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A0A315QVE1 · A0A315QVE1_9FIRM

  • 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.

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 site77substrate
Binding site95a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site106a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site106a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site169a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site176substrate
Binding site202a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site233a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site233a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

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
      CI949_3198

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 7-U2-L
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Halanaerobiales > Halanaerobiaceae > Halanaerobium

Accessions

  • Primary accession
    A0A315QVE1

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-240Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    249
  • Mass (Da)
    27,232
  • Last updated
    2018-10-10 v1
  • MD5 Checksum
    5C9CC9C3E0C154B545C19A4841C86503
MIILKSRREIDIMREANQIVAETHAYLAENIKPGISTAELDQLADEFIRSKGAVPSFKGYQGFPASICISINEEVVHGIPADHRFLEAGDIVSIDIGTFYEGFNGDAARTHAVGSISENASKLLKVTEESLLKGIEKAVIGNRLFDISHAVQEYVEKNGFSVVRDYVGHGIGRDMHEDPQIPNFGPAGKGPKLKKGMTLAIEPMVNIGGYEVETLEDDWTVVTKDRSLSAHFEHTIAITEAGVEILSKL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QBLR01000222
EMBL· GenBank· DDBJ
PUU88229.1
EMBL· GenBank· DDBJ
Genomic DNA

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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