A0A7L5ZF91 · A0A7L5ZF91_9ACTN

  • Protein
    Multifunctional fusion protein
  • Gene
    map
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.

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 site92AMP (UniProtKB | ChEBI)
Binding site127ATP (UniProtKB | ChEBI)
Binding site133AMP (UniProtKB | ChEBI)
Binding site144AMP (UniProtKB | ChEBI)
Binding site163ATP (UniProtKB | ChEBI)
Binding site280substrate
Binding site297a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site308a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site308a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site373a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site380substrate
Binding site406a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site437a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site437a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloaminopeptidase activity
Biological ProcessAMP salvage
Biological Processphosphorylation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Adenylate kinase
  • EC number
  • Short names
    AK
  • Alternative names
    • ATP-AMP transphosphorylase
    • ATP:AMP phosphotransferase
    • Adenylate monophosphate kinase
  • Recommended name
    Methionine aminopeptidase
  • EC number
  • Short names
    MAP
    ; MetAP
  • Alternative names
    • Peptidase M

Gene names

    • Name
      map
    • Synonyms
      adk
    • ORF names
      HZY73_05670

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SSC1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Micropruina

Accessions

  • Primary accession
    A0A7L5ZF91

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region30-59NMP
Domain209-443Peptidase M24

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    472
  • Mass (Da)
    50,633
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    F2C881F9EB4E6EDDACA16025A29A28FF
MRLLIMGPPGAGKGTQAQGIAARYEIPAISTGMIFRENITNRTALGEQIKRIISSGGYVPDELTLKVIFERLAADDCRNGWLLDGXPRTLGQVTALAERMAARGTHLDAVISITGNVDELVARMLKRAEIEGRADDNEETIRHRFQVYAEQTDXRCWPTTASRGSWSRWTAWAASRRLRSGSRRRWTPSSPLXVSRAGIEVKRPDQIIAMRAAGLVVARTLAAVKAAAAPGVTTGELDQLAREELARAGATSSFLGYGAGFRLPPXPGVTCISVNSEIVHGIPGERVLAPGDIVSVDFGAILNGWHGDSAITFGVGELAAGAQRLSDVTREAMWRGIAAARVGARIGDVGHAIERYVGAQPERYGIVREYTGHGIGTAMHXTPDVPNYGRPHRGPMLVNGMCLAIEPMLTLGGEGTATLDDEWTVVTRDGSLASHWEHTIAITRRGVWVLTAEDGGEELLTALGGRFGPLAD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP059261
EMBL· GenBank· DDBJ
QLQ15268.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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