3UCA

Crystal structure of isoprenoid synthase (target EFI-501974) from clostridium perfringens

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d3ucab_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	automated matches	automated matches	(Clostridium perfringens ) [TaxId: 1502 ],	SCOPe (2.08)
A	d3ucaa_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	automated matches	automated matches	(Clostridium perfringens ) [TaxId: 1502 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Terpenoid synthases	8058983	3001615	SCOP2B (2022-06-29)
A	SCOP2 Family	Isoprenyl diphosphate synthases	8058982	4001453	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Terpenoid synthases	8058983	3001615	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)
B	polyprenyl_synt	e3ucaB1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: polyprenyl_synt	ECOD (1.6)
A	polyprenyl_synt	e3ucaA1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: polyprenyl_synt	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.600.10	Mainly Alpha	Orthogonal Bundle	Farnesyl Diphosphate Synthase	Farnesyl Diphosphate Synthase	CATH (4.3.0)
A	1.10.600.10	Mainly Alpha	Orthogonal Bundle	Farnesyl Diphosphate Synthase	Farnesyl Diphosphate Synthase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00348	Polyprenyl synthetase (polyprenyl_synt)	Polyprenyl synthetase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Geranyltranstransferase	prenyltransferase activity geranyltranstransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process terpenoid biosynthetic process phospholipid biosynthetic process farnesyl diphosphate metabolic process phospholipid metabolic process biosynthetic process farnesyl diphosphate biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process terpenoid biosynthetic process phospholipid biosynthetic process farnesyl diphosphate metabolic process phospholipid metabolic process biosynthetic process farnesyl diphosphate biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process terpenoid metabolic process lipid metabolic process isoprenoid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000092	Polyprenyl synthetase	Family
A, B	IPR053378	Prenyl diphosphate synthase	Family
A, B	IPR008949	Isoprenoid synthase domain superfamily	Homologous Superfamily
A, B	IPR033749	Polyprenyl synthetase, conserved site	Conserved Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.