HAMAP rule MF_01975

General rule information [?]

Accession	MF_01975
Dates	5-JUN-2013 (Created) 1-JUN-2023 (Last updated, Version 12)
Name	MetAP_2_arc
Scope(s)	Archaea
Template(s)	P56218 (MAP2_PYRFU); B6YTG0 (MAP2_THEON); [ Recover all ]
Triggered by	HAMAP; MF_01975 (Get profile general information and statistics)

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	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	Name=Co(2+); Xref=ChEBI:CHEBI:48828; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Fe(2+); Xref=ChEBI: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 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:0004239; Molecular function:initiator methionyl aminopeptidase activity

Cross-references [?]

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 [?]