EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR018375 Coproporphyrinogen III oxidase, conserved site

Protein matches Help

UniProtKB

Matches:

727 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR018375 Coproporphyrinogen-3_ox_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01021	COPROGEN_OXIDASE	727
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001260 Coproporphyrinogen III oxidase

GO Term annotation Help

Process

GO:0006779 porphyrin biosynthetic process
GO:0055114 oxidation reduction

Function

GO:0004109 coproporphyrinogen oxidase activity

InterPro annotation

Entry Details in BioMart

Abstract

Coprogen oxidase (i.e. coproporphyrin III oxidase or coproporphyrinogenase) catalyses the oxidative decarboxylation of coproporphyrinogen III to proto-porhyrinogen IX in the haem and chlorophyll biosynthetic pathways [1, 2]. The protein is a homodimer containing two internally bound iron atoms per molecule of native protein [3]. The enzyme is active in the presence of molecular oxygen that acts as an electron acceptor). The enzyme is widely distributed having been found in a variety of eukaryotic and prokaryotic sources.

Structural links Help

PDB - click here

SCOP: d.248.1.1

CATH: 3.40.1500.10

Database links Help

Enzyme: EC:1.3.3.3

CluSTr: ALLvsALL:2852:40.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018375

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P11353 Coproporphyrinogen-III oxidase

P36551 Coproporphyrinogen-III oxidase, mitochondrial

P36552 Coproporphyrinogen-III oxidase, mitochondrial

Q9LR75 Coproporphyrinogen-III oxidase, chloroplastic

Q9V3D2 Coproporphyrinogen-III oxidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001260	Coproporphyrinogen III oxidase
IPR018375	Coproporphyrinogen III oxidase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S. Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation. J. Biol. Chem. 268 21359-63 1993 [PubMed: 8407975] http://intl.jbc.org/cgi/reprint/268/28/21359.pdf
2.	Madsen O, Sandal L, Sandal NN, Marcker KA. A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules. Plant Mol. Biol. 23 35-43 1993 [PubMed: 8219054] http://dx.doi.org/10.1007/BF00021417
3.	Camadro JM, Chambon H, Jolles J, Labbe P. Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 156 579-87 1986 [PubMed: 3516695] http://dx.doi.org/10.1111/j.1432-1033.1986.tb09617.x

Additional Reading Open in usermanual
	Xu K, Elliott T. Cloning, DNA sequence, and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase. J. Bacteriol. 176 1994 3196-203 [PubMed: 8195073] http://jb.asm.org/cgi/content/abstract/176/11/3196
	Xu K, Elliott T. An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. J. Bacteriol. 175 1993 4990-9 [PubMed: 8349542] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8349542
	Phillips JD, Whitby FG, Warby CA, Labbe P, Yang C, Pflugrath JW, Ferrara JD, Robinson H, Kushner JP, Hill CP. Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae. J. Biol. Chem. 279 2004 38960-8 [PubMed: 15194705] http://dx.doi.org/10.1074/jbc.M406050200

InterPro 23.1