AC   MF_00181;
DC   Protein; auto
TR   HAMAP; MF_00181; -; 1; level=0
XX
Names: Cytosol_peptidase_M17
XX
ID   AMPA
DE   RecName: Full=Probable cytosol aminopeptidase;
DE            EC=3.4.11.1;
DE   AltName: Full=Leucine aminopeptidase;
DE            Short=LAP;
DE            EC=3.4.11.10;
DE   AltName: Full=Leucyl aminopeptidase;
GN   Name=pepA;
XX
CC   -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC       intracellular proteins. Catalyzes the removal of unsubstituted N-
CC       terminal amino acids from various peptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC         is preferably Leu, but may be other amino acids including Pro
CC         although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC         methyl esters are also readily hydrolyzed, but rates on arylamides
CC         are exceedingly low.; EC=3.4.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC         but not glutamic or aspartic acids.; EC=3.4.11.10;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 manganese ions per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
XX
DR   Pfam; PF00883; Peptidase_M17; 1; trigger=no
DR   PRINTS; PR00481; LAMNOPPTDASE; 1; trigger=no
DR   PROSITE; PS00631; CYTOSOL_AP; 1; trigger=no
XX
KW   Cytoplasm
KW   Hydrolase
KW   Protease
KW   Aminopeptidase
KW   Manganese
KW   Metal-binding
XX
GO   GO:0004177; F:aminopeptidase activity
GO   GO:0008235; F:metalloexopeptidase activity
GO   GO:0030145; F:manganese ion binding
GO   GO:0005737; C:cytoplasm
XX
FT   From: AMPA_ECOLI (P68767)
FT   ACT_SITE        282
FT   Condition: K
FT   ACT_SITE        356
FT   Condition: R
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: K
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: E
XX
Size: 445-524;
Related: MF_00504;
Template: P68767; P27888;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in SHEON
Plasmid: None
Comments: Possible wrong C-terminal sequence in METSV
XX
# Revision 1.37 2023/01/17
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