A3ML79 · PYRG_BURM7

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 site71ATP (UniProtKB | ChEBI)
Binding site71Mg2+ (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 site356L-glutamine (UniProtKB | ChEBI)
Active site383Nucleophile; for glutamine hydrolysis
Binding site384-387L-glutamine (UniProtKB | ChEBI)
Binding site407L-glutamine (UniProtKB | ChEBI)
Binding site473L-glutamine (UniProtKB | ChEBI)
Active site520
Active site522

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 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
    • Ordered locus names
      BMA10247_1468

Organism names

Accessions

  • Primary accession
    A3ML79

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001394021-553CTP synthase

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-270Amidoligase domain
Domain295-547Glutamine amidotransferase type-1

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    553
  • Mass (Da)
    61,042
  • Last updated
    2007-04-03 v1
  • MD5 Checksum
    551401797A66BF2CFE6362FE1A314171
MTKYVFVTGGVVSSLGKGIAAASLAAILESRGLKVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFISTKMRKANNFTTGQIYESVIRKERRGDYLGKTVQVIPHITNEIQAFIERGAASATCGEPDVAIVEIGGTVGDIESLPFLEAARQMSLRLGRNSACFVHLTLVPFIATAGELKTKPTQHSVQKLREIGISPHVLLCRADRPIPDDESKKISLFSNVPEDAVISVWDVDSIYKIPQMLHDQGLDRLICEELRLDPQPADLRMWAALVEKLQNPKHEVTIGMVGKYVDLTESYKSLIEALRHASIHTSTKVNIEYIDSEELETNGTASLAHLDAVLVPGGFGRRGTEGKIAAVRYAREAKVPYLGICLGMQLAVIEFARDVVGLKQANSTEFDPNTPERVVALITEWYDREGKVEKRTEDSDLGGTMRLGSQRCPIKPGTLAEAIYGKDVNERHRHRYEVNNRFVPQLEAGGLVISARTPSEDLPEMMELPSTMHPWFVGVQFHPEFTSTPRDGHPLFKSFVQAALACQQTRAGAKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000548
EMBL· GenBank· DDBJ
ABO04521.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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