HAMAP rule MF_01975

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]

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

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 [?]

Aminopeptidase
Hydrolase
Metal-binding
Protease

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

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