A0A0D1E3G9 · A0A0D1E3G9_USTMA

Function

function

Cotranslationally 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).

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 site144substrate
Binding site161a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site172a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site172a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site238a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site245substrate
Binding site271a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site303a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site303a divalent metal cation 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentcytosolic ribosome
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetalloaminopeptidase activity
Molecular FunctionmRNA binding
Molecular Functionzinc ion binding
Biological Processnegative regulation of gene expression
Biological Processprotein processing

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine aminopeptidase
  • EC number

Gene names

    • ORF names
      UMAG_10253

Organism names

Accessions

  • Primary accession
    A0A0D1E3G9

Proteomes

Organism-specific databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain79-310Peptidase M24
Region340-387Disordered
Compositional bias354-378Polar residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    387
  • Mass (Da)
    42,003
  • Last updated
    2015-04-29 v1
  • MD5 Checksum
    45F56B5AB347602E2597DF3FDD66F499
MPPTATNQGSSDDKAAASTSTFDPFAHIRSFKYSGSLKAVYPLSPKPKIPPSIRRPNYAREGFLESRNIKVNNKADQDGVRKAAALAREVLEIAAAHAKPGVTTDELDKIVFAEAIKRDCYPSPLGYHGYPKSVCTSINEVICHGIPDQRPLEDGDILNLDVTLFHKGYHGDLNATFPVGKKAEDDAESMKLIRVARECLDAAINICGPGVPYGEIGRVIQPLAESQGCAVVKNYTGHGISNCFHAAPTVYHHATKKSYGIMKPGHIFTIEPMLNLGTEWRDLSWPDDWTVATVDGARSAAAEETLLITETGVEILTAKGGPRHIDTTERRKLLEQQIKSREERKKRRKLDNGGASTPVSDTATETPAPENTNVTTKIASGPAVPES

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias354-378Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM003142
EMBL· GenBank· DDBJ
KIS70659.1
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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