AC   PRU00678;
DC   Domain;
TR   PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1; level=0
XX
Names: Prokaryotic zinc-dependent phospholipase C domain
Function: Phospholipase C (EC 3.1.4.3) has a ~245 amino-acids domain
 with the active site (PLC) in a cleft which is also occupied by 3 zinc
 ions. There are nine conserved residues known to be involved in binding the
 zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp.
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3>
DE   + AltName: Full=phospholipase C;
DE            EC=3.1.4.3;
DE            Short=PLC;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 3 Zn(2+) ions per subunit.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
end case
CC   -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC       family.
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3>
DR   PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1; trigger=no
end case
XX
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3>
GO   GO:0016787; F:hydrolase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0008270; F:zinc ion binding
XX
KW   Hydrolase
KW   Metal-binding
KW   Zinc
end case
XX
FT   From: PS51346
FT   DOMAIN          3..to
FT                   /note="Zn-dependent PLC #"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT   Group: 1; Condition: W
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT   Group: 1; Condition: H
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#3"
FT   Group: 3; Condition: D
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#3"
FT   Group: 3; Condition: H
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#3"
FT   Group: 3; Condition: H
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT   Group: 1; Condition: D
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#3"
FT   Group: 3; Condition: D
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT   Group: 2; Condition: H
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT   Group: 2; Condition: H
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT   Group: 2; Condition: E
XX
Chop: Nter=3; Cter=0;
Size: 230-260;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q46150;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.10 2022/11/19
//