A0A1F5BCK9 · A0A1F5BCK9_9BACT

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

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site10-15ATP (UniProtKB | ChEBI)
Binding site31AMP (UniProtKB | ChEBI)
Binding site36AMP (UniProtKB | ChEBI)
Binding site57-59AMP (UniProtKB | ChEBI)
Binding site85-88AMP (UniProtKB | ChEBI)
Binding site92AMP (UniProtKB | ChEBI)
Binding site124ATP (UniProtKB | ChEBI)
Binding site127Zn2+ (UniProtKB | ChEBI); structural
Binding site130Zn2+ (UniProtKB | ChEBI); structural
Binding site133-134ATP (UniProtKB | ChEBI)
Binding site147Zn2+ (UniProtKB | ChEBI); structural
Binding site150Zn2+ (UniProtKB | ChEBI); structural
Binding site157AMP (UniProtKB | ChEBI)
Binding site168AMP (UniProtKB | ChEBI)
Binding site196ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionnucleoside diphosphate kinase activity
Molecular Functionzinc ion binding
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
      A2V57_02360

Organism names

Accessions

  • Primary accession
    A0A1F5BCK9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region30-59NMP
Region123-160LID
Domain124-159Adenylate 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. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.

Sequence similarities

Belongs to the adenylate kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    223
  • Mass (Da)
    23,560
  • Last updated
    2017-02-15 v1
  • Checksum
    F1F7DAE42CF54479
MRIILLGAPGSGKGTVAEGLRSAYGFPKISTGDLLREAVREGTPLGIVAASQMGKGGLVDDATVLALLRERLARDDCRGGHVLDGFPRTLAQADSLESIGAPGPEVVFDLQVSDEVVLRRLTNRRTCPKCEAIYHLLNKPPKTAGICDACGTALVQRNDDTSEVIVERLRTYHAKTEPLVARYAAKGALYRIDGDGPAGAVLGEVRKVLDAVLGRAESTGTGE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MEYF01000039
EMBL· GenBank· DDBJ
OGD28342.1
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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