A0A1B9B0W3 · A0A1B9B0W3_9BACI

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 site76substrate
Binding site93a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site104a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site104a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site167a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site174substrate
Binding site201a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site232a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site232a divalent metal cation 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
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
      A8L44_02325

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FJAT-27986
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0A1B9B0W3

Proteomes

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-239Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    247
  • Mass (Da)
    26,716
  • Last updated
    2016-11-02 v1
  • Checksum
    D4C23CA40202EFFB
MIVKNEKDLEGLKAVGAVVSRVREAMKLATVPGITTLELDLIAKKIFEETGAVSAPKNEYDFPGFTCISVNEEVAHGIPGKRIINEGDMVNIDVSAVLNGYYGDTGISFPVGTTTSEKEKLCQCAVDAFYQGISKAKAGSKKNQIGKAVFNTAKQNGFTVIKNLTGHGIGRSLHEKPDHILNYFDPWDSELLHEGTVLAVEPFISTKATMVTEAGDGWTFITSDKSLVAQCEHTIIVTKNEPIILTL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MAYV01000001
EMBL· GenBank· DDBJ
OCA89795.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help