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cytochrome c oxidase subunit 2 (mitochondrion) [Lepilemur tymerlachsoni]
cytochrome c oxidase subunit II( domain architecture ID 11475897)
cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
COX2 | MTH00098 | cytochrome c oxidase subunit II; Validated |
1-227 | 1.14e-165 | ||||
cytochrome c oxidase subunit II; Validated : Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 455.72 E-value: 1.14e-165
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Name | Accession | Description | Interval | E-value | ||||
COX2 | MTH00098 | cytochrome c oxidase subunit II; Validated |
1-227 | 1.14e-165 | ||||
cytochrome c oxidase subunit II; Validated Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 455.72 E-value: 1.14e-165
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CcO_II_C | cd13912 | C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
93-222 | 1.88e-90 | ||||
C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I. Pssm-ID: 259979 [Multi-domain] Cd Length: 130 Bit Score: 261.74 E-value: 1.88e-90
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COX2 | pfam00116 | Cytochrome C oxidase subunit II, periplasmic domain; |
95-214 | 7.85e-79 | ||||
Cytochrome C oxidase subunit II, periplasmic domain; Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 232.30 E-value: 7.85e-79
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CyoA | COG1622 | Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
6-223 | 1.37e-52 | ||||
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 169.24 E-value: 1.37e-52
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CoxB | TIGR02866 | cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
12-223 | 8.93e-43 | ||||
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport] Pssm-ID: 274329 [Multi-domain] Cd Length: 199 Bit Score: 143.29 E-value: 8.93e-43
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Name | Accession | Description | Interval | E-value | ||||
COX2 | MTH00098 | cytochrome c oxidase subunit II; Validated |
1-227 | 1.14e-165 | ||||
cytochrome c oxidase subunit II; Validated Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 455.72 E-value: 1.14e-165
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COX2 | MTH00117 | cytochrome c oxidase subunit II; Provisional |
1-227 | 7.26e-157 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 177178 [Multi-domain] Cd Length: 227 Bit Score: 433.57 E-value: 7.26e-157
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COX2 | MTH00129 | cytochrome c oxidase subunit II; Provisional |
1-227 | 2.92e-139 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 177187 [Multi-domain] Cd Length: 230 Bit Score: 389.07 E-value: 2.92e-139
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COX2 | MTH00076 | cytochrome c oxidase subunit II; Provisional |
1-227 | 5.98e-138 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 164646 [Multi-domain] Cd Length: 228 Bit Score: 385.67 E-value: 5.98e-138
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COX2 | MTH00154 | cytochrome c oxidase subunit II; Provisional |
1-227 | 3.81e-132 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 214438 [Multi-domain] Cd Length: 227 Bit Score: 371.08 E-value: 3.81e-132
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COX2 | MTH00185 | cytochrome c oxidase subunit II; Provisional |
1-227 | 8.80e-129 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 164736 [Multi-domain] Cd Length: 230 Bit Score: 362.67 E-value: 8.80e-129
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COX2 | MTH00168 | cytochrome c oxidase subunit II; Provisional |
1-225 | 2.33e-125 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 177223 [Multi-domain] Cd Length: 225 Bit Score: 353.90 E-value: 2.33e-125
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COX2 | MTH00038 | cytochrome c oxidase subunit II; Provisional |
1-227 | 1.44e-122 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 177113 [Multi-domain] Cd Length: 229 Bit Score: 347.07 E-value: 1.44e-122
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COX2 | MTH00140 | cytochrome c oxidase subunit II; Provisional |
6-226 | 2.09e-122 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 346.54 E-value: 2.09e-122
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COX2 | MTH00139 | cytochrome c oxidase subunit II; Provisional |
1-226 | 5.04e-117 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 214429 [Multi-domain] Cd Length: 226 Bit Score: 332.84 E-value: 5.04e-117
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COX2 | MTH00008 | cytochrome c oxidase subunit II; Validated |
6-225 | 4.75e-109 | ||||
cytochrome c oxidase subunit II; Validated Pssm-ID: 164584 [Multi-domain] Cd Length: 228 Bit Score: 312.56 E-value: 4.75e-109
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COX2 | MTH00023 | cytochrome c oxidase subunit II; Validated |
4-226 | 9.10e-106 | ||||
cytochrome c oxidase subunit II; Validated Pssm-ID: 214402 [Multi-domain] Cd Length: 240 Bit Score: 304.75 E-value: 9.10e-106
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COX2 | MTH00051 | cytochrome c oxidase subunit II; Provisional |
4-226 | 7.43e-104 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 177126 [Multi-domain] Cd Length: 234 Bit Score: 299.77 E-value: 7.43e-104
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CcO_II_C | cd13912 | C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
93-222 | 1.88e-90 | ||||
C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I. Pssm-ID: 259979 [Multi-domain] Cd Length: 130 Bit Score: 261.74 E-value: 1.88e-90
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COX2 | MTH00027 | cytochrome c oxidase subunit II; Provisional |
4-223 | 1.47e-85 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 214405 [Multi-domain] Cd Length: 262 Bit Score: 254.56 E-value: 1.47e-85
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COX2 | pfam00116 | Cytochrome C oxidase subunit II, periplasmic domain; |
95-214 | 7.85e-79 | ||||
Cytochrome C oxidase subunit II, periplasmic domain; Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 232.30 E-value: 7.85e-79
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COX2 | MTH00080 | cytochrome c oxidase subunit II; Provisional |
23-227 | 1.00e-76 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 177149 [Multi-domain] Cd Length: 231 Bit Score: 230.67 E-value: 1.00e-76
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CyoA | COG1622 | Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
6-223 | 1.37e-52 | ||||
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 169.24 E-value: 1.37e-52
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COX2 | MTH00047 | cytochrome c oxidase subunit II; Provisional |
17-214 | 6.51e-45 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 214412 [Multi-domain] Cd Length: 194 Bit Score: 148.56 E-value: 6.51e-45
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PTZ00047 | PTZ00047 | cytochrome c oxidase subunit II; Provisional |
118-215 | 3.13e-44 | ||||
cytochrome c oxidase subunit II; Provisional Pssm-ID: 240243 [Multi-domain] Cd Length: 162 Bit Score: 145.73 E-value: 3.13e-44
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CoxB | TIGR02866 | cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
12-223 | 8.93e-43 | ||||
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport] Pssm-ID: 274329 [Multi-domain] Cd Length: 199 Bit Score: 143.29 E-value: 8.93e-43
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CuRO_HCO_II_like | cd13842 | Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ... |
95-212 | 1.26e-31 | ||||
Cupredoxin domain of Heme-copper oxidase subunit II; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259911 [Multi-domain] Cd Length: 95 Bit Score: 111.23 E-value: 1.26e-31
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CuRO_CcO_Caa3_II | cd04213 | The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ... |
94-207 | 3.72e-29 | ||||
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I. Pssm-ID: 259875 [Multi-domain] Cd Length: 103 Bit Score: 105.01 E-value: 3.72e-29
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COX2_TM | pfam02790 | Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ... |
1-83 | 1.22e-28 | ||||
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices. Pssm-ID: 397083 [Multi-domain] Cd Length: 89 Bit Score: 103.18 E-value: 1.22e-28
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CuRO_HCO_II_like_5 | cd13919 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
95-207 | 3.36e-22 | ||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259986 [Multi-domain] Cd Length: 107 Bit Score: 87.31 E-value: 3.36e-22
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CuRO_HCO_II_like_3 | cd13914 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
96-223 | 1.40e-20 | ||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259981 [Multi-domain] Cd Length: 108 Bit Score: 83.23 E-value: 1.40e-20
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CuRO_HCO_II_like_6 | cd13918 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
67-223 | 2.70e-20 | ||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259985 [Multi-domain] Cd Length: 139 Bit Score: 83.27 E-value: 2.70e-20
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CuRO_HCO_II_like_2 | cd13915 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
94-207 | 8.36e-19 | ||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259982 [Multi-domain] Cd Length: 98 Bit Score: 78.05 E-value: 8.36e-19
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ba3_CcO_II_C | cd13913 | C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ... |
140-207 | 1.53e-08 | ||||
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; 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. Pssm-ID: 259980 [Multi-domain] Cd Length: 99 Bit Score: 50.65 E-value: 1.53e-08
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Cupredoxin | cd00920 | Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
129-212 | 2.23e-08 | ||||
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II. Pssm-ID: 259860 [Multi-domain] Cd Length: 110 Bit Score: 50.69 E-value: 2.23e-08
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CuRO_UO_II | cd04212 | The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ... |
140-207 | 3.48e-05 | ||||
The cupredoxin domain of Ubiquinol oxidase subunit II; 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. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved. Pssm-ID: 259874 [Multi-domain] Cd Length: 99 Bit Score: 41.38 E-value: 3.48e-05
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CuRO_HCO_II_like_1 | cd13916 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
96-207 | 4.75e-05 | ||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259983 [Multi-domain] Cd Length: 93 Bit Score: 40.83 E-value: 4.75e-05
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N2OR_C | cd04223 | The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ... |
157-207 | 1.58e-03 | ||||
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain. Pssm-ID: 259885 [Multi-domain] Cd Length: 95 Bit Score: 36.83 E-value: 1.58e-03
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CuRO_HCO_II_like_4 | cd13917 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
151-207 | 5.28e-03 | ||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259984 [Multi-domain] Cd Length: 88 Bit Score: 35.04 E-value: 5.28e-03
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Blast search parameters | ||||
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