A0A0A1H2Q1 · A0A0A1H2Q1_9BURK

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.

Caution

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

Catalytic activity

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.

Features

Showing features for binding site.

121620406080100120140160180200
TypeIDPosition(s)Description
Binding site8-13ATP (UniProtKB | ChEBI)
Binding site29AMP (UniProtKB | ChEBI)
Binding site34AMP (UniProtKB | ChEBI)
Binding site55-57AMP (UniProtKB | ChEBI)
Binding site83-86AMP (UniProtKB | ChEBI)
Binding site90AMP (UniProtKB | ChEBI)
Binding site121ATP (UniProtKB | ChEBI)
Binding site130-131ATP (UniProtKB | ChEBI)
Binding site154AMP (UniProtKB | ChEBI)
Binding site165AMP (UniProtKB | ChEBI)
Binding site201ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionnucleoside diphosphate kinase activity
Biological ProcessAMP salvage
Biological Processnucleoside diphosphate metabolic process
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate kinase
  • EC number
  • Short names
    AK
  • Alternative names
    • ATP-AMP transphosphorylase
    • ATP:AMP phosphotransferase
    • Adenylate monophosphate kinase

Gene names

    • Name
      adk
    • ORF names
      E1O_14720

Organism names

Accessions

  • Primary accession
    A0A0A1H2Q1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region28-57NMP
Region120-157LID
Domain121-156Adenylate kinase active site lid
Region126-151Disordered
Compositional bias136-151Basic and acidic residues

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    216
  • Mass (Da)
    23,592
  • Last updated
    2015-02-04 v1
  • Checksum
    FEB4E06EBE9A1D6A
MILLGPPGAGKGTQAGFLTAKLGIPQISTGDMLRAAVKAGTPLGLAAKKVMEAGQLVSDDLIIGLVRDRLAQPDCARGYLFDGFPRTLAQAEALKQAEVPIDLVLEFAVPDAEIIERMSGRRVHPGSGRSYHVRFNPPKIADRDDHTGEPLVQRDDDREEIVRKRLEVYHAQTRPLIAYYSDWAASGDPRAPRYRTVDGVGAMTEIQARIEAALRQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias136-151Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP014683
EMBL· GenBank· DDBJ
BAP88603.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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