7Q4G

Structure of coproheme decarboxylase from Corynebacterium dipththeriae Y135A mutant in complex with coproheme

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Chlor_dismutase_C	e7q4gA2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_C	ECOD (1.6)
A	Chlor_dismutase_N	e7q4gA1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_N	ECOD (1.6)
B	Chlor_dismutase_C	e7q4gB2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_C	ECOD (1.6)
B	Chlor_dismutase_N	e7q4gB1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_N	ECOD (1.6)
D	Chlor_dismutase_C	e7q4gD2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_C	ECOD (1.6)
D	Chlor_dismutase_N	e7q4gD1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_N	ECOD (1.6)
E	Chlor_dismutase_C	e7q4gE2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_C	ECOD (1.6)
E	Chlor_dismutase_N	e7q4gE1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_N	ECOD (1.6)
C	Chlor_dismutase_C	e7q4gC2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_C	ECOD (1.6)
C	Chlor_dismutase_N	e7q4gC1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Chlor_dismutase_N	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E	PF06778	Chlorite dismutase (Chlor_dismutase)	Chlorite dismutase	This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyses the disproportionation of chlorite into chloride and oxygen [1]. Note that many family members are hypothetical proteins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	Coproheme decarboxylase from Corynebacterium diphtheriae Y135A mutant in complex with coproheme	oxidoreductase 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 binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	heme B biosynthetic process heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process heme B metabolic process tetrapyrrole biosynthetic process biosynthetic process metabolic process porphyrin-containing compound metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR010644	Heme-dependent peroxidase ChdC/CLD	Family
A, B, C, D, E	IPR011008	Dimeric alpha-beta barrel	Homologous Superfamily

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.