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ProRule PRU10073


General rule information [?]

PURL https://purl.expasy.org/prosite/rule/PRU10073
Accession PRU10073
Dates 16-OCT-2006 (Created)
19-NOV-2022 (Last updated, Version 13)
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 (DPEP1_BOVIN);

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.



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UniProtKB rule member sequences [?]