A0A1J1I2M5 · A0A1J1I2M5_9DIPT

  • Protein
    UMP-CMP kinase
  • Gene
    putative UMP-CMP kinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site52-57ATP (UniProtKB | ChEBI)
Binding site78a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site100-102a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site131-134a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site138CMP (UniProtKB | ChEBI)
Binding site172ATP (UniProtKB | ChEBI)
Binding site179a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site190a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site218ATP (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

    • Name
      putative UMP-CMP kinase
    • ORF names
      CLUMA_CG006573

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Nematocera > Chironomoidea > Chironomidae > Clunio

Accessions

  • Primary accession
    A0A1J1I2M5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region72-102NMPbind

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
    240
  • Mass (Da)
    27,215
  • Last updated
    2017-02-15 v1
  • Checksum
    EA054111C7BBE6B8
MIPVLNQLLKTKLVVKCFKRHVTLSPLSGNKFILRKMENNKPKIIFVLGAPGAGKGTQCEKIVNSFGFKHLSAGDLLREERAREGSQFGSLIEDCITNGKIVPVEITCSLLENAIIKTNQETGNNKFLIDGFPRNEDNLQGWQRQMSEKVDFLFVLFFECSQDKCVERCLKRGQAGSGRTDDNMESLKKRFDTYMNDTMAIINHYRGLGKVRQIFANEDPETVFKSVKNALTEAQEQKLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CVRI01000036
EMBL· GenBank· DDBJ
CRK93102.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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