B7S454 · B7S454_PHATC

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 site65-70ATP (UniProtKB | ChEBI)
Binding site92a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site113-115a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site144-147a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site151CMP (UniProtKB | ChEBI)
Binding site184ATP (UniProtKB | ChEBI)
Binding site190a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site201a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site229ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
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
      PHATRDRAFT_bd1367

Organism names

  • Taxonomic identifier
  • Strain
    • CCAP 1055/1
  • Taxonomic lineage
    Eukaryota > Sar > Stramenopiles > Ochrophyta > Bacillariophyta > Bacillariophyceae > Bacillariophycidae > Naviculales > Phaeodactylaceae > Phaeodactylum

Accessions

  • Primary accession
    B7S454

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane16-37Helical

Keywords

PTM/Processing

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region183-193LID

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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    245
  • Mass (Da)
    27,241
  • Last updated
    2009-02-10 v1
  • Checksum
    7CFC3328FB934ED4
MPDKDCDYHKGTRPTFNLSFCPFSLGIFLGTAVLVALNRRQSQRNSSEDETLPTCQVVFVLGGPGAGKGTQCELVTQHQPGWSHLSAGDLLRAERQRGGELGDTINKCIADGRLVPSKVTCRLLEKGMHEVYAKSGGTKFLIDGFPRSQGNAEAWKDTMSHHKVEFVLFLDCPEEVMIGRLLERGQTSGRNDDNMQVIKKRFETFELETAPIVDWYDQQGKVKRVSADKGQEDVYADVAALFETL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS999284
EMBL· GenBank· DDBJ
EEC42578.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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