A0A232ERL3 · A0A232ERL3_9HYME

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.

Caution

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

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site29-34ATP (UniProtKB | ChEBI)
Binding site50AMP (UniProtKB | ChEBI)
Binding site55AMP (UniProtKB | ChEBI)
Binding site76-78AMP (UniProtKB | ChEBI)
Binding site104-107AMP (UniProtKB | ChEBI)
Binding site111AMP (UniProtKB | ChEBI)
Binding site157ATP (UniProtKB | ChEBI)
Binding site166-167ATP (UniProtKB | ChEBI)
Binding site190AMP (UniProtKB | ChEBI)
Binding site201AMP (UniProtKB | ChEBI)
Binding site229ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentintraciliary transport particle A
Cellular Componentmitochondrial intermembrane space
Cellular Componentnon-motile cilium
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Biological ProcessADP biosynthetic process
Biological ProcessAMP metabolic process
Biological ProcessATP metabolic process
Biological Processintraciliary retrograde transport
Biological Processnon-motile cilium assembly
Biological Processphosphorylation
Biological Processprotein localization to cilium

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
      Ak2
    • ORF names
      TSAR_008652

Organism names

  • Taxonomic identifier
  • Strain
    • Alberta
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Proctotrupomorpha > Chalcidoidea > Pteromalidae > Pteromalinae > Trichomalopsis

Accessions

  • Primary accession
    A0A232ERL3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, repeat.

TypeIDPosition(s)Description
Region1-34Disordered
Region49-78NMPbind
Region156-193LID
Domain157-192Adenylate kinase active site lid
Repeat306-337WD
Domain360-448Anaphase-promoting complex subunit 4-like WD40

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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,151
  • Mass (Da)
    127,951
  • Last updated
    2017-10-25 v1
  • Checksum
    FBCDF9417C217001
MAPKTESLPKENVEEPSRGINAVLLGPPGSGKGTQAPMLKERYCVCHLSTGDMLRAEIQSGSALGAELKKVMDAGKLVSDDLVVNMIDKNLEKPECQRGFLLDGFPRTVPQAEKVATAAINICVTLDEMLEKKKTKLDAVIEFGIDDNLLVKRITGRLIHPASGRSYHEEFAPPKVAMKDDITGEPLIKRSDDNAEALKKRLASYHSQTQPLVDYYALRGIHNYVNAAKSSEQVFKDIDTIFLTAIQADQKKAWNQKQGYIAVGGEDGLLKVIRADSGASTTDNTNNSGKTRSMTASSNLSMNQTLEGHNGHIQVVTWNEEHQKLTSSDQNGVIIVWMLYKGSWNEEMINNRNKSVVRGMSWSSNGQKICIVYEDGAVIVGSVEGNRIWGKELKGLSLTAVQWSPDAKFLLFGTRNGEAHLYDDQGVFLTKLENISNGRVQGIVALDWYNGKNGYTAVDCPVLAVCFQSGRMVLLRDISDENPIVVDTGMTMACCVWNTYGSLLAIAGILMGEDKNNSNVVCFYSSLGDHLKTLKIPGKDISCCAWEGGSLRIALSVDSNIYFANIRPNYKWAYFGTTVVFTDDKVGKDGVCVTFWNTVTNARYFKYVSSLISIVACGDHCVLAAKNDLTQSEERYALYVCNAISTPVDTKYLDLEPNQVAMNQNMVIAASKSNFLLWYFRAPRNSALNASGKSRRDRLYHVDDTPTGVTEVIQDLDRDKTYESPISRRETVDPICCISASEKLLIVGRESGMVQQYSLPQVTLSKRYSTSRKPCKISINCDSTRAAIIDSQGLLRLLDLATVKDRDRERDRDDGRDKDKADDVSKFERKDAWAVCWAQDNPKLFAILEKSRMYVFRGLEPEEPITCSGYVCSFKDLEIRCVLLDELVRNPEEARPELLVELEIKSLRDTKELLARVGLREAEEFVRDNSHPRLWRLLGEHALRQGDLEAAENAMVRCADYLGIRFVKRLRGIQEPGLRRAEVLGFLGAGRRLQAIELYRKADCPLDAAKLLLELAAEQARRRAPPLRLKKLYVLAALLVQEHLEGTRPGQVRRGLLAGLSEASGEDAQVVEQAWRGAEAYHFLLLAHLPDYCVACPNCATGFPACVVSGRPLMNQASTWLCTVCKHRAASERDVVNVNGCPLCHSIITYM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NNAY01002594
EMBL· GenBank· DDBJ
OXU20972.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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