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24  structures 1940  species 1  interaction 2155  sequences 8  architectures

Family: Coprogen_oxidas (PF01218)

Summary: Coproporphyrinogen III oxidase

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This is the Wikipedia entry entitled "Coproporphyrinogen III oxidase". More...

Coproporphyrinogen III oxidase Edit Wikipedia article

Coproporphyrinogen oxidase

PDB rendering based on 2aex.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CPOX; CPO; CPX; HCP
External IDs OMIM612732 MGI104841 HomoloGene76 ChEMBL: 1681618 GeneCards: CPOX Gene
EC number 1.3.3.3
RNA expression pattern
PBB GE CPOX 204172 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1371 12892
Ensembl ENSG00000080819 ENSMUSG00000022742
UniProt P36551 P36552
RefSeq (mRNA) NM_000097 NM_007757
RefSeq (protein) NP_000088 NP_031783
Location (UCSC) Chr 3:
98.24 – 98.31 Mb
Chr 16:
58.67 – 58.68 Mb
PubMed search [1] [2]
Coprogen_oxidas
PDB 1vju EBI.jpg
coproporphyrinogen iii oxidase from leishmania major
Identifiers
Symbol Coprogen_oxidas
Pfam PF01218
InterPro IPR001260
PROSITE PDOC00783

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.

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ "Entrez Gene: CPOX coproporphyrinogen oxidase". 
  4. ^ "Hereditary coproporphyria". Genetic and Rare Diseases Information Center. National Institutes of Health. Retrieved 8 August 2011. 
  5. ^ "CPOX". Genetics Home Reference. Retrieved 8 August 2011. 
  6. ^ 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. 
  7. ^ 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. 

Further reading[edit]


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

External links[edit]


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

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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Coproporphyrinogen III oxidase Provide feedback

No Pfam abstract.

External database links

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

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Domain organisation

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Alignments

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  Seed
(93)
Full
(2155)
Representative proteomes NCBI
(1719)
Meta
(2513)
RP15
(214)
RP35
(409)
RP55
(570)
RP75
(700)
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  Seed
(93)
Full
(2155)
Representative proteomes NCBI
(1719)
Meta
(2513)
RP15
(214)
RP35
(409)
RP55
(570)
RP75
(700)
Alignment:
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  Seed
(93)
Full
(2155)
Representative proteomes NCBI
(1719)
Meta
(2513)
RP15
(214)
RP35
(409)
RP55
(570)
RP75
(700)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

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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 View help on HMM parameters

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
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

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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