A0A1B3CRI9 · A0A1B3CRI9_PSEFL

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 site76substrate
Binding site94a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site105a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site105a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site168a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site175substrate
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
Cellular Componentcytosol
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
      IM720_14700

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KF1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A1B3CRI9

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-238Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    251
  • Mass (Da)
    27,616
  • Last updated
    2016-11-02 v1
  • MD5 Checksum
    DC696C966314F3A7726375A68469372F
MIKTPAQLTVMREAGRLLAQVFSMLDGFVIAGRSTLELDAAVEAFIRNDLKARPASLGQYDYPFSINTSINEVVCHGMPSAKDILKDGDIINIDITLEKGGFIADSSKMYMIGNVPPKARRLVEMTFEAMWAGIRQVKPGARLGDIGHAIQSHAQANGYSVVREYCGHGIGRQMHEEPQVLHFGRPGTGLELREGMVFTIEPMLNQGSAKVRSLKDGWTVVTKDNSLSAQWEHTVAVTRDGFEVLTLQKTD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP063233
EMBL· GenBank· DDBJ
QOU07912.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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