A0A0L8I3E8 · A0A0L8I3E8_OCTBM

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.

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 site47-52ATP (UniProtKB | ChEBI)
Binding site73a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site95-97a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site122-125a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site129CMP (UniProtKB | ChEBI)
Binding site163ATP (UniProtKB | ChEBI)
Binding site169a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site180a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site208ATP (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 ProcessCDP biosynthetic process
Biological Processphosphorylation
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

    • ORF names
      OCBIM_22036563mg

Organism names

Accessions

  • Primary accession
    A0A0L8I3E8

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region67-97NMPbind
Region162-172LID

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    224
  • Mass (Da)
    24,854
  • Last updated
    2015-11-11 v1
  • Checksum
    583FDD06338C5BBE
MLTGFSRQSQFKGRLKYFLKTFIQKSSLSSVIMTNRFNVVFILGGPGAGKGTQCANIVENFDYGHLSAGDLLRAERNDSNSQYGALIDKHIKEGSIVPVSITCSLLKKAMEASGKNNFLIDGFPRNKDNLAGWDSEMTETATVKLVLYFTCSEDVCVQRCLKRGETSGRADDNIESLKKRIMTFNSSTKPVIDHYKKLGLVKEVLAESGPSEVFEEVKTIFDNL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KQ416645
EMBL· GenBank· DDBJ
KOF96043.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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