A0A5H6RQM0 · A0A5H6RQM0_SALET

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.

TypeIDPosition(s)Description
Binding site14CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site14UTP (UniProtKB | ChEBI)
Binding site15-20ATP (UniProtKB | ChEBI)
Binding site72ATP (UniProtKB | ChEBI)
Binding site72Mg2+ (UniProtKB | ChEBI)
Binding site140Mg2+ (UniProtKB | ChEBI)
Binding site147-149CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site187-192CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site187-192UTP (UniProtKB | ChEBI)
Binding site223CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site223UTP (UniProtKB | ChEBI)
Binding site239-241ATP (UniProtKB | ChEBI)
Binding site352L-glutamine (UniProtKB | ChEBI)
Active site379Nucleophile
Active site379Nucleophile; for glutamine hydrolysis
Binding site380-383L-glutamine (UniProtKB | ChEBI)
Binding site403L-glutamine (UniProtKB | ChEBI)
Binding site470L-glutamine (UniProtKB | ChEBI)
Active site515
Active site517

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase 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
      APM01_10680
      , BFV08_15220
      , DM677_03205
      , DN927_02685
      , DOG83_16595
      , DPE57_04415
      , DQK10_18415
      , DU046_22720
      , DYS13_00930
      , DYT81_21650
      , E5908_07055
      , EWI81_22405
      , G4R07_001677

Organism names

  • Taxonomic identifier
  • Strains
    • 146074
    • 275776
    • 298956
    • M210
    • FSIS11811772
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella

Accessions

  • Primary accession
    A0A5H6RQM0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-266Amidoligase domain
Domain5-266CTP synthase N-terminal
Domain301-534Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    545
  • Mass (Da)
    60,095
  • Last updated
    2019-12-11 v1
  • Checksum
    EF186DF728B2EAB8
MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQLAVDIGREHALFMHLTLVPYLAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISMKDVDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVETRGVEILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMDNANSTEFVPDCKYPVVALITEWRDEDGNVEVRSEKSDLGGTMRLGAQQCQLSDDSLVRQLYGASTIVERHRHRYEVNNMLLKQIEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEHQKRQAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAGVGK010000003
EMBL· GenBank· DDBJ
EBS3931158.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHDUY010000002
EMBL· GenBank· DDBJ
EBU9892184.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHXHM010000062
EMBL· GenBank· DDBJ
ECB3379632.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHYZU010000004
EMBL· GenBank· DDBJ
ECB8844430.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKIXE010000006
EMBL· GenBank· DDBJ
ECS2228802.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKLKV010000002
EMBL· GenBank· DDBJ
ECT0130979.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKLWJ010000115
EMBL· GenBank· DDBJ
ECT1545193.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKMFT010000110
EMBL· GenBank· DDBJ
ECT2693587.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKNWZ010000005
EMBL· GenBank· DDBJ
ECT7928735.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKSPP010000001
EMBL· GenBank· DDBJ
ECV1595438.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKSBI010000025
EMBL· GenBank· DDBJ
ECV3390244.1
EMBL· GenBank· DDBJ
Genomic DNA
DAATIJ010000003
EMBL· GenBank· DDBJ
HAE8736554.1
EMBL· GenBank· DDBJ
Genomic DNA
RVCL01000012
EMBL· GenBank· DDBJ
MLO06625.1
EMBL· GenBank· DDBJ
Genomic DNA

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