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HAMAP rule MF_01974

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General rule information [?]

Accession MF_01974
Dates 31-MAY-2013 (Created)
1-JUN-2023 (Last updated, Version 11)
Name MetAP_1
Templates P0AE18 (MAP1_ECOLI); P9WK19 (MAP12_MYCTU); Q9ZCD3 (MAP1_RICPR): [Recover all]
case <OC:Bacteria>
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Methionine aminopeptidase;
AltName: Full=Peptidase M;
Gene name

Comments [?]

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 Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=;
Cofactor Co(2+)
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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Subunit Monomer.
Similarity Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Keywords [?]

Gene Ontology [?]

GO:0046872; Molecular function: metal ion binding.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0004239; Molecular function: initiator methionyl aminopeptidase activity.

Cross-references [?]

PROSITE PS00680; MAP_1; 1;
Pfam PF00557; Peptidase_M24; 1;
NCBIfam TIGR00500; met_pdase_I; 1;

Features [?]

From: MAP1_ECOLI (P0AE18)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     97     97       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     D   1
BINDING     108     108       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     D   1
BINDING     108     108       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     D   1
BINDING     171     171       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     H   1
BINDING     204     204       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     E   1
BINDING     235     235       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     E   1
BINDING     235     235       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     E   1
BINDING     79     79       /ligand="substrate     H  
BINDING     178     178       /ligand="substrate     H  

Additional information [?]

Size range 248-305 amino acids
Related rules None
Fusion None