Q1GTY6 · PYRG_SPHAL

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.

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 site13CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site13UTP (UniProtKB | ChEBI)
Binding site14-19ATP (UniProtKB | ChEBI)
Binding site54L-glutamine (UniProtKB | ChEBI)
Binding site71ATP (UniProtKB | ChEBI)
Binding site71Mg2+ (UniProtKB | ChEBI)
Binding site139Mg2+ (UniProtKB | ChEBI)
Binding site146-148CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191UTP (UniProtKB | ChEBI)
Binding site222CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site222UTP (UniProtKB | ChEBI)
Binding site354L-glutamine (UniProtKB | ChEBI)
Active site381Nucleophile; for glutamine hydrolysis
Binding site382-385L-glutamine (UniProtKB | ChEBI)
Binding site405L-glutamine (UniProtKB | ChEBI)
Binding site470L-glutamine (UniProtKB | ChEBI)
Active site515
Active site517

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

Protein family/group 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
    • Ordered locus names
      Sala_1170

Organism names

Accessions

  • Primary accession
    Q1GTY6

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002662231-543CTP synthase

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-265Amidoligase domain
Domain291-542Glutamine amidotransferase type-1

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    543
  • Mass (Da)
    59,457
  • Last updated
    2006-06-27 v1
  • Checksum
    B33AAC32224CA804
MARFIFITGGVVSSLGKGLMAASLAALLQARGYRVRIRKFDPYLNVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFTGVAARQSDNVTSGRIYQGIIAKERRGDYLGATVQVVPHVTDAIKDFARAETDDLDFVLCEIGGTVGDIESLPFIEAIRQLKNEVGRDNAISVHVTLVPYIAAAGELKTKPTQHSVRELASLGVQPDILLCRCEKPLPDSERAKIALFCNVRKEAVIPALDADSIYSVPVQYHGEGLDSEVLRAFGILDAPAPDLTAWYDIMDRKQHPEGEVTIGVVGKYVSLPDAYKSLNEALVHGGMAHRVKVNIRWLDAEMFERDEDLVANLEPLHGILVPGGFGERGSEGKIASVRFARERNVPFFGICLGMQMACIEAARNTSGIANASSTEFGPTDEPVVGLITEWMSAEGLQKRGANTDLGGTMRLGAYDAKLSPNSHVASVYGTNEISERHRHRYEVNGAYRERLEKGGLVFSGMSPDGMLPEIVERPDHPWFIGVQFHPELKSKPFDPHPLFAGFIEAAVKQSRLV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000356
EMBL· GenBank· DDBJ
ABF52886.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp