AC   MF_01279;
DC   Protein; auto
TR   HAMAP; MF_01279; -; 1; level=0
XX
Names: X_Pro_dipeptid
XX
ID   PEPQ
DE   RecName: Full=Xaa-Pro dipeptidase;
DE            Short=X-Pro dipeptidase;
DE            EC=3.4.13.9;
DE   AltName: Full=Imidodipeptidase;
DE   AltName: Full=Proline dipeptidase;
DE            Short=Prolidase;
GN   Name=pepQ;
XX
CC   -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal
CC       position.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline;
CC         Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 manganese ions per subunit.;
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type
CC       prolidase subfamily.
XX
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1; trigger=no
DR   Pfam; PF00557; Peptidase_M24; 1; trigger=no
XX
KW   Dipeptidase
KW   Hydrolase
KW   Manganese
KW   Metal-binding
KW   Metalloprotease
KW   Protease
XX
GO   GO:0008235; F:metalloexopeptidase activity
GO   GO:0016805; F:dipeptidase activity
XX
FT   From: PEPQ_ECOLI (P21165)
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         384
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: E
XX
Size: 429-452;
Related: None;
Template: P21165; Q44238; P77814;
Scope:
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in IDILO
Plasmid: None
Comments: PepQ from Alteromonas sp. and Pseudoalteromonas haloplanktis was also shown to
 efficiently catalyze the hydrolysis of toxic organophosphorus cholinesterase-inhibiting
 compounds including insecticide paraoxon and nerve gases such as O-isopropyl
 methylphosphonofluoridate (sarin) and O-pinacolyl (soman).
XX
# Revision 1.16 2023/05/26
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