AC   PRU10073;
DC   Domain;
TR   PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1; level=0
TR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1; level=0
XX
Names: Renal dipeptidase family
 microsomal dipeptidase
 membrane dipeptidase
Function: Renal  dipeptidase (rDP) (EC 3.4.13.19) and related enzymes are
 zinc-dependent metalloenzymes which hydrolyze a wide range of dipeptides.
XX
case <FTGroup:1> or <FTGroup:2> or not <AnyFeature:PS51365>
DE   + AltName: Full=dipeptidase;
DE            EC=3.4.13.19;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
case <Feature:PS51365:365=C> and <FTGroup:3> and <FTGroup:4>
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
end case
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Peptidase M19 family.
XX
case <FTGroup:1> or <FTGroup:2>
GO   GO:0016805; F:dipeptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0008237; F:metallopeptidase activity
GO   GO:0008233; F:peptidase activity
GO   GO:0008270; F:zinc ion binding
XX
KW   Dipeptidase
KW   Hydrolase
KW   Metal-binding
KW   Metalloprotease
KW   Protease
KW   Zinc
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51365
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: D
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Group: 2; Condition: E
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Group: 2; Condition: Y
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Group: 2; Condition: H
FT   BINDING         152
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         230
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         290
FT                   /ligand="substrate"
FT   Condition: D
FT   DISULFID        71..154
FT   Tag: disulf; Group: 3; Condition: C-x*-C
FT   DISULFID        226..258
FT   Tag: disulf; Group: 4; Condition: C-x*-C
FT   DISULFID        365
FT                   /note="Interchain"
FT   Tag: disulf; Condition: C-x*-C
FT   From: PS00869
case not <AnyFeature:PS51365>
FT   BINDING         2
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
end case
XX
Chop: Nter=0; Cter=1;
Size: 260-380;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q3SZM7;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.13 2022/11/19
//