A0A1V5PMK5 · A0A1V5PMK5_9FIRM

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 site33ATP (UniProtKB | ChEBI)
Binding site36Zn2+ (UniProtKB | ChEBI); structural
Binding site39Zn2+ (UniProtKB | ChEBI); structural
Binding site42-43ATP (UniProtKB | ChEBI)
Binding site56Zn2+ (UniProtKB | ChEBI); structural
Binding site59Zn2+ (UniProtKB | ChEBI); structural
Binding site66AMP (UniProtKB | ChEBI)
Binding site77AMP (UniProtKB | ChEBI)
Binding site105ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functionzinc ion binding
Biological ProcessAMP salvage

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
      BWY61_02002

Organism names

Accessions

  • Primary accession
    A0A1V5PMK5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region32-69LID
Domain33-68Adenylate kinase active site lid

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
    119
  • Mass (Da)
    13,344
  • Last updated
    2017-06-07 v1
  • MD5 Checksum
    4A7DE01FF21FA5A36E357E5CB402A99E
MLDAELTKLNDKIDFAINVDVPDENIVRRMSGRRSCPSCGATYHIVHIPPKQEGVCDKCGAALVQRDDDKEETVKNRLKVYHEQTQPLIDFYEKKGVLQNVDGTVDSEEVFAAIVKILG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MWAW01000504
EMBL· GenBank· DDBJ
OQA18964.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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