A0A8B7BW87 · A0A8B7BW87_PHODC

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 site37-42ATP (UniProtKB | ChEBI)
Binding site63a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site84-86a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site111-114a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site118CMP (UniProtKB | ChEBI)
Binding site150ATP (UniProtKB | ChEBI)
Binding site154a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site165a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site193ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Function(d)CMP kinase activity
Molecular FunctionATP binding
Molecular FunctionUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological ProcessCDP biosynthetic process
Biological ProcessUDP 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
      )

Gene names

    • Name
      LOC103704920

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Arecaceae > Coryphoideae > Phoeniceae > Phoenix

Accessions

  • Primary accession
    A0A8B7BW87

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

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
    210
  • Mass (Da)
    23,352
  • Last updated
    2022-01-19 v1
  • Checksum
    03A7295D3F2E7B4A
MGTVVDAPATTNASKDVSENHLGDKQVTVVFVLGGPGSGKGTQCANIVEHFGFTHLSAGDLLRAEIKSGSENGTMIQNMIKEGKIVPSEVTIKLLQRAMLESENNKFLIDGFPRNEENRAAFEEVTKIVPEFVLFFDCSEEEMEKRLLSRNQGREDDNIDTIRKRFKVFVESSLPVVEYYNSKSKVKKIDAGKPINEVFEDVKGIFSLFA

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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