A0A0A1VRG5 · A0A0A1VRG5_MICAE

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

Type
IDPosition(s)Description
Binding site48CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site48UTP (UniProtKB | ChEBI)
Binding site49-54ATP (UniProtKB | ChEBI)
Binding site106ATP (UniProtKB | ChEBI)
Binding site106Mg2+ (UniProtKB | ChEBI)
Binding site176Mg2+ (UniProtKB | ChEBI)
Binding site183-185CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site223-228CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site223-228UTP (UniProtKB | ChEBI)
Binding site259CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site259UTP (UniProtKB | ChEBI)
Binding site277ATP (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 site497L-glutamine (UniProtKB | ChEBI)
Active site542
Active site544

GO annotations

AspectTerm
Cellular Componentcytosol
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
    • ORF names
      N44_00507

Organism names

  • Taxonomic identifier
  • Strain
    • NIES-44
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Microcystaceae > Microcystis

Accessions

  • Primary accession
    A0A0A1VRG5

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-302Amidoligase domain
Domain38-302CTP synthase N-terminal
Domain339-561Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    581
  • Mass (Da)
    64,635
  • Last updated
    2015-02-04 v1
  • Checksum
    9913BFF464BFD292
MKSGKMTPPFGFSQGQPHPENSYPLLGIIDRRKNFMSKFVFVTGGVVSSIGKGIVAASLGRLLKSRDYSVSILKLDPYINVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFTDTELSRLNSVTTGSIYQAVLNKERRGAYMGGTVQVIPHITNEIKERILRVAKDTNPDIVITEIGGTVGDIESLPFLEAIRQFRKDVGRNNVVYMHVTLIPWIPAAKEMKTKPTQHSVKELRSIGIQPDVLVCRCHLPLQPGLKEKLSAFCDVPVESVITAQDASSIYEVPLNLEKEGLAQQTLELLNLGPRYPHLEEWENLIRQMQSPSQKLEIAIVGKYVQLGDAYLSVVEALKHAAIALNSEIELRWVSAEDVDNDSAEAHLSGVDGIVVPGGFGIRGVDGKIKAIEYARVNNIPFLGLCLGMQCSIIEWGRNVARLERANSSEFEEDTPNPVINLLPEQADVVDLGGTMRLGLYPCRLNPDSLAFSLYGQEVIYERHRHRYEFNNAYRSLFFETGYLVSGTSPDGRLVEIIELPKHPFFIATQFHPEFRSRPNKAHPLFYGFMKAALKSAEQKFSLSGQHSAIS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BBPA01000019
EMBL· GenBank· DDBJ
GAL92219.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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