AC   MF_01975;
DC   Protein; auto
TR   HAMAP; MF_01975; -; 1; level=0
XX
Names: MetAP_2_arc
XX
ID   MAP2
DE   RecName: Full=Methionine aminopeptidase;
DE            Short=MAP;
DE            Short=MetAP;
DE            EC=3.4.11.18;
DE   AltName: Full=Peptidase M;
GN   Name=map;
XX
CC   -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC       N-terminal methionine is often cleaved when the second residue in the
CC       primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC       Thr, or Val).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC       and a low affinity metal-binding site. The true nature of the
CC       physiological cofactor is under debate. The enzyme is active with
CC       cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC       aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC       physiological conditions, and the catalytically relevant metal-binding
CC       site has been assigned to the histidine-containing high-affinity site.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase archaeal type 2 subfamily.
XX
DR   PROSITE; PS01202; MAP_2; 1; trigger=no
DR   Pfam; PF00557; Peptidase_M24; 1; trigger=no
DR   PRINTS; PR00599; MAPEPTIDASE; 1; trigger=no
DR   NCBIfam; TIGR00501; met_pdase_II; 1; trigger=no
XX
KW   Aminopeptidase
KW   Hydrolase
KW   Metal-binding
KW   Protease
XX
GO   GO:0046872; F:metal ion binding
GO   GO:0070006; F:metalloaminopeptidase activity
GO   GO:0004239; F:initiator methionyl aminopeptidase activity
XX
FT   From: MAP2_PYRFU (P56218)
FT   BINDING         82
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Group: 1; Condition: D
FT   BINDING         93
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Group: 1; Condition: D
FT   BINDING         93
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: D
FT   BINDING         153
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         187
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         280
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Group: 1; Condition: E
FT   BINDING         280
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         62
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         161
FT                   /ligand="substrate"
FT   Condition: H
XX
Size: 284-307;
Related: None;
Template: P56218; B6YTG0;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.12 2023/06/01
//