B6SY94 · B6SY94_MAIZE

  • Protein
    UMP-CMP kinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • 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 site23-28ATP (UniProtKB | ChEBI)
Binding site49a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site70-72a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site97-100a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site104CMP (UniProtKB | ChEBI)
Binding site136ATP (UniProtKB | ChEBI)
Binding site140a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site151a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site179ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular FunctionCMP kinase activity
Molecular FunctiondCMP kinase activity
Molecular FunctionUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processphosphorylation
Biological Processpyrimidine nucleotide 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
      )

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea

Accessions

  • Primary accession
    B6SY94

Subcellular Location

Keywords

Expression

Gene expression databases

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    221
  • Mass (Da)
    24,857
  • Last updated
    2008-12-16 v1
  • Checksum
    4C7BE21A41CDAE6C
MSQAGAFPPGKKITVVFVIGGPGSGKGTQCSKIVRHFGFTHLSAGDLLRQQVQSDTEHGAMIKNLMHEGKLVPSDIIVRLLLTAMLQSGNDRFLVDGFPRNEENRRAYESIIGIEPELVLFIDCPREELERRILHRDQGRDDDNVDTIRKRFQVFHDSTLPVVLYYDRMGKVRRVDGAKSADAVFEDVKAIFTQLLTTQVHSLTHIYLPFSPIDCSVLIKP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EU957709
EMBL· GenBank· DDBJ
ACG29827.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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