A0A172Z1W8 · A0A172Z1W8_9PSED

  • Protein
    Methionine aminopeptidase
  • Gene
    map
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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
      A7J50_2610

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PAMC 27494
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A172Z1W8

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-239Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    251
  • Mass (Da)
    27,389
  • Last updated
    2016-09-07 v1
  • Checksum
    8CACE53FFB8D6742
MIKTAAQLAVMRESGRLLAQVFTMLDGFVAAGRSTLELDSAVEAFIRNDLNARPASLGQYDYPFCINTSINEVVCHGMPSAKEILKDGDIINIDITLEKGGFIADSSKMYMIGNVAPKAQRLVEKTFEAMWAGIRQVRPGARLGDIGHAIQSHAQANGYSVVREYCGHGIGREMHEEPQILHFGRPGTGLELREGMVFTIEPMLNQGSAKVRSLKDGWTVVTKDNSLSAQWEHTVAVTASGFEILTLQPAV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP015600
EMBL· GenBank· DDBJ
ANF86009.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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