGEADLDLGNYERFLDIALSKDNNITTGKVYSSVIEKERRGDYLGKTVQVVPHITDEIQDWIENVANEFSDEENNPPDACVIELGGTVGDIESAPFVEALRQFQFRVGKENICFVHVSLVPVMGPVGEQKTKPTQHTVKELRGLGIIPDILVCRSEVALVDETREKLAKFCHVSSEAVISAHDVANIYHVPIMMNRQGVRELLASKLNFNLPDKNKLLEDWEAMANHVNSLEEEVHIAMVGKYTGLSDSYLSVTKALQHASYSVGKKLVIDWIESVNLEVGDSSESEVYQKSWDLLKRADGILVPGGFGGRGIEGKISAAKYARENNIPYLGVCLGLQVATIEFCRNVLGIKNANSAEFDDNEENHVVVFMPEISKTHMGGTMRLGSKPTPFLVDDCKIRRLYNNESYVDERHRHRYEVNPELIERIEEAGLIYVGKDETGQRCEIMELKDHPYYVGTQYHPEFKSRPNRPSPPFLGLLKAACGIEI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KP211910
EMBL· GenBank· DDBJ
ANV80855.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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