A0A1Z4MW41 · A0A1Z4MW41_9CYAN

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.

118420406080100120140160180
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 site130AMP (UniProtKB | ChEBI)
Binding site141AMP (UniProtKB | ChEBI)
Binding site169ATP (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

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
      NIES37_16500

Organism names

  • Taxonomic identifier
  • Strain
    • NIES-37
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Tolypothrichaceae > Tolypothrix

Accessions

  • Primary accession
    A0A1Z4MW41

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region31-60NMP

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    184
  • Mass (Da)
    20,468
  • Last updated
    2017-09-27 v1
  • Checksum
    6B6D2E5520403C19
MTQLIFLGPPGAGKGTQSQKLAQSLQIPHISTGDILRQAMKDQTPLGVKAQSYVDSGELVPDELVQDLVQERLGQADAQSGWILDGFPRKVSQAEFLAKLLETIHQAGERVVNLDVPDDVVVARLLARGRKDDSEEVIRRRLEIYRSETAPLINYYRDRQKLLTVNGNQSPEEVTDALHKVIAF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP018248
EMBL· GenBank· DDBJ
BAY97706.1
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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