Annotations: 1TXN

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1txna_	Alpha and beta proteins (a+b)	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
B	d1txnb_	Alpha and beta proteins (a+b)	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01218	e1txnA1	A: a+b three layers	X: Coproporphyrinogen III oxidase (From Topology)	H: Coproporphyrinogen III oxidase (From Topology)	T: Coproporphyrinogen III oxidase	F: PF01218	ECOD (1.6)
B	PF01218	e1txnB1	A: a+b three layers	X: Coproporphyrinogen III oxidase (From Topology)	H: Coproporphyrinogen III oxidase (From Topology)	T: Coproporphyrinogen III oxidase	F: PF01218	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1500.10	Alpha Beta	3-Layer(aba) Sandwich	oxygen-dependent coproporphyrinogen oxidase	Coproporphyrinogen III oxidase, aerobic	CATH (4.3.0)
B	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 organonitrogen compound metabolic process tetrapyrrole metabolic process heme biosynthetic process organonitrogen compound biosynthetic process pigment biosynthetic process organic cyclic compound metabolic process organic substance metabolic process tetrapyrrole biosynthetic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process organonitrogen compound metabolic process tetrapyrrole metabolic process heme biosynthetic process organonitrogen compound biosynthetic process pigment biosynthetic process organic cyclic compound metabolic process organic substance metabolic process tetrapyrrole biosynthetic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process metabolic process porphyrin-containing compound metabolic process protoporphyrinogen IX metabolic process protoporphyrinogen IX biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

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 R01GM133198.