2QT8

Coproporphyrinogen III oxidase from Leishmania major

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	d2qt8b2	Alpha and beta proteins (a+b)	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	automated matches	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
B	d2qt8b3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
A	d2qt8a2	Alpha and beta proteins (a+b)	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	automated matches	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
A	d2qt8a3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Coproporphyrinogen III oxidase	8036379	3001418	SCOP2B (2022-06-29)
A	SCOP2 Family	Coproporphyrinogen III oxidase	8024000	4001379	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Coproporphyrinogen III oxidase	8036379	3001418	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	Coprogen_oxidas	e2qt8B1	A: a+b three layers	X: Coproporphyrinogen III oxidase (From Topology)	H: Coproporphyrinogen III oxidase (From Topology)	T: Coproporphyrinogen III oxidase	F: Coprogen_oxidas	ECOD (1.6)
A	Coprogen_oxidas	e2qt8A1	A: a+b three layers	X: Coproporphyrinogen III oxidase (From Topology)	H: Coproporphyrinogen III oxidase (From Topology)	T: Coproporphyrinogen III oxidase	F: Coprogen_oxidas	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.1500.10	Alpha Beta	3-Layer(aba) Sandwich	oxygen-dependent coproporphyrinogen oxidase	Coproporphyrinogen III oxidase, aerobic	CATH (4.3.0)
A	3.40.1500.10	Alpha Beta	3-Layer(aba) Sandwich	oxygen-dependent coproporphyrinogen oxidase	Coproporphyrinogen III oxidase, aerobic	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01218	Coproporphyrinogen III oxidase (Coprogen_oxidas)	Coproporphyrinogen III oxidase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Coproporphyrinogen III oxidase	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity coproporphyrinogen oxidase activity oxidoreductase activity, acting on the CH-CH group of donors catalytic activity oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor	pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process protoporphyrinogen IX metabolic process pigment biosynthetic process protoporphyrinogen IX biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036406	Oxygen-dependent coproporphyrinogen III oxidase superfamily	Homologous Superfamily
A, B	IPR001260	Coproporphyrinogen III oxidase, aerobic	Family
A, B	IPR018375	Coproporphyrinogen III oxidase, 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.