A0A1J5IGY9 · A0A1J5IGY9_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

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 site130Zn2+ (UniProtKB | ChEBI); structural
Binding site135Zn2+ (UniProtKB | ChEBI); structural
Binding site138-139ATP (UniProtKB | ChEBI)
Binding site152Zn2+ (UniProtKB | ChEBI); structural
Binding site155Zn2+ (UniProtKB | ChEBI); structural
Binding site162AMP (UniProtKB | ChEBI)
Binding site173AMP (UniProtKB | ChEBI)
Binding site201ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionzinc ion binding
Biological ProcessAMP salvage

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
      AUK24_02600

Organism names

Accessions

  • Primary accession
    A0A1J5IGY9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region30-59NMP
Domain127-164Adenylate 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
    217
  • Mass (Da)
    24,244
  • Last updated
    2017-02-15 v1
  • Checksum
    5E1799841CECB089
MKIILLGAPGAGKGTVARLLTETDGSVQISTGDILRASVREGTELGKQARGYMDRGELVPDSLIMGIMKIRLQEEDCKKGFILDGFPRTIPQAVELEKILETLGIKLDFVVNLEVPREVILDRLTTRRTCLSPECQEIYNVKSNPPTTDDKCKKCGSPVMQRDDETEEAIIRRLSTYTQKTSPLIGFYQREGILKNFVSLDSKETVGKIREALNKDR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MNZP01000055
EMBL· GenBank· DDBJ
OIP91678.1
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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