A0A1Q7JXU3 · A0A1Q7JXU3_9ARCH

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

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

Cofactor

Protein has several cofactor binding sites:
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.
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site62substrate
Binding site82a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site93a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site93a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site153a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site161substrate
Binding site187a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site282a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site282a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
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
      AUJ08_08220

Organism names

Accessions

  • Primary accession
    A0A1Q7JXU3

Proteomes

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-200Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    297
  • Mass (Da)
    32,986
  • Last updated
    2017-04-12 v1
  • Checksum
    A5372BD4704B5AB8
MNFECYLQAGKIAAQVREGARRKYYVGSTLFEICESVEAQIRSMNGQPAFPVNTSLNEIAAHYTAEPNDATVVKEGDVLKIDIGVHVDGYIADTAVTLCYDAKYESLVKAAETALGEAVRMARANTKASDIGRVIEGTIVKFGFRPIQNLSGHSLKQYTIHAGKSIPNIWTIGSSFTLLANEAYAIEPFVTTKDGQGVVHEGKTRNIFGITSRKPIKDKEADNLLELMWTRFRTLPFALRWLTDKYEEKDLRRLVDILAKKRNVHAYPILVEGRGKIVAQAEHTLIPTDSVVNVITL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MNFY01000309
EMBL· GenBank· DDBJ
OLC80727.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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