A0A2H4VEI4 · A0A2H4VEI4_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 site16CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site16UTP (UniProtKB | ChEBI)
Binding site17-22ATP (UniProtKB | ChEBI)
Binding site57L-glutamine (UniProtKB | ChEBI)
Binding site74ATP (UniProtKB | ChEBI)
Binding site74Mg2+ (UniProtKB | ChEBI)
Binding site144Mg2+ (UniProtKB | ChEBI)
Binding site151-153CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site191-196CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site191-196UTP (UniProtKB | ChEBI)
Binding site227CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site227UTP (UniProtKB | ChEBI)
Binding site245ATP (UniProtKB | ChEBI)
Binding site354L-glutamine (UniProtKB | ChEBI)
Active site381Nucleophile
Active site381Nucleophile; for glutamine hydrolysis
Binding site382-385L-glutamine (UniProtKB | ChEBI)
Binding site404L-glutamine (UniProtKB | ChEBI)
Binding site461L-glutamine (UniProtKB | ChEBI)
Active site506
Active site508

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
      BK007_11115
      , HG719_10810

Organism names

  • Taxonomic identifier
  • Strains
    • MO-MB1
    • HO_2020
  • Taxonomic lineage
    Archaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanobacterium

Accessions

  • Primary accession
    A0A2H4VEI4

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-270Amidoligase domain
Domain6-270CTP synthase N-terminal
Domain306-525Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    537
  • Mass (Da)
    60,454
  • Last updated
    2018-02-28 v1
  • Checksum
    331D015029B498B0
MVYLSKYIVVTGGVVSSIGKGITAASIGRILRSYGVDVTAIKIDPYLNWDSGTLNPYQHGEVFVTEDGMETDLDLGHYERFLDVNLSGKSNITTGKVYSSVINHERKGDYLGSCVQIIPHITNKIKDMVRKIAQESQAEVVLVEVGGTVGDIESQPFLEALRQLRNEEGHDNVMFVHVTYVPYLRAAGEFKTKPTQHSTKELRSTGIIPDMIICRSELSIDQPLKNKIAHFCDVEREAVINTPDVGSIYEVPLIINQENVGEYIINRIKIDAGEQDLTEWEKVVESLKQEDYQVSVGIIGKYVELEDAYMSIRESLKHAAANLGIKVNIEWIQAENIIDEEKVSHLDSLLIPGGFGERGISGKLDAVRYSLQNKVPLFGICLGMQCMVIEFARLEGFEGAHSTEFDTETTYPVIDLMEEQKKIKNMGGTMRLGSYPCKLKDGTMAHEAYGEEEVSERHRHRYELNNDYRDVLREKGLIISGTSPDDFLVEMIELKDHPWFLGCQFHPEFKSRPNKAHPIFVSFLRAALENHKHKSGN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP017766
EMBL· GenBank· DDBJ
AUB56508.1
EMBL· GenBank· DDBJ
Genomic DNA
JABBYL010000038
EMBL· GenBank· DDBJ
NMO10296.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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