A0A0K0E5I3 · A0A0K0E5I3_STRER

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

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 site106-109AMP (UniProtKB | ChEBI)
Binding site113AMP (UniProtKB | ChEBI)
Binding site144ATP (UniProtKB | ChEBI)
Binding site150AMP (UniProtKB | ChEBI)
Binding site161AMP (UniProtKB | ChEBI)
Binding site189ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function(d)CMP kinase activity
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionnucleoside diphosphate kinase activity
Biological ProcessADP biosynthetic process
Biological ProcessAMP metabolic process
Biological ProcessATP metabolic process
Biological Processnucleoside triphosphate biosynthetic process
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate kinase isoenzyme 1
  • EC number
  • Short names
    AK 1
  • Alternative names
    • ATP-AMP transphosphorylase 1
    • ATP:AMP phosphotransferase
    • Adenylate monophosphate kinase

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Strongyloidoidea > Strongyloididae > Strongyloides

Accessions

  • Primary accession
    A0A0K0E5I3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region49-78NMPbind
Region143-153LID

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. AK1 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    206
  • Mass (Da)
    22,795
  • Last updated
    2015-10-14 v1
  • MD5 Checksum
    F8652B271D2C954A0A7AFE07A3DAF426
MMAPTKKNIDLSALKKANVPIIFIVGGPGSGKGTQCDKIVAKYGFTHISSGDLLREELKSGSERAGELLKIMELGQLVPMEVVLDLIKERILQSIEKGSKGFLIDGYPREVVQGEKFEAEIQEAKTVIYFEVAESTLVKRLLGRAQTSGRADDNEETIKKRITTFNQSTAPVVDYYEKKGKLYKINAEGSVDEIFSKVSTHLDKIL

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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