HAMAP logo

HAMAP rule MF_01279

Send feedback

General rule information [?]

Accession MF_01279
Dates 15-AUG-2007 (Created)
19-NOV-2022 (Last updated, Version 15)
Name X_Pro_dipeptid
Bacteria; Gammaproteobacteria
Templates P21165 (PEPQ_ECOLI); Q44238 (PEPQ_ALTSX); P77814 (PEPQ_PSEHA): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Xaa-Pro dipeptidase;
Short=X-Pro dipeptidase;
AltName: Full=Imidodipeptidase;
AltName: Full=Proline dipeptidase;
Gene name

Comments [?]

Function Splits dipeptides with a prolyl residue in the C-terminal position.
Catalytic activity Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.; EC=;
Cofactor Mn(2+)
Note: Binds 2 manganese ions per subunit.
Similarity Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.

Keywords [?]

Gene Ontology [?]

GO:0008235; Molecular function: metalloexopeptidase activity.
GO:0016805; Molecular function: dipeptidase activity.

Cross-references [?]

Pfam PF00557; Peptidase_M24; 1;

Features [?]

From: PEPQ_ECOLI (P21165)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     246     246       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     D  
BINDING     257     257       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     D  
BINDING     257     257       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     D  
BINDING     339     339       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     H  
BINDING     384     384       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     E  
BINDING     423     423       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     E  
BINDING     423     423       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     E  

Additional information [?]

Size range 429-452 amino acids
Related rules None
Fusion 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).