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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU10073


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU10073
General rule information [?]

Accession PRU10073
Dates 16-OCT-2006 (Created)
19-NOV-2022 (Last updated, Version 14)
Data class Domain;
Predictors PROSITE; PS00869; RENAL_DIPEPTIDASE_1
PROSITE; PS51365; RENAL_DIPEPTIDASE_2
Name Renal dipeptidase family
Function Renal dipeptidase (rDP) (EC 3.4.13.19) and related enzymes are zinc-dependent metalloenzymes which hydrolyze a wide range of dipeptides.
Scope(s) Eukaryota
Bacteria
Archaea
Example(s) Q3SZM7;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1> or <FTGroup:2> or not <AnyFeature:PS51365>
Protein name + AltName: Full=dipeptidase;
                 EC=3.4.13.19;

Comments [?]

CATALYTIC ACTIVITY Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19;
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
case <Feature:PS51365:365=C> and <FTGroup:3> and <FTGroup:4>
SUBUNITHomodimer; disulfide-linked.
end case
SIMILARITYBelongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.

Keywords [?]

Dipeptidase
Hydrolase
Metal-binding
Metalloprotease
Protease
Zinc
end case
case <FTTag:disulf>
Disulfide bond
end case

Gene Ontology [?]

case <FTGroup:1> or <FTGroup:2>
GO:0016805; Molecular function:dipeptidase activity
GO:0016787; Molecular function:hydrolase activity
GO:0046872; Molecular function:metal ion binding
GO:0008237; Molecular function:metallopeptidase activity
GO:0008233; Molecular function:peptidase activity
GO:0008270; Molecular function:zinc ion binding

Features [?]

From: PS51365
Key From To Description Tag Condition FTGroup
BINDING 20 20 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#1"
/ligand_note="catalytic"		 H 1
BINDING 22 22 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#1"
/ligand_note="catalytic"		 D 1
BINDING 125 125 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#1"
/ligand_note="catalytic"		 E 1
BINDING 125 125 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="catalytic"		 E 2
BINDING 198 198 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="catalytic"		 Y 2
BINDING 219 219 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="catalytic"		 H 2
BINDING 152 152 /ligand="substrate" H
BINDING 230 230 /ligand="substrate" R
BINDING 290 290 /ligand="substrate" D
DISULFID 71 154 disulf C-x*-C 3
DISULFID 226 258 disulf C-x*-C 4
DISULFID 365 365 /note="Interchain" disulf C-x*-C
From: PS00869
Key From To Description Tag Condition FTGroup
case not <AnyFeature:PS51365>
BINDING 2 2 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#1"
/ligand_note="catalytic"
end case

Additional information [?]

Size range 260-380 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

UniProtKB rule member sequences [?]