A0A0S3SEV4 · A0A0S3SEV4_PHAAN

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 site62-67ATP (UniProtKB | ChEBI)
Binding site88a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site109-111a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site136-139a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site143CMP (UniProtKB | ChEBI)
Binding site175ATP (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
      Vigan.06G267400
    • ORF names
      VIGAN_06267400

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Shumari
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Vigna

Accessions

  • Primary accession
    A0A0S3SEV4

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
    239
  • Mass (Da)
    27,000
  • Last updated
    2016-02-17 v1
  • Checksum
    9A57836CC0CEB3CA
MWKLATKSSRFLPLLLQLPKHDASLSQRFTTGFPFHSPFQETGGISPKQVATVITFVLGGPGSGKGTQCAKIVETFGYKHLSAGDLLRREMSSDSKYGSMILNTIKEGKIVPSEVTVKLILREMKSSDNRKFLIDGFPRSEENRIAFEQIIGAEPRFVLFFDCPEEEMVKRVLSRNEGRVDDNIDTMRNRLKVFEALNLPVIDYYAKKGKLYRINAVGTADEIFKQVRPVFEACELEAK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP015039
EMBL· GenBank· DDBJ
BAT91352.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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