AC   MF_01974;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01974; -; 1; level=0
XX
Names: MetAP_1
XX
ID   MAP1
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). Requires deformylation of the N(alpha)-formylated
CC       initiator methionine before it can be hydrolyzed.
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 type 1 subfamily.
XX
DR   PROSITE; PS00680; MAP_1; 1; trigger=no
DR   Pfam; PF00557; Peptidase_M24; 1; trigger=no
DR   PRINTS; PR00599; MAPEPTIDASE; 1; trigger=no
DR   NCBIfam; TIGR00500; met_pdase_I; 1; trigger=no
XX
KW   Aminopeptidase
KW   Hydrolase
KW   Protease
KW   Metal-binding
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: MAP1_ECOLI (P0AE18)
FT   BINDING         97
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Group: 1; Condition: D
FT   BINDING         108
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Group: 1; Condition: D
FT   BINDING         108
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         171
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         204
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         235
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Group: 1; Condition: E
FT   BINDING         235
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         79
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         178
FT                   /ligand="substrate"
FT   Condition: H
XX
Size: 248-305;
Related: None;
Template: P0AE18; P9WK19; Q9ZCD3;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACSU, MYCTU, SYNY3
Plasmid: None
Comments: None
XX
# Revision 1.11 2023/06/01
//