Summary: Di-haem cytochrome c peroxidase
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Di-haem cytochrome c peroxidase Edit Wikipedia article
Di-haem cytochrome c peroxidase | |||||||||
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![]() crystal structure of the di-haem cytochrome c peroxidase from pseudomonas aeruginosa
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Identifiers | |||||||||
Symbol | CCP_MauG | ||||||||
Pfam | PF03150 | ||||||||
Pfam clan | CL0318 | ||||||||
InterPro | IPR004852 | ||||||||
SCOP | 1eb7 | ||||||||
SUPERFAMILY | 1eb7 | ||||||||
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In molecular biology, the di-haem cytochrome c peroxidase family is a group of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidizable substrate. However, since they possess two, instead of one, haem prosthetic groups, this family of bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site).[1] The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognised.[2]
References
- ^ Fulop V, Ridout CJ, Greenwood C, Hajdu J (November 1995). "Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa". Structure. 3 (11): 1225–33. PMID 8591033. doi:10.1016/s0969-2126(01)00258-1.
- ^ Gak ER, Tsygankov YD, Chistoserdov AY (June 1997). "Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum ' KT and analysis of mau mutants". Microbiology. 143 (6): 1827–35. PMID 9202457. doi:10.1099/00221287-143-6-1827.
This article incorporates text from the public domain Pfam and InterPro IPR004852
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This is a family of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidisable substrate. However, since they possess two, instead of one, haem prosthetic groups, bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site) [1]. The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognised [2].
Literature references
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Fulop V, Ridout CJ, Greenwood C, Hajdu J; , Structure 1995;3:1225-1233.: Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. PUBMED:8591033 EPMC:8591033
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Gak ER, Tsygankov YD, Chistoserdov AY; , Microbiology 1997;143:1827-1835.: Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum' KT and analysis of mau mutants. PUBMED:9202457 EPMC:9202457
Internal database links
SCOOP: | Cytochrom_C |
Similarity to PfamA using HHSearch: | DHOR |
External database links
SCOP: | 1eb7 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004852
This is a group of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidizable substrate. However, since they possess two, instead of one, haem prosthetic groups, bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site) [PUBMED:8591033]. The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognised [PUBMED:9202457].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | oxidoreductase activity (GO:0016491) |
Biological process | oxidation-reduction process (GO:0055114) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Cytochrome-c (CL0318), which has the following description:
This family includes proteins where a covalently-bound haem completes the core. The core is three helices in an open folded leaf formation. The members are monodomain cytochromes.
The clan contains the following 13 members:
CCP_MauG Cytochrom_C Cytochrom_C1 Cytochrom_C550 Cytochrome-c551 Cytochrome_CBB3 Dehyd-heme_bind DHC DHOR DUF1924 FixO Haem_bd PSCyt1Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (491) |
Full (4407) |
Representative proteomes | UniProt (20946) |
NCBI (33011) |
Meta (644) |
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RP15 (596) |
RP35 (1980) |
RP55 (4486) |
RP75 (7991) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (491) |
Full (4407) |
Representative proteomes | UniProt (20946) |
NCBI (33011) |
Meta (644) |
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RP15 (596) |
RP35 (1980) |
RP55 (4486) |
RP75 (7991) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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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.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_3135 (release 6.5) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Mifsud W |
Number in seed: | 491 |
Number in full: | 4407 |
Average length of the domain: | 165.10 aa |
Average identity of full alignment: | 31 % |
Average coverage of the sequence by the domain: | 40.16 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 150 | ||||||||||||
Family (HMM) version: | 15 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
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 CCP_MauG domain has been found. There are 88 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 sequence.
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