F4FYF2 · F4FYF2_METCR

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).

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 site65substrate
Binding site85a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site96a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site96a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site156a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site164substrate
Binding site189a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site283a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site283a divalent metal cation 1 (UniProtKB | ChEBI)

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
    • Ordered locus names
      Mcup_0162

Organism names

Accessions

  • Primary accession
    F4FYF2

Proteomes

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-197Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    297
  • Mass (Da)
    33,150
  • Last updated
    2011-06-28 v1
  • Checksum
    B5C2FD97FAF66D8E
MTEDELKLVKTAGEIAAKARDLGAKLIKPGVKVIDVCESVEKAIIEHGARPAFPCNLSINQEAAHYSPIIGDEKVIPEEAIVKLDIGAHIDGYITDTAITVYLNDRMERLAEAAKDALRAAISNFKAGASLSDIGRSIEKIIKSYGYKPIRNLGGHLIRRYELHAGVFVPNVFERIPGRIQVGNTYAIEPFATDGGGEVIEGKDVTIYSLRNKNVRELDENERRLSEEIERRFRTLPFSERWLGDLGEKEEIERLLKILSKKGVLHSYPVLIEVKKGLVSQFEHTVYVDDNETTILT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002656
EMBL· GenBank· DDBJ
AEB94271.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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