cytochrome oxidase subunit I, partial (mitochondrion) [Synthesiomyia nudiseta]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Heme_Cu_Oxidase_I super family | cl00275 | Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-78 | 1.43e-59 | ||
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily. The actual alignment was detected with superfamily member MTH00153: Pssm-ID: 469701 Cd Length: 511 Bit Score: 188.54 E-value: 1.43e-59
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| Name | Accession | Description | Interval | E-value | ||
| COX1 | MTH00153 | cytochrome c oxidase subunit I; Provisional |
1-78 | 1.43e-59 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177210 Cd Length: 511 Bit Score: 188.54 E-value: 1.43e-59
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| Cyt_c_Oxidase_I | cd01663 | Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-78 | 6.64e-53 | ||
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center. Pssm-ID: 238833 Cd Length: 488 Bit Score: 170.74 E-value: 6.64e-53
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| CyoB | COG0843 | Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-74 | 2.88e-32 | ||
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; Pssm-ID: 440605 Cd Length: 535 Bit Score: 115.99 E-value: 2.88e-32
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| CtaD_CoxA | TIGR02891 | cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-75 | 2.97e-32 | ||
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport] Pssm-ID: 213748 Cd Length: 499 Bit Score: 115.78 E-value: 2.97e-32
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| COX1 | pfam00115 | Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-78 | 1.01e-23 | ||
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members. Pssm-ID: 459678 Cd Length: 432 Bit Score: 91.87 E-value: 1.01e-23
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| Name | Accession | Description | Interval | E-value | ||
| COX1 | MTH00153 | cytochrome c oxidase subunit I; Provisional |
1-78 | 1.43e-59 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177210 Cd Length: 511 Bit Score: 188.54 E-value: 1.43e-59
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| Cyt_c_Oxidase_I | cd01663 | Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-78 | 6.64e-53 | ||
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center. Pssm-ID: 238833 Cd Length: 488 Bit Score: 170.74 E-value: 6.64e-53
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| COX1 | MTH00223 | cytochrome c oxidase subunit I; Provisional |
1-78 | 1.96e-48 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177260 Cd Length: 512 Bit Score: 159.37 E-value: 1.96e-48
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| COX1 | MTH00167 | cytochrome c oxidase subunit I; Provisional |
1-78 | 2.28e-47 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177222 Cd Length: 512 Bit Score: 156.76 E-value: 2.28e-47
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| COX1 | MTH00116 | cytochrome c oxidase subunit I; Provisional |
1-78 | 2.36e-47 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177177 Cd Length: 515 Bit Score: 156.79 E-value: 2.36e-47
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| COX1 | MTH00142 | cytochrome c oxidase subunit I; Provisional |
1-78 | 5.65e-47 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 214431 Cd Length: 511 Bit Score: 155.65 E-value: 5.65e-47
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| COX1 | MTH00183 | cytochrome c oxidase subunit I; Provisional |
1-78 | 1.18e-41 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177234 Cd Length: 516 Bit Score: 141.60 E-value: 1.18e-41
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| COX1 | MTH00103 | cytochrome c oxidase subunit I; Validated |
1-78 | 2.07e-41 | ||
cytochrome c oxidase subunit I; Validated Pssm-ID: 177165 Cd Length: 513 Bit Score: 140.79 E-value: 2.07e-41
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| COX1 | MTH00007 | cytochrome c oxidase subunit I; Validated |
1-78 | 2.35e-41 | ||
cytochrome c oxidase subunit I; Validated Pssm-ID: 133649 Cd Length: 511 Bit Score: 140.81 E-value: 2.35e-41
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| COX1 | MTH00037 | cytochrome c oxidase subunit I; Provisional |
1-78 | 3.10e-41 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177112 Cd Length: 517 Bit Score: 140.35 E-value: 3.10e-41
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| COX1 | MTH00077 | cytochrome c oxidase subunit I; Provisional |
1-78 | 1.11e-39 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 214419 Cd Length: 514 Bit Score: 136.22 E-value: 1.11e-39
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| COX1 | MTH00079 | cytochrome c oxidase subunit I; Provisional |
1-78 | 2.29e-39 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177148 Cd Length: 508 Bit Score: 135.19 E-value: 2.29e-39
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| COX1 | MTH00182 | cytochrome c oxidase subunit I; Provisional |
1-78 | 7.79e-39 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 214451 Cd Length: 525 Bit Score: 134.18 E-value: 7.79e-39
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| COX1 | MTH00184 | cytochrome c oxidase subunit I; Provisional |
1-78 | 8.95e-38 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177235 Cd Length: 519 Bit Score: 131.10 E-value: 8.95e-38
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| COX1 | MTH00048 | cytochrome c oxidase subunit I; Provisional |
1-78 | 2.65e-35 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 177123 Cd Length: 511 Bit Score: 124.40 E-value: 2.65e-35
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| COX1 | MTH00026 | cytochrome c oxidase subunit I; Provisional |
1-78 | 1.49e-33 | ||
cytochrome c oxidase subunit I; Provisional Pssm-ID: 164599 Cd Length: 534 Bit Score: 119.73 E-value: 1.49e-33
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| Heme_Cu_Oxidase_I | cd00919 | Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-78 | 3.99e-33 | ||
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily. Pssm-ID: 238461 Cd Length: 463 Bit Score: 117.63 E-value: 3.99e-33
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| CyoB | COG0843 | Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-74 | 2.88e-32 | ||
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; Pssm-ID: 440605 Cd Length: 535 Bit Score: 115.99 E-value: 2.88e-32
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| CtaD_CoxA | TIGR02891 | cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-75 | 2.97e-32 | ||
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport] Pssm-ID: 213748 Cd Length: 499 Bit Score: 115.78 E-value: 2.97e-32
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| Ubiquinol_Oxidase_I | cd01662 | Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-74 | 4.49e-29 | ||
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center. Pssm-ID: 238832 Cd Length: 501 Bit Score: 107.28 E-value: 4.49e-29
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| COX1 | pfam00115 | Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-78 | 1.01e-23 | ||
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members. Pssm-ID: 459678 Cd Length: 432 Bit Score: 91.87 E-value: 1.01e-23
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| ba3-like_Oxidase_I | cd01660 | ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
4-71 | 1.96e-03 | ||
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919. Pssm-ID: 238830 Cd Length: 473 Bit Score: 34.95 E-value: 1.96e-03
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