A0A0G0FG21 · A0A0G0FG21_9BACT

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 site101a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site112a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site112a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site176a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site183substrate
Binding site209a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site240a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site240a 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
      UR90_C0030G0003

Organism names

Accessions

  • Primary accession
    A0A0G0FG21

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-247Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    256
  • Mass (Da)
    28,244
  • Last updated
    2015-07-22 v1
  • Checksum
    EFE4768EEC662AB8
MIIIKTPEEIEILREGGKHLASVLFKLKERVASGISTKELDSYALKLIRDFGDEPAFLNYRPMGARTPFPSSLCVSVNDEVVHGIPNEDRVLKEGDIVSLDLGLKHKGLFTDMAITVPVGKISVSNQKLLEVTEKALQIGISVAQRGNTTGDIGYAIEKFVRLQGKYGIVEILAGHGVGREIHEDPYIPNFGKKGKGEELIPGMVIAIEPMINNGTKNVTIDDDEWTFRTADRKNSAHFEHTILITESEPEVLTKL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LBQY01000030
EMBL· GenBank· DDBJ
KKP86420.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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