R4FMZ5 · R4FMZ5_RHOPR

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.

124620406080100120140160180200220240
TypeIDPosition(s)Description
Binding site28-33ATP (UniProtKB | ChEBI)
Binding site49AMP (UniProtKB | ChEBI)
Binding site54AMP (UniProtKB | ChEBI)
Binding site75-77AMP (UniProtKB | ChEBI)
Binding site103-106AMP (UniProtKB | ChEBI)
Binding site110AMP (UniProtKB | ChEBI)
Binding site145ATP (UniProtKB | ChEBI)
Binding site154-155ATP (UniProtKB | ChEBI)
Binding site178AMP (UniProtKB | ChEBI)
Binding site189AMP (UniProtKB | ChEBI)
Binding site217ATP (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
      Ak2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Rhodnius

Accessions

  • Primary accession
    R4FMZ5

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Note: Predominantly mitochondrial.

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region48-77NMPbind
Region144-181LID
Domain145-180Adenylate 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
    246
  • Mass (Da)
    27,755
  • Last updated
    2013-06-26 v1
  • Checksum
    F024F7FC33AA65B0
MAPQAKPALQVRDDNEDTLRAVFLGPPGSGKGTQAPLLKNRFSVCHLATGDMLRAEVATGSSLGQRIKKVMDAGQLVSDDLVCDLIDSNLDKPECKYGFLLDGFPRTIVQAQKLDKLLEKRRTYLDAAVEFSIDDNLLVRRITGRLFHPASGRSYHEEFHPPKVPMKDDLTGEPLIKRSDDNVDALKKRLDSYHKQTSPLIDYYRKQGIHYKIDASKPADTVFNMIESIFFKCISYKSSKERLRNV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACPB03013754
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
GAHY01001539
EMBL· GenBank· DDBJ
JAA75971.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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