A0A918TGD4 · A0A918TGD4_9BACT

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site15-20ATP (UniProtKB | ChEBI)
Binding site36AMP (UniProtKB | ChEBI)
Binding site41AMP (UniProtKB | ChEBI)
Binding site62-64AMP (UniProtKB | ChEBI)
Binding site88-91AMP (UniProtKB | ChEBI)
Binding site95AMP (UniProtKB | ChEBI)
Binding site126ATP (UniProtKB | ChEBI)
Binding site129Zn2+ (UniProtKB | ChEBI); structural
Binding site132Zn2+ (UniProtKB | ChEBI); structural
Binding site143Zn2+ (UniProtKB | ChEBI); structural
Binding site146Zn2+ (UniProtKB | ChEBI); structural
Binding site153AMP (UniProtKB | ChEBI)
Binding site164AMP (UniProtKB | ChEBI)
Binding site192ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionzinc ion binding
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
    • ORF names
      GCM10007100_07810

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KCTC 12988
  • Taxonomic lineage
    Bacteria > Verrucomicrobiota > Verrucomicrobiia > Verrucomicrobiales > Verrucomicrobiaceae > Roseibacillus

Accessions

  • Primary accession
    A0A918TGD4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region35-64NMP

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
    206
  • Mass (Da)
    22,769
  • Last updated
    2023-02-22 v1
  • Checksum
    D87945E33F0CE9A2
MPADVRCFTMLGPPASGKGTQGRLLAERLGIAYLSTGARLRREIEEGSPLGQRAQVFLDRNQYVPDSLAVELVKSWVLRHEEGWLLDGFPRSIPQAEALLEFAPQAFTVIHLSVPEEELRSRVVTRRECISCGFVSTNDHKQCPKCGGELEARADDSAEGFEKRFQAYQSLTIPALELLKTRTTVVTIEGLGSREEVAGAIQDQLT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BMXI01000002
EMBL· GenBank· DDBJ
GHC44937.1
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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