Summary: Coproporphyrinogen III oxidase

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Wikipedia: Coproporphyrinogen III oxidase
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Coproporphyrinogen III oxidase Edit Wikipedia article

Coproporphyrinogen oxidase

PDB rendering based on 2aex.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
2AEX

Identifiers

Symbols

CPOX; CPO; CPX; HCP

External IDs

OMIM: 612732 MGI: 104841 HomoloGene: 76 ChEMBL: 1681618 GeneCards: CPOX Gene

EC number

1.3.3.3

Gene Ontology
Molecular function	• coproporphyrinogen oxidase activity • protein homodimerization activity
Cellular component	• cytoplasm • mitochondrion • mitochondrial inner membrane • mitochondrial intermembrane space
Biological process	• porphyrin-containing compound metabolic process • protoporphyrinogen IX biosynthetic process • heme biosynthetic process • response to iron ion • response to lead ion • response to insecticide • small molecule metabolic process • response to arsenic-containing substance • response to methylmercury
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
98.24 – 98.31 Mb

Chr 16:
58.67 – 58.68 Mb

PubMed search

[1]

[2]

Coprogen_oxidas

coproporphyrinogen iii oxidase from leishmania major

Identifiers

Symbol

Coprogen_oxidas

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Coproporphyrinogen-III oxidase, mitochondrial is an enzyme that in humans is encoded by the CPOX gene.^[1]^[2]^[3] A genetic defect in the enzyme results in a reduced production of heme in animals. The medical condition associated with this enzyme defect is called hereditary coproporphyria.^[4] ^[5]

It is an enzyme involved in the sixth step of porphyrin metabolism it catalyses the oxidative decarboxylation of coproporphyrinogen III to proto-porphyrinogen IX in the haem and chlorophyll biosynthetic pathways.^[2]^[6] The protein is a homodimer containing two internally bound iron atoms per molecule of native protein.^[7] 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.

[edit] References

^ Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y (Jun 1995). "A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria". Hum Mol Genet 4 (2): 275–8. doi:10.1093/hmg/4.2.275. PMID 7757079.
^ ^a ^b Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S (Nov 1993). "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation". J Biol Chem 268 (28): 21359–63. PMID 8407975.
^ "Entrez Gene: CPOX coproporphyrinogen oxidase".
^ "Hereditary coproporphyria". Genetic and Rare Diseases Information Center. National Institutes of Health. Retrieved 8 August 2011.
^ "CPOX". Genetics Home Reference. Retrieved 8 August 2011.
^ Madsen O, Sandal L, Sandal NN, Marcker KA (October 1993). "A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules". Plant Mol. Biol. 23 (1): 35–43. doi:10.1007/BF00021417. PMID 8219054.
^ Camadro JM, Chambon H, Jolles J, Labbe P (May 1986). "Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae". Eur. J. Biochem. 156 (3): 579–87. doi:10.1111/j.1432-1033.1986.tb09617.x. PMID 3516695.

[edit] Further reading

Fujita H, Kondo M, Taketani S et al. (1995). "Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria". Hum. Mol. Genet. 3 (10): 1807–10. doi:10.1093/hmg/3.10.1807. PMID 7849704.
Cacheux V, Martasek P, Fougerousse F et al. (1994). "Localization of the human coproporphyrinogen oxidase gene to chromosome band 3q12". Hum. Genet. 94 (5): 557–9. doi:10.1007/BF00211026. PMID 7959694.
Delfau-Larue MH, Martasek P, Grandchamp B (1995). "Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping". Hum. Mol. Genet. 3 (8): 1325–30. doi:10.1093/hmg/3.8.1325. PMID 7987309.
Martasek P, Nordmann Y, Grandchamp B (1994). "Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms". Hum. Mol. Genet. 3 (3): 477–80. doi:10.1093/hmg/3.3.477. PMID 8012360.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Martasek P, Camadro JM, Delfau-Larue MH et al. (1994). "Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3024–8. doi:10.1073/pnas.91.8.3024. PMC 43507. PMID 8159699.
Taketani S, Kohno H, Furukawa T et al. (1994). "Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase". Biochim. Biophys. Acta 1183 (3): 547–9. doi:10.1016/0005-2728(94)90083-3. PMID 8286403.
Lamoril J, Deybach JC, Puy H et al. (1997). "Three novel mutations in the coproporphyrinogen oxidase gene". Hum. Mutat. 9 (1): 78–80. doi:10.1002/(SICI)1098-1004(1997)9:1<78::AID-HUMU17>3.0.CO;2-M. PMID 8990017.
Daimon M, Gojyou E, Sugawara M et al. (1997). "A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria". Hum. Genet. 99 (2): 199–201. doi:10.1007/s004390050338. PMID 9048920.
Schreiber WE, Zhang X, Senz J, Jamani A (1997). "Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene". Hum. Mutat. 10 (3): 196–200. doi:10.1002/(SICI)1098-1004(1997)10:3<196::AID-HUMU3>3.0.CO;2-H. PMID 9298818.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Lamoril J, Puy H, Gouya L et al. (1998). "Neonatal hemolytic anemia due to inherited harderoporphyria: clinical characteristics and molecular basis". Blood 91 (4): 1453–7. PMID 9454777.
Susa S, Daimon M, Kondo H et al. (1999). "Identification of a novel mutation of the CPO gene in a Japanese hereditary coproporphyria family". Am. J. Med. Genet. 80 (3): 204–6. doi:10.1002/(SICI)1096-8628(19981116)80:3<204::AID-AJMG4>3.0.CO;2-G. PMID 9843038.
Rosipal R, Lamoril J, Puy H et al. (1999). "Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update". Hum. Mutat. 13 (1): 44–53. doi:10.1002/(SICI)1098-1004(1999)13:1<44::AID-HUMU5>3.0.CO;2-Q. PMID 9888388.
Taketani S, Furukawa T, Furuyama K (2001). "Expression of coproporphyrinogen oxidase and synthesis of hemoglobin in human erythroleukemia K562 cells". Eur. J. Biochem. 268 (6): 1705–11. doi:10.1046/j.1432-1327.2001.02045.x. PMID 11248690.
Lamoril J, Puy H, Whatley SD et al. (2001). "Characterization of Mutations in the CPO Gene in British Patients Demonstrates Absence of Genotype-Phenotype Correlation and Identifies Relationship between Hereditary Coproporphyria and Harderoporphyria". Am. J. Hum. Genet. 68 (5): 1130–8. doi:10.1086/320118. PMC 1226094. PMID 11309681.
Elkon H, Don J, Melamed E et al. (2003). "Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase". J. Mol. Neurosci. 18 (3): 229–38. doi:10.1385/JMN:18:3:229. PMID 12059041.
Wiman A, Floderus Y, Harper P (2002). "Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria". J. Hum. Genet. 47 (8): 407–12. doi:10.1007/s100380200059. PMID 12181641.

PDB gallery

2aex: The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary Coproporphyria

Heme synthesis—note that some reactions occur in the cytoplasm and some in the mitochondrion (yellow)

[edit] External links

Coproporphyrinogen III Oxidases at the US National Library of Medicine Medical Subject Headings (MeSH)

This oxidoreductase article is a stub. You can help Wikipedia by expanding it.

Oxidoreductases: CH-CH oxidoreductases (EC 1.3)

1.3.1: NAD/NADP acceptor

1.3.3: Oxygen acceptor

Dihydroorotate dehydrogenase
Coproporphyrinogen III oxidase
Protoporphyrinogen oxidase

1.3.5: Quinone

Succinate dehydrogenase
- SDHA
- SDHB
- SDHC
- SDHD

1.3.99: Other acceptors

B
enzm
1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
2.7.10
2.7.11-12
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
- 5
- 6
- 7
- 22
- 23
- 24
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

Metabolism: amino acid metabolism · porphyrin/heme enzymes

Porphyrin biosynthesis

early mitochondrial: Aminolevulinic acid synthase (ALAS1, ALAS2) · Porphobilinogen synthase

cytosolic: Porphobilinogen deaminase · Uroporphyrinogen III synthase · Uroporphyrinogen III decarboxylase · Coproporphyrinogen III oxidase

late mitochondrial: Protoporphyrinogen oxidase · Ferrochelatase

Heme degradation
to bile

spleen: Heme oxygenase · Biliverdin reductase

liver: glucuronosyltransferase (UGT1A1)

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

M: MYL

cell/phys (coag, heme, immu, gran), csfs

rbmg/mogr/tumr/hist, sysi/epon, btst

drug (B1/2/3+5+6), btst, trns

This article incorporates text from the public domain Pfam and InterPro IPR001260

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Coproporphyrinogen III oxidase Provide feedback

No Pfam abstract.

External database links

PANDIT:	PF01218
PROSITE:	PDOC00783
Pseudofam:	PF01218
SYSTERS:	Coprogen_oxidas

This tab holds annotation information from the InterPro database.

InterPro entry IPR001260

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 [PUBMED:8407975, PUBMED:8219054]. The protein is a homodimer containing two internally bound iron atoms per molecule of native protein [PUBMED:3516695]. 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.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Molecular function	coproporphyrinogen oxidase activity (GO:0004109)
Biological process	oxidation-reduction process (GO:0055114)
Biological process	porphyrin-containing compound biosynthetic process (GO:0006779)

Domain organisation

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	Seed (93)	Full (2155)	Representative proteomes				NCBI (1719)	Meta (2513)
	Seed (93)	Full (2155)	RP15 (214)	RP35 (409)	RP55 (570)	RP75 (700)	NCBI (1719)	Meta (2513)
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Key: available, not generated, — not available.

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	Seed (93)	Full (2155)	Representative proteomes				NCBI (1719)	Meta (2513)
	Seed (93)	Full (2155)	RP15 (214)	RP35 (409)	RP55 (570)	RP75 (700)	NCBI (1719)	Meta (2513)
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	Seed (93)	Full (2155)	RP15 (214)	RP35 (409)	RP55 (570)	RP75 (700)	NCBI (1719)	Meta (2513)
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Curation

Seed source:

Prosite

Previous IDs:

none

Type:

Family

Author:

Finn RD, Bateman A

Number in seed:

93

Number in full:

2155

Average length of the domain:

276.40 aa

Average identity of full alignment:

51 %

Average coverage of the sequence by the domain:

93.10 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	20.0	20.0
Trusted cut-off	22.6	22.5
Noise cut-off	18.9	18.4

Model length:

296

Family (HMM) version:

13

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Coprogen_oxidas

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Coprogen_oxidas domain has been found. There are 24 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: Coprogen_oxidas (PF01218)

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Summary: Coproporphyrinogen III oxidase

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Coproporphyrinogen III oxidase Edit Wikipedia article

[edit] References

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[edit] External links

Coproporphyrinogen III oxidase Provide feedback

External database links

InterPro entry IPR001260

Gene Ontology

Domain organisation

Alignments

Alignment types

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Curation and family details

Curation

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Sub-species

Too many species/sequences

Tree controls

Annotation

Download tree

Selected sequences

Species trees

Interactive tree

Interactions

Structures