A0A2H3DA29 · A0A2H3DA29_ARMGA

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.

Catalytic activity

Features

Showing features for binding site.

125520406080100120140160180200220240
TypeIDPosition(s)Description
Binding site48-53ATP (UniProtKB | ChEBI)
Binding site69AMP (UniProtKB | ChEBI)
Binding site74AMP (UniProtKB | ChEBI)
Binding site95-97AMP (UniProtKB | ChEBI)
Binding site124-127AMP (UniProtKB | ChEBI)
Binding site131AMP (UniProtKB | ChEBI)
Binding site166ATP (UniProtKB | ChEBI)
Binding site175-176ATP (UniProtKB | ChEBI)
Binding site199AMP (UniProtKB | ChEBI)
Binding site210AMP (UniProtKB | ChEBI)
Binding site238ATP (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
Biological Processphosphorylation

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
      ARMGADRAFT_1053979

Organism names

Accessions

  • Primary accession
    A0A2H3DA29

Proteomes

Subcellular Location

Cytoplasm, cytosol
Note: Predominantly mitochondrial.

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region68-97NMPbind
Region165-202LID
Domain166-201Adenylate kinase active site lid

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    255
  • Mass (Da)
    28,096
  • Last updated
    2018-01-31 v1
  • Checksum
    B3098BCB58138A02
MGASEELEYLKSLVAQLNDKIGALEAKAKNAAPTPAQQLRTILIGPPGAGKGTQAPRIREQFCVCHLATGDMLREQVTAKTALGVEAKKIMDAGGLVSDEIMVGMIKDQLENNKECKNGFVLDGFPRTVPQAKKLDSMLEARKEKLDSVVQLQIDDQLLISRITGRLIHPASGRSYHKEFHPPKKPMTDDITGEPLIQRSDDNVETLQKRLGSFHSMTGPVVDYYRVKGLWHGIDAAQSPSVVWDNLRKVFTGKQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KZ293659
EMBL· GenBank· DDBJ
PBK92079.1
EMBL· GenBank· DDBJ
Genomic DNA

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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