B2GJ13 · KAD_KOCRD

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.

Catalytic activity

Pathway

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

Features

Showing features for binding site.

118820406080100120140160180
TypeIDPosition(s)Description
Binding site11-16ATP (UniProtKB | ChEBI)
Binding site32AMP (UniProtKB | ChEBI)
Binding site37AMP (UniProtKB | ChEBI)
Binding site58-60AMP (UniProtKB | ChEBI)
Binding site86-89AMP (UniProtKB | ChEBI)
Binding site93AMP (UniProtKB | ChEBI)
Binding site128ATP (UniProtKB | ChEBI)
Binding site134AMP (UniProtKB | ChEBI)
Binding site145AMP (UniProtKB | ChEBI)
Binding site173ATP (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
    • Ordered locus names
      KRH_06360

Organism names

Accessions

  • Primary accession
    B2GJ13

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10002044171-188Adenylate kinase

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region31-60NMP
Region127-137LID

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
    188
  • Mass (Da)
    20,578
  • Last updated
    2008-06-10 v1
  • Checksum
    C27D6C8AB2862AE5
MTRMLIIGPPGAGKGTQAARISERLGVPAISTGDIFRANIKDQTELGREAQRYTDAGNLVPDSVTNEMVRDRLSHEDVSGGFLLDGYPRTVAQVEELDRILEANGVGLDVVLLLTADNDELVSRLLGRAQEQGRTDDTEDVIRHRLDVYDEQTAPVVGVYEDRGIVVRVDGLGSIDHVTERIMAALER

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009152
EMBL· GenBank· DDBJ
BAG28983.1
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