A0A6H3AB95 · A0A6H3AB95_BACAN

  • Protein
    Methionine aminopeptidase
  • Gene
    maP2
  • 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 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
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
      maP2
    • Synonyms
      map
    • Ordered locus names
      GBAA_1590

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Ames ancestor
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group

Accessions

  • Primary accession
    A0A6H3AB95
  • Secondary accessions
    • A0A0F7REQ1
    • E9R667
    • E9R668
    • Q6I0Y8
    • Q6KUU2
    • Q81SQ6

Proteomes

Interaction

Subunit

Monomer.

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
    248
  • Mass (Da)
    27,149
  • Last updated
    2020-10-07 v1
  • Checksum
    3D03486581721543
MITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKGINTFVETYLEKHGATSEQKGYNGYPYAVCASVNDEMCHGFPNEIPLNEGDIVTIDMVVNLNGGLSDSAWTYIVGNVSDEAERLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSVARDFTGHGIGKKIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYCKVDLNGWTARTMDGKLSAQYEHTIVITKDGPIILTKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017334
EMBL· GenBank· DDBJ
AAT30689.1
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.
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.
FeedbackHelp