Q98Q02 · KAD_MYCPU

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.

121420406080100120140160180200
TypeIDPosition(s)Description
Binding site12-17ATP (UniProtKB | ChEBI)
Binding site33AMP (UniProtKB | ChEBI)
Binding site38AMP (UniProtKB | ChEBI)
Binding site59-61AMP (UniProtKB | ChEBI)
Binding site88-91AMP (UniProtKB | ChEBI)
Binding site95AMP (UniProtKB | ChEBI)
Binding site127ATP (UniProtKB | ChEBI)
Binding site130Zn2+ (UniProtKB | ChEBI); structural
Binding site133Zn2+ (UniProtKB | ChEBI); structural
Binding site150Zn2+ (UniProtKB | ChEBI); structural
Binding site153Zn2+ (UniProtKB | ChEBI); structural
Binding site160AMP (UniProtKB | ChEBI)
Binding site171AMP (UniProtKB | ChEBI)
Binding site199ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentintracellular membrane-bounded organelle
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionnucleoside diphosphate kinase activity
Molecular Functionzinc ion binding
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
      MYPU_5670

Organism names

Accessions

  • Primary accession
    Q98Q02

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001588051-214Adenylate kinase

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region32-61NMP
Region126-163LID

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    214
  • Mass (Da)
    24,564
  • Last updated
    2001-10-01 v1
  • MD5 Checksum
    8E6D27AEC3B6373C0AA79D6F8393BA52
MIKRFIVFGPPGVGKGTLASLVSQKYGFEHISTGNIFRSQIASNSELGIKLKEIVESGGYVPDSITNEIVKKTLADLEKEQKSYILDGYPRTLNQIEFLFSLNKAQEYSVWFLEAPSEIILKRLSGRRICPSCNAQYHIYFKKSKLDTKCEIDQSELIQRKDDQESSIIKRLEIYEKQTNSLKKYFKELGILVEIDASKDREEILKELEQKVSL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL445565
EMBL· GenBank· DDBJ
CAC13740.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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