I4YGI5 · I4YGI5_WALMC

Function

function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Features

Showing features for binding site.

126320406080100120140160180200220240260
TypeIDPosition(s)Description
Binding site57-62ATP (UniProtKB | ChEBI)
Binding site78AMP (UniProtKB | ChEBI)
Binding site83AMP (UniProtKB | ChEBI)
Binding site133-136AMP (UniProtKB | ChEBI)
Binding site140AMP (UniProtKB | ChEBI)
Binding site175ATP (UniProtKB | ChEBI)
Binding site184-185ATP (UniProtKB | ChEBI)
Binding site208AMP (UniProtKB | ChEBI)
Binding site219AMP (UniProtKB | ChEBI)
Binding site247ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrial intermembrane space
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Biological ProcessADP biosynthetic process
Biological ProcessAMP metabolic process
Biological ProcessATP metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate kinase
  • EC number
  • Alternative names
    • ATP-AMP transphosphorylase
    • ATP:AMP phosphotransferase
    • Adenylate kinase cytosolic and mitochondrial
    • Adenylate monophosphate kinase

Gene names

    • Name
      ADK1
    • ORF names
      WALSEDRAFT_31703

Organism names

Accessions

  • Primary accession
    I4YGI5

Proteomes

Subcellular Location

Cytoplasm, cytosol
Note: Predominantly mitochondrial.

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for coiled coil, region, domain.

TypeIDPosition(s)Description
Coiled coil5-32
Region77-106NMPbind
Region174-211LID
Domain175-210Adenylate kinase active site lid
Region183-202Disordered

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. AK2 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    263
  • Mass (Da)
    29,169
  • Last updated
    2012-09-05 v1
  • Checksum
    BB27D1AF20E12BC8
MSGIKESAQQELEHLKSLVKDLSDKIVDLEQRSKAAVLPSGRTPSEELRMILIGPPGAGKGTQAPNIVNKYNVCHLATGDMLRSEVGKKTALGVEAKQIMDAGGLISDEIVVGMIKNQLETNEKCKLGFILDGFPRTVPQAEKLDDMLSSKKQSVDHAVELQIADQLLISRITGRLVHPASGRSYHKEFNPPKKPMTDDLTGEPLIQRSDDNVEALRKRLNTYHQQTTPVVEYYRKQNKHRPIDASQSPKLVWENLSAIFASK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JH668226
EMBL· GenBank· DDBJ
EIM23077.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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