A0A1Y6B3E7 · A0A1Y6B3E7_9BACT

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 site77substrate
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 site202a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site233a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site233a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloaminopeptidase activity
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
      SAMN06296036_101257

Organism names

Accessions

  • Primary accession
    A0A1Y6B3E7

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-239Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    256
  • Mass (Da)
    27,960
  • Last updated
    2017-08-30 v1
  • Checksum
    094501ABC890A9BA
MIYLKSDAEIDDMKEAGGLAAKLLELVEEHIKPGITTLELNDLCHDFTMSYGAISAPLNYKGFPKSICTSINDVVCHGIPSAKAKLKDGDIINVDVTPIVNGFHGDTSKTFLVGNVSPKRQKLVKVAKECLDKGIQVVEPGVRVGDIGAAIQKHAEAQKFSVVREFVGHGIGRNFHEDPQVTHYGQPGTGKRLEPGMVFTIEPMINEGHWKTKIKKDKWTAVTIDGGDSAQFEHTIAIRSNGTVEILTLIENYRGN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FWZT01000001
EMBL· GenBank· DDBJ
SME89383.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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