Summary: Cytochrome C oxidase subunit II, periplasmic domain
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Cytochrome c oxidase subunit II Edit Wikipedia article
| Cytochrome c oxidase subunit II, transmembrane domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Bacterial cytochrome c oxidase complex. Subunit II indicated by blue. | |||||||||
| Identifiers | |||||||||
| Symbol | COX2_TM | ||||||||
| Pfam | PF02790 | ||||||||
| InterPro | IPR011759 | ||||||||
| PROSITE | PDOC00075 | ||||||||
| SCOP | 1occ | ||||||||
| SUPERFAMILY | 1occ | ||||||||
| TCDB | 3.D.4 | ||||||||
| OPM superfamily | 4 | ||||||||
| OPM protein | 1v55 | ||||||||
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| Cytochrome C oxidase subunit II, periplasmic domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | COX2 | ||||||||
| Pfam | PF00116 | ||||||||
| InterPro | IPR002429 | ||||||||
| PROSITE | PDOC00075 | ||||||||
| SCOP | 1occ | ||||||||
| SUPERFAMILY | 1occ | ||||||||
| TCDB | 3.D.4 | ||||||||
| OPM superfamily | 4 | ||||||||
| OPM protein | 1v55 | ||||||||
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Cytochrome c oxidase subunit II, abbreviated CoxII, is the second subunit of cytochrome c oxidase.
Cytochrome c oxidase (EC 1.9.3.1)[1][2] is an oligomeric enzymatic complex which is a component of the respiratory chain and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The enzyme complex consists of 3-4 subunits (prokaryotes) to up to 13 polypeptides (mammals). In Leigh's disease, there may be an abnormality or deficiency of cytochrome oxidase.
Subunit 2 (CO II) transfers the electrons from cytochrome c to the catalytic subunit 1. It contains two adjacent transmembrane regions in its N-terminus and the major part of the protein is exposed to the periplasmic or to the mitochondrial intermembrane space, respectively. CO II provides the substrate-binding site and contains a copper centre called Cu(A) (see IPR001505), probably the primary acceptor in cytochrome c oxidase. An exception is the corresponding subunit of the cbb3-type oxidase which lacks the copper A redox-centre. Several bacterial CO II have a C-terminal extension that contains a covalently bound haem c.
The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.
[edit] Human proteins containing this domain
[edit] References
- ^ Capaldi RA, Malatesta F, Darley-Usmar VM (1983). "Structure of cytochrome c oxidase". Biochimica et biophysica acta 726 (2): 135–148. PMID 6307356.
- ^ García-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB (September 1994). "The superfamily of heme-copper respiratory oxidases". Journal of bacteriology 176 (18): 5587–5600. PMC 196760. PMID 8083153. http://jb.asm.org/content/176/18/5587.full.pdf.
[edit] Further reading
- Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S (1996). "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A". Science 272 (5265): 1136–44. Bibcode 1996Sci...272.1136T. doi:10.1126/science.272.5265.1136. PMID 8638158.
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No Pfam abstract.
Literature references
-
Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S; , Science 1996;272:1136-1144.: The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. PUBMED:8638158 EPMC:8638158
Internal database links
| Similarity to PfamA using HHSearch: | Cupredoxin_1 |
External database links
| HOMSTRAD: | COX2 |
| PANDIT: | PF00116 |
| PROSITE: | PDOC00075 |
| Pseudofam: | PF00116 |
| SCOP: | 1occ |
| SYSTERS: | COX2 |
| Transporter classification: | 3.D.4 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002429
Cytochrome c oxidase (EC) [PUBMED:6307356, PUBMED:8083153] is an oligomeric enzymatic complex which is a component of the respiratory chain and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The number of polypeptides in the complex ranges from 3-4 (prokaryotes), up to 13(mammals).
Subunit 2 (CO II) transfers the electrons from cytochrome c to the catalytic subunit 1. It contains two adjacent transmembrane regions in its N terminus and the major part of the protein is exposed to the periplasmic or to the mitochondrial intermembrane space, respectively. CO II provides the substrate-binding site and contains a copper centre called Cu(A), probably the primary acceptor in cytochrome c oxidase. An exception is the corresponding subunit of the cbb3-type oxidase which lacks the copper A redox-centre. Several bacterial CO II have a C-terminal extension that contains a covalently bound haem c.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | membrane (GO:0016020) |
| Molecular function | copper ion binding (GO:0005507) |
| cytochrome-c oxidase activity (GO:0004129) |
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 CU_oxidase (CL0026), which contains the following 9 members:
Copper-bind COX2 Cu-oxidase Cu-oxidase_2 Cu-oxidase_3 Cu_bind_like Cupredoxin_1 Ephrin SoxEAlignments
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (32) |
Full (31269) |
Representative proteomes | NCBI (28095) |
Meta (2586) |
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| RP15 (349) |
RP35 (789) |
RP55 (1076) |
RP75 (1320) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (32) |
Full (31269) |
Representative proteomes | NCBI (28095) |
Meta (2586) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (349) |
RP35 (789) |
RP55 (1076) |
RP75 (1320) |
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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.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
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: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Sonnhammer ELL, Griffiths-Jones SR |
| Number in seed: | 32 |
| Number in full: | 31269 |
| Average length of the domain: | 106.00 aa |
| Average identity of full alignment: | 48 % |
| Average coverage of the sequence by the domain: | 47.64 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 120 | ||||||||||||
| 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 COX2 domain has been found. There are 144 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