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HAMAP rule MF_01975

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General rule information [?]

Accession MF_01975
Dates 5-JUN-2013 (Created)
19-NOV-2022 (Last updated, Version 10)
Name MetAP_2_arc
Scope
Archaea
Templates P56218 (MAP2_PYRFU); B6YTG0 (MAP2_THEON): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
MAP2
Protein name
RecName: Full=Methionine aminopeptidase;
Short=MAP;
Short=MetAP;
EC 3.4.11.18;
AltName: Full=Peptidase M;
Gene name
map

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).
Catalytic activity Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18;
Cofactor Co(2+)
Zn(2+)
Mn(2+)
Fe(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 archaeal type 2 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0046872; Molecular function: metal ion binding.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0070084; Biological process: protein initiator methionine removal.

Cross-references [?]

PROSITE PS01202; MAP_2; 1;
Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
TIGRFAMs TIGR00501; met_pdase_II; 1;

Features [?]

From: MAP2_PYRFU (P56218)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     82     82       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     D   1
BINDING     93     93       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     D   1
BINDING     93     93       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     D   1
BINDING     153     153       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     H   1
BINDING     187     187       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     E   1
BINDING     280     280       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     E   1
BINDING     280     280       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     E   1
BINDING     62     62       /ligand="substrate     H  
BINDING     161     161       /ligand="substrate     H  

Additional information [?]

Size range 284-307 amino acids
Related rules None
Fusion None