B3LG61 · KAD2_YEAS1

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. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.

Catalytic activity

Features

Showing features for binding site.

122220406080100120140160180200220
TypeIDPosition(s)Description
Binding site16-21ATP (UniProtKB | ChEBI)
Binding site37AMP (UniProtKB | ChEBI)
Binding site42AMP (UniProtKB | ChEBI)
Binding site63-65AMP (UniProtKB | ChEBI)
Binding site92-95AMP (UniProtKB | ChEBI)
Binding site99AMP (UniProtKB | ChEBI)
Binding site134ATP (UniProtKB | ChEBI)
Binding site143-144ATP (UniProtKB | ChEBI)
Binding site167AMP (UniProtKB | ChEBI)
Binding site178AMP (UniProtKB | ChEBI)
Binding site206ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrial intermembrane space
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Biological ProcessADP biosynthetic process
Biological ProcessAMP metabolic process
Biological ProcessATP metabolic process
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate kinase
  • EC number
  • Alternative names
    • ATP-AMP transphosphorylase
    • ATP:AMP phosphotransferase
    • Adenylate kinase cytosolic and mitochondrial
    • Adenylate monophosphate kinase

Gene names

    • Name
      ADK1
    • ORF names
      SCRG_00298

Organism names

Accessions

  • Primary accession
    B3LG61

Proteomes

Subcellular Location

Cytoplasm, cytosol
Note: Predominantly mitochondrial.

Keywords

PTM/Processing

Features

Showing features for initiator methionine, propeptide, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
PropeptidePRO_00003656912Removed in mature form
Modified residue2N-acetylserine
Modified residue3N-acetylserine
ChainPRO_00003656923-222Adenylate kinase

Keywords

Interaction

Subunit

Monomer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region36-65NMP
Region133-170LID

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. AK2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    222
  • Mass (Da)
    24,255
  • Last updated
    2008-09-02 v1
  • Checksum
    FE566FD8015907CE
MSSSESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQIAKGTQLGLEAKKIMDQGGLVSDDIMVNMIKDELTNNPACKNGFILDGFPRTIPQAEKLDQMLKEQGTPLEKAIELKVDDELLVARITGRLIHPASGRSYHKIFNPPKEDMKDDVTGEALVQRSDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDASQPPATVWADILNKLGKD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH408043
EMBL· GenBank· DDBJ
EDV08090.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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