A0A292IHV9 · A0A292IHV9_9MOLU

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.

122620406080100120140160180200220
TypeIDPosition(s)Description
Binding site13-18ATP (UniProtKB | ChEBI)
Binding site34AMP (UniProtKB | ChEBI)
Binding site39AMP (UniProtKB | ChEBI)
Binding site60-62AMP (UniProtKB | ChEBI)
Binding site91-94AMP (UniProtKB | ChEBI)
Binding site98AMP (UniProtKB | ChEBI)
Binding site129ATP (UniProtKB | ChEBI)
Binding site132Zn2+ (UniProtKB | ChEBI); structural
Binding site135Zn2+ (UniProtKB | ChEBI); structural
Binding site138-139ATP (UniProtKB | ChEBI)
Binding site154Zn2+ (UniProtKB | ChEBI); structural
Binding site157Zn2+ (UniProtKB | ChEBI); structural
Binding site164AMP (UniProtKB | ChEBI)
Binding site175AMP (UniProtKB | ChEBI)
Binding site203ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentintracellular membrane-bounded organelle
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
      MAMA39_00040

Organism names

Accessions

  • Primary accession
    A0A292IHV9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region33-62NMP
Domain129-166Adenylate 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
    226
  • Mass (Da)
    25,358
  • Last updated
    2017-12-20 v1
  • Checksum
    5FBD271D162A30E1
MTKKRLIFIGAPGTGKGTISQMLKSQWNYVHLSTGNLFRNIIKQDSALGQTIATCLQAGKYVSDEITNAVIEQTFASDANQLRTQGFILDGYPRTLGQAKFLATLTPIDCVILLAVNDFSPIIKRLSGRLVCLQCQTVYNTNVAQTTPKVSNQCDFDHSTLTKRKDDEPQIIQDRIEHYLQSIQPVIDFYDDCNQLVKIDASLELSKLYDAVVAVLKERYERIHSP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG937516
EMBL· GenBank· DDBJ
CDN40132.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp