HAMAP rule MF_01279
General rule information
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| Accession | MF_01279 |
| Dates | 15-AUG-2007 (Created)
26-MAY-2023 (Last updated, Version 16) |
| Name | X_Pro_dipeptid |
| Scope(s) |
Bacteria Gammaproteobacteria |
| Template(s) | P21165 (PEPQ_ECOLI); Q44238 (PEPQ_ALTSX); P77814 (PEPQ_PSEHA); [ Recover all ] |
| Triggered by |
HAMAP; MF_01279 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=pepQ; |
Comments
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| FUNCTION | Splits dipeptides with a prolyl residue in the C-terminal position. |
| CATALYTIC ACTIVITY | Reaction=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline; Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9; |
| COFACTOR | Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 manganese ions per subunit.; |
| SIMILARITY | Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily. |
Keywords
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Gene Ontology
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| GO:0008235; Molecular function:metalloexopeptidase activity |
| GO:0016805; Molecular function:dipeptidase activity |
Cross-references
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Features
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| 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
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| Size range | 429-452 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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). |