A0A3A1XUL9 · A0A3A1XUL9_9BIFI

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.
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 site127ATP (UniProtKB | ChEBI)
Binding site133AMP (UniProtKB | ChEBI)
Binding site144AMP (UniProtKB | ChEBI)
Binding site172ATP (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
      CJI49_04830

Organism names

Accessions

  • Primary accession
    A0A3A1XUL9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region30-59NMP

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    186
  • Mass (Da)
    20,725
  • Last updated
    2018-12-05 v1
  • Checksum
    DEEDD294F3361102
MRLLIMGPQGVGKGTQAALLSEHYGIPAISTGDIFRYNLKNHTELGKQVQGYLDKGELVPDELTNSIVKDRLAQDDAKSGWILDGYPRNASQVQALDRMLEELGTPLDHVVALEAERDVLLERMQKRAVEQGRSDDTPEVIAKRLETYEKETAPLLDIYDSRGQLVEVDGVGDIKEINNRIVESLN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NQOQ01000002
EMBL· GenBank· DDBJ
RIY28881.1
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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