A0A3P9BBH7 · A0A3P9BBH7_9CICH

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. Also displays broad nucleoside diphosphate kinase activity.

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 site36-41ATP (UniProtKB | ChEBI)
Binding site72-74a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site104-107a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site111CMP (UniProtKB | ChEBI)
Binding site145ATP (UniProtKB | ChEBI)
Binding site151a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site162a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site190ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionCMP kinase activity
Molecular FunctiondCMP kinase activity
Molecular Functionnucleoside diphosphate 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
      )
    • Nucleoside-diphosphate kinase
      (EC:2.7.4.6
      ) . EC:2.7.4.6 (UniProtKB | ENZYME | Rhea)
    • Uridine monophosphate/cytidine monophosphate kinase
      (UMP/CMP kinase
      ; UMP/CMPK
      )

Gene names

    • Name
      CMPK1
    • Synonyms
      CMPK

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Cichlomorphae > Cichliformes > Cichlidae > African cichlids > Pseudocrenilabrinae > Haplochromini > Maylandia > Maylandia zebra complex

Accessions

  • Primary accession
    A0A3P9BBH7

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Note: Predominantly nuclear.

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region144-154LID

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
    207
  • Mass (Da)
    23,363
  • Last updated
    2019-02-13 v1
  • Checksum
    36BC55E2CF418034
MIGRLFGNLSQKVPSLLYRVSLVMKPQVVFVLGGPGAGKGTQCSKIVESYGYTHLEESEFGQLIANYIKEGKIVPVEITINLLRKAMEATMKENENKFRFLIDGFPRNEDNLQGWNSVMDGKADVKFVLFFDCSNEVCINRCLERGKSSGRTDDNRESLEKRIQTYLQSTRPIIDLYEKQGKVHTIDASRSVDEVFADVKAILDKEG

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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