4S23 | pdb_00004s23

Structure of the GcpE-HMBPP complex from Thermus thermophilius

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GcpE N-terminal domain-like	8053955	3002254	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Nitrite and sulphite reductase 4Fe-4S domain-like	8053960	3000646	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nitrite and sulphite reductase 4Fe-4S domain-like	8053960	3000646	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GcpE N-terminal domain-like	8053955	3002254	SCOP2B (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	GcpE_C	e4s23A2	A: a+b three layers	X: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	H: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	T: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4	F: GcpE_C	ECOD (1.6)
A	GcpE_N	e4s23A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: GcpE_N	ECOD (1.6)
B	GcpE_C	e4s23B2	A: a+b three layers	X: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	H: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	T: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4	F: GcpE_C	ECOD (1.6)
B	GcpE_N	e4s23B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: GcpE_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
A	3.30.413.10	Alpha Beta	2-Layer Sandwich	Sulfite Reductase Hemoprotein	domain 1	CATH (4.3.0)
B	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
B	3.30.413.10	Alpha Beta	2-Layer Sandwich	Sulfite Reductase Hemoprotein	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04551	GcpE TIM-barrel domain (GcpE)	GcpE TIM-barrel domain	In a variety of organisms, including plants and several eubacteria, isoprenoids are synthesised by the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the termi ...	In a variety of organisms, including plants and several eubacteria, isoprenoids are synthesised by the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the terminal biosynthetic steps of the MEP pathway have not been fully elucidated. GcpE gene of Escherichia coli is involved in this pathway [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase	oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor oxidoreductase activity oxidoreductase activity, acting on CH or CH2 groups 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) catalytic activity iron-sulfur cluster binding binding 4 iron, 4 sulfur cluster binding metal cluster binding small molecule binding 4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin) cation binding transition metal ion binding iron ion binding oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor oxidoreductase activity oxidoreductase activity, acting on CH or CH2 groups 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) catalytic activity iron-sulfur cluster binding binding 4 iron, 4 sulfur cluster binding metal cluster binding small molecule binding 4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin) cation binding transition metal ion binding iron ion binding ion binding metal ion binding	isoprenoid biosynthetic process isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway isopentenyl diphosphate biosynthetic process lipid biosynthetic process carbohydrate derivative metabolic process primary metabolic process glyceraldehyde-3-phosphate metabolic process phospholipid biosynthetic process aldehyde metabolic process phospholipid metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process isoprenoid biosynthetic process isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway isopentenyl diphosphate biosynthetic process lipid biosynthetic process carbohydrate derivative metabolic process primary metabolic process glyceraldehyde-3-phosphate metabolic process phospholipid biosynthetic process aldehyde metabolic process phospholipid metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process lipid metabolic process isoprenoid metabolic process isopentenyl diphosphate metabolic process terpenoid biosynthetic process terpenoid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR016425	4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase, bacterial	Family
A, B	IPR011005	Dihydropteroate synthase-like superfamily	Homologous Superfamily
A, B	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily	Homologous Superfamily
A, B	IPR004588	4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase, bacterial-type	Family

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.