A0A1E3RUR1 · A0A1E3RUR1_9MYCO

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 site10-15ATP (UniProtKB | ChEBI)
Binding site31AMP (UniProtKB | ChEBI)
Binding site36AMP (UniProtKB | ChEBI)
Binding site57-59AMP (UniProtKB | ChEBI)
Binding site85-88AMP (UniProtKB | ChEBI)
Binding site92AMP (UniProtKB | ChEBI)
Binding site127ATP (UniProtKB | ChEBI)
Binding site129AMP (UniProtKB | ChEBI)
Binding site140AMP (UniProtKB | ChEBI)
Binding site167ATP (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
    • ORF names
      BHQ17_12950

Organism names

  • Taxonomic identifier
  • Strain
    • M7
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium

Accessions

  • Primary accession
    A0A1E3RUR1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region30-59NMP

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
    182
  • Mass (Da)
    20,167
  • Last updated
    2017-01-18 v1
  • Checksum
    05AA8402688F55D1
MRVVLLGPPGAGKGTQAQKLSEKLGIPQISTGDLFRQNIGDGTPLGLEAKRYLDAGDLVPSELTNKLVEDRITQPDAAQGFILDGYPRSVEQAEALDEMLTQRNTKLDAVLEFVVSEEELFTRLKARGRADDTEEVIHNRMQVYRDETQPLLEYYRDNNLQTVDAVGGLDEVFARALHALGK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MIGZ01000065
EMBL· GenBank· DDBJ
ODQ93561.1
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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