A0A0W8H075 · A0A0W8H075_ACIJO

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.

Type
IDPosition(s)Description
Binding site13CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site13UTP (UniProtKB | ChEBI)
Binding site14-19ATP (UniProtKB | ChEBI)
Binding site71ATP (UniProtKB | ChEBI)
Binding site71Mg2+ (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 site354L-glutamine (UniProtKB | ChEBI)
Active site381Nucleophile
Active site381Nucleophile; for glutamine hydrolysis
Binding site382-385L-glutamine (UniProtKB | ChEBI)
Binding site405L-glutamine (UniProtKB | ChEBI)
Binding site472L-glutamine (UniProtKB | ChEBI)
Active site517
Active site519

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular FunctionCTP synthase 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
      ACNJC6_01644
      , AJO04nite_17960
      , DI542_02230
      , EGT73_02350
      , I6G67_06970
      , N5C10_06665
      , N5C97_03190
      , N5D11_08720
      , N5I27_10410
      , NCTC10308_01356
      , QBJ73_00310

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • C6
    • S2_003_000_R3_20
    • NCTC10308
    • AJ_385
    • NBRC 102197
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter

Accessions

  • Primary accession
    A0A0W8H075

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-266Amidoligase domain
Domain4-265CTP synthase N-terminal
Domain302-536Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    546
  • Mass (Da)
    61,001
  • Last updated
    2016-03-16 v1
  • Checksum
    B061F4715A2209E5
MTHFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRRAKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGEGYDVAIVEIGGTVGDIESLPFMESVRQLMVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEYDVDADTTRKIALFTNVEARAVVVCKDARSIYQIPRTFYEQNVDDLICERFGFNDLPEADLTDWDNVVEALLNPEYTVRVAMVGKYVELPDAYKSVNEALLHAGIQNRVKVQIDYVNAEELESQDVNEVLKDMDAILVPGGFGERGTEGKMQAIKFARENGVPFLGICLGMQLAVIEYARNVVGISDASSTEFNRSTKSPLIGLITEWLDERGEVQQRNVDSDLGGTMRLGAQKSELVEGTKTREVYGSADIIERHRHRYEMNNRFIPALEEAGMKISGYSPVQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFASFIDAAKAQYKKAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BJUJ01000046
EMBL· GenBank· DDBJ
GEK44538.1
EMBL· GenBank· DDBJ
Genomic DNA
JAOCDR010000015
EMBL· GenBank· DDBJ
MDH0656200.1
EMBL· GenBank· DDBJ
Genomic DNA
JAOCCL010000005
EMBL· GenBank· DDBJ
MDH0825516.1
EMBL· GenBank· DDBJ
Genomic DNA
JAOCBE010000001
EMBL· GenBank· DDBJ
MDH0968950.1
EMBL· GenBank· DDBJ
Genomic DNA
JAOCIL010000001
EMBL· GenBank· DDBJ
MDH1438770.1
EMBL· GenBank· DDBJ
Genomic DNA
QFQJ01000005
EMBL· GenBank· DDBJ
PZQ93338.1
EMBL· GenBank· DDBJ
Genomic DNA
CP065666
EMBL· GenBank· DDBJ
QPS05173.1
EMBL· GenBank· DDBJ
Genomic DNA
RHXE01000003
EMBL· GenBank· DDBJ
RSE26520.1
EMBL· GenBank· DDBJ
Genomic DNA
FUUY01000004
EMBL· GenBank· DDBJ
SJX22013.1
EMBL· GenBank· DDBJ
Genomic DNA
UFRV01000006
EMBL· GenBank· DDBJ
SUT94117.1
EMBL· GenBank· DDBJ
Genomic DNA
CP121776
EMBL· GenBank· DDBJ
WMG18119.1
EMBL· GenBank· DDBJ
Genomic DNA

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