A0AAC8N1M9 · A0AAC8N1M9_HELPX

Function

function

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.

Catalytic activity

  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
    EC:3.4.11.18 (UniProtKB | ENZYME | Rhea)

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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site78substrate
Binding site95a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site106a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site106a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site169a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site176substrate
Binding site206a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site237a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site237a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetalloaminopeptidase activity
Molecular Functiontransition metal ion binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine aminopeptidase
  • EC number
  • Short names
    MAP
    ; MetAP
  • Alternative names
    • Peptidase M

Gene names

    • Name
      map
    • ORF names
      C2840_06750
      , C2842_06745
      , SE88_06700

Organism names

  • Taxonomic identifier
  • Strains
    • 26695-1MET
    • 26695-dR
    • 26695-dRdM2
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    A0AAC8N1M9

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Structure

3D structure databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-241Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    253
  • Mass (Da)
    27,577
  • Last updated
    2024-05-29 v1
  • MD5 Checksum
    7588ADBA7E2834E3F62BC5DED9689550
MAISIKSPKEIKALRKAGELTAQALALLEREVRPGVSLLELDKMAEDFIKSSHARPAFKGLYGFPNSVCMSLNEVVIHGIPTDYVLQEGDIIGLDLGVEVDGYYGDSALTLPIGAISPQDEKLLACSKESLMHAINSIRVGMHFKELSQILESTITERGFVPLKGFCGHGIGKKPHEEPEIPNYLEKGVKPNSGPKIKEGMVFCLEPMVCQKQGEPKILADKWSVVSVDGLNTSHHEHTIAIVGNKAVILTER

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010436
EMBL· GenBank· DDBJ
AJF11061.1
EMBL· GenBank· DDBJ
Genomic DNA
CP026326
EMBL· GenBank· DDBJ
AUV78420.1
EMBL· GenBank· DDBJ
Genomic DNA
CP026324
EMBL· GenBank· DDBJ
AUV79929.1
EMBL· GenBank· DDBJ
Genomic DNA

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Disclaimer

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