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HAMAP annotation rule: MF_01279
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General rule information

Accession MF_01279
Dates 15-AUG-2007 (Created)
18-AUG-2010 (Last updated, Version 7)
Data class Protein
Predictors HAMAP; MF_01279; [distribution of match scores in UniProtKB];[seed alignment for MF_01279]
Names X-Pro_dipeptid


Propagated annotation

Identifier, protein and gene names
Identifier PEPQ
Protein name
RecName: Full=Xaa-Pro dipeptidase;
Short=X-Pro dipeptidase;
EC=3.4.13.9;
AltName: Full=Imidodipeptidase;
AltName: Full=Proline dipeptidase;
Short=Prolidase;
Gene name pepQ
Comments
FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal position (By similarity).
CATALYTIC ACTIVITY: Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
COFACTOR: Binds 2 manganese ions per subunit (By similarity).
SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.
Cross-references
PROSITE PS00491; PROLINE_PEPTIDASE; 1;
Pfam PF00557; Peptidase_M24; 1;
Keywords
Dipeptidase, Hydrolase, Manganese, Metal-binding, Metalloprotease, Protease.
Gene Ontology
GO:0008235; Molecular function: metalloexopeptidase activity.
GO:0016805; Molecular function: dipeptidase activity.
Features
From: PEPQ_ECOLI (P21165)
Key     From     To       Description   Condition   FTGroup
METAL     246     246       Manganese 2 (By similarity)   D  
METAL     257     257       Manganese 1 (By similarity)   D  
METAL     257     257       Manganese 2 (By similarity)   D  
METAL     339     339       Manganese 1 (By similarity)   H  
METAL     384     384       Manganese 1 (By similarity)   E  
METAL     423     423       Manganese 1 (By similarity)   E  
METAL     423     423       Manganese 2 (By similarity)   E  


Additional information

Size range: 429-452 amino acids
Related UniRules: None
Template: P21165 (PEPQ_ECOLI); Q44238 (PEPQ_ALTSX); P77814 (PEPQ_PSEHA): [Recover all]
Scope: Bacteria; Gammaproteobacteria
Fusion: Nter: None; Cter: None
Duplicate: in IDILO
Plasmid encoded: 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).

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UniProtKB rule member sequences