Summary: Cytochrome oxidase c subunit VIb
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This is the Wikipedia entry entitled "Cytochrome c oxidase". More...
Cytochrome c oxidase Edit Wikipedia article
The enzyme cytochrome c oxidase is a large transmembrane protein found in the mitochondrion and is the terminal electron acceptor in the electron transfer chain, taking four reducing equivalents from cytochrome c and converting molecular oxygen to water. In the process, it translocates protons, helping to establish a chemiosmotic potential that ATP synthase then uses to synthesize ATP.
Summary reaction:
4 Fe+2-cyochrome c + 4H+ + O2 → 4 Fe+3-cytochrome c + H20.
The complex is a large lipoprotein comprised of a number of metal prosthetic sites and 13 protein subunits, which in mammals, 10 are nuclear in origin and 3 are synthesized mitochondrially. The complex contains 2 cytochromes, the a and a3 cytochromes, and two copper centers, the CuA and CuB centers. In fact, the cytochrome a3 and CuB are a binuclear center and this is the site of oxygen reduction. The mechanism of action of this large complex is still an active research topic.
Further information
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Cytochrome oxidase c subunit VIb Provide feedback
Cytochrome c oxidase, a 13 sub-unit complex, EC:1.9.3.1 is the terminal oxidase in the mitochondrial electron transport chain. This family is composed of the potentially heme-binding subunit IVb of the oxidase.
Literature references
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Carrero-Valenzuela RD, Quan F, Lightowlers R, Kennaway NG, Litt M, Forte M; , Gene 1991;102:229-236.: Human cytochrome c oxidase subunit VIb: characterization and mapping of a multigene family. PUBMED:1651883 EPMC:1651883
Internal database links
SCOOP: | CHCH UPF0203 |
External database links
SCOP: | 2occ |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003213
Cytochrome c oxidase ( EC ) is an oligomeric enzymatic complex that is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen [ PUBMED:6307356 ]. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane.
In eukaryotes, in addition to the three large subunits, I, II and III, that form the catalytic centre of the enzyme complex, there are a variable number of small polypeptide subunits. One of these subunits is the potentially haem-binding subunit, VIb, which is encoded in the nucleus [ PUBMED:11136449 ]. Subunit VIb is one of three mammalian subunits that lacks a transmembrane region. It is located on the cytosolic side of the membrane and helps form the dimer interface with the corresponding subunit on the other monomer complex [ PUBMED:12874793 , PUBMED:16364442 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | respiratory chain complex IV (GO:0045277) |
mitochondrion (GO:0005739) |
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 CHCH (CL0351), which has the following description:
The conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain) superfamily members include NADH-ubiquinone oxidoreductases, some cytochrome oxidases and yeast mitochondrial ribosomal proteins. Within each helix of the CHCH domain there are two cysteines present in a C-X9-C motif.
The clan contains the following 8 members:
CHCH Cmc1 COX17 COX6B CX9C MTCP1 NDUF_B7 Ndufs5Alignments
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 and the UniProtKB sequence database. More...
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Seed (57) |
Full (3590) |
Representative proteomes | UniProt (5514) |
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RP15 (623) |
RP35 (1587) |
RP55 (2724) |
RP75 (3686) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (57) |
Full (3590) |
Representative proteomes | UniProt (5514) |
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RP15 (623) |
RP35 (1587) |
RP55 (2724) |
RP75 (3686) |
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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.
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.
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Curation and family details
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Curation
Seed source: | Pfam-B_9188 (release 5.2) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Mian N |
Number in seed: | 57 |
Number in full: | 3590 |
Average length of the domain: | 66.6 aa |
Average identity of full alignment: | 31 % |
Average coverage of the sequence by the domain: | 54.45 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 76 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 COX6B domain has been found. There are 136 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.