A0A1L8EE30 · A0A1L8EE30_HAEIR

Function

function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per monomer.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site54-59ATP (UniProtKB | ChEBI)
Binding site80a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site102-104a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site129-132a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site136CMP (UniProtKB | ChEBI)
Binding site170ATP (UniProtKB | ChEBI)
Binding site177a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site188a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site216ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionCMP kinase activity
Molecular FunctiondCMP kinase activity
Molecular FunctionUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processpyrimidine nucleotide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UMP-CMP kinase
  • EC number
  • Alternative names
    • Deoxycytidylate kinase
      (CK
      ; dCMP kinase
      )
    • Uridine monophosphate/cytidine monophosphate kinase
      (UMP/CMP kinase
      ; UMP/CMPK
      )

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Muscoidea > Muscidae > Haematobia

Accessions

  • Primary accession
    A0A1L8EE30

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region74-104NMPbind

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    234
  • Mass (Da)
    26,179
  • Last updated
    2017-03-15 v1
  • Checksum
    52186ECD4B11B767
MFKVLARSCNLFAVQSKHSTHTCTKKLSKITPSLTKLRMSEEKPKIVFVLGGPGAGKGTQCSKIVERFQFVHLSAGDLLREERAREGSEVGALIEDYIRNGKIVPVEVTCSLLEAAMKKSGKNKFLIDGFPRNQDNLEGWNRQMSDKVDFQFVLFFNCSEEVCVNRCLSRGQSGSGRSDDNMESLKKRIQTYNNDSLPIIKHFEELGKVKQIDASPSADEVFSKVEEVFGQSGF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GFDG01001914
EMBL· GenBank· DDBJ
JAV16885.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

Disclaimer

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