Q5L3R7 · Q5L3R7_GEOKA

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 site77substrate
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 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
      GK0128

Organism names

Accessions

  • Primary accession
    Q5L3R7

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-239Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    255
  • Mass (Da)
    27,883
  • Last updated
    2005-02-01 v1
  • Checksum
    BF83D5C25DF690B9
MIRCKTAQEIALMREAGKIVSLTLKELQKHIRPGITTKELDAIAEEVIRSHGAIPSFKGYQGFPGSICASVNEELVHGIPSSRALREGDIITIDVGAQYEGYHADSAWTYPVGEIDAETKRLLDVTEQSLYVGLAEAKPGARLTNISHAIQTYVEAHHFSVVREYVGHGIGQHLHEDPQIPHYGPPNKGPILRPGMALCIEPMVNAGSRYVKTLADDWTVVTADGKRCAHFEHTIVITEDGCEILTHCGNESPTS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000043
EMBL· GenBank· DDBJ
BAD74413.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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