Annotations: 1AH7

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ah7a_	All alpha proteins	Phospholipase C/P1 nuclease	Phospholipase C/P1 nuclease	Phospholipase C	Bacterial phosholipase C	(Bacillus cereus ) [TaxId: 1396 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Phospholipase C	8026382	4001408	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phospholipase C/P1 nuclease	8038761	3001513	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00882	e1ah7A1	A: alpha bundles	X: Phospholipase C/P1 nuclease (From Topology)	H: Phospholipase C/P1 nuclease (From Topology)	T: Phospholipase C/P1 nuclease	F: PF00882	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.575.10	Mainly Alpha	Orthogonal Bundle	P1 Nuclease	P1 Nuclease	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00882	Zinc dependent phospholipase C (Zn_dep_PLPC)	Zinc dependent phospholipase C	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PHOSPHOLIPASE C	phosphoric ester hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphatidylcholine phospholipase C activity phospholipase C activity hydrolase activity catalytic activity phospholipase activity lipase activity cation binding transition metal ion binding zinc ion binding ion binding binding phosphoric ester hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphatidylcholine phospholipase C activity phospholipase C activity hydrolase activity catalytic activity phospholipase activity lipase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	biological process involved in interspecies interaction between organisms cellular process disruption of cell in another organism disruption of anatomical structure in another organism killing of cells of another organism cell killing	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR008947	Phospholipase C/P1 nuclease domain superfamily	Homologous Superfamily
A	IPR029002	Phospholipase C/D	Domain
A	IPR001531	Zinc-dependent phospholipase C	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	phospholipase C M-CSA #27	Phospholipase C (PLC) from Bacillus cereus is a monomeric protein with a degree of similarly to mammalian PLCs and can mimic the action of mammalian PLCs for example by stimulating prostaglandin synthesis. The active site contains three Zn(II) ions which activate the cleavage of membrane phospholipids, liberating the polar head group and diacylglycerol. Although phosphatidylcholine is the preferred substrate, phosphatidylserine and phosphatidylethanolamine are also accepted.	Defined by 8 residues: HIS:A-14ASP:A-55HIS:A-69HIS:A-118ASP:A-122HIS:A-128HIS:A-142GLU:A-146 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.4.3 (PDB Primary Data) Search M-CSA Motif + EC 3.1.4.3

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