A0AAE5CF30 · A0AAE5CF30_RHOHA

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.

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

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 site83substrate
Binding site100a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site111a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site111a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site174a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site181substrate
Binding site207a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site239a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site239a 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
      GS505_05625

Organism names

Accessions

  • Primary accession
    A0AAE5CF30

Proteomes

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-246Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    256
  • Mass (Da)
    26,663
  • Last updated
    2024-05-29 v1
  • Checksum
    1486C85B30ED31EE
MVELKTESEIQGMRAAGRVVADALAAARAHAQVGVSLRELDAVAARVVADAGAEPLFLNYRPNWAATPFPGVLCTSVNDAVVHGIPSGYRLRDGDLVSIDGGARLNGWCGDSAISFVVGAANPADEALVAATDEALRRGIEAARVGNRLGDIGAAIGTFARSRGFGLLADHGGHGIGRVMHESPDVPNEARAGRGMRLRDGLVLAIEPMLIADGSDDYRHDADGWTLRTVTGARAAHSEHTVAITDDGPVVLTARH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WUYZ01000001
EMBL· GenBank· DDBJ
NKS25342.1
EMBL· GenBank· DDBJ
Genomic DNA

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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