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Conserved domains on  [gi|821680801|gb|AKH58552|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Tetrix subulata]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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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 ...
 1-123 1.62e-75

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: 232.07  E-value: 1.62e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00153 111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00153 191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-123 1.62e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 232.07  E-value: 1.62e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00153 111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00153 191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-123 4.13e-71

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: 220.05  E-value: 4.13e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:cd01663  104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:cd01663  184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-123 4.91e-43

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 147.58  E-value: 4.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:COG0843  115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:COG0843  195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 9-123 5.72e-22

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: 89.17  E-value: 5.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801    9 GAGTGWTVYPPLAGpiahsgaaVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMdQLPLFVWSVMITAILLLLSLP 88
Cdd:pfam00115 104 GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 821680801   89 VLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 123
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-123 1.62e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 232.07  E-value: 1.62e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00153 111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00153 191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-123 4.13e-71

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: 220.05  E-value: 4.13e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:cd01663  104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:cd01663  184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-123 1.60e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 211.46  E-value: 1.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00167 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTT 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00167 193 ILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-123 3.95e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 208.02  E-value: 3.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00116 113 LASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITA 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00116 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-123 3.84e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 205.34  E-value: 3.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00142 111 LSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITA 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00142 191 ILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-123 5.09e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 204.83  E-value: 5.09e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00223 110 LSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTA 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00223 190 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-123 1.44e-57

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 185.47  E-value: 1.44e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00103 113 LASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITA 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00103 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-123 6.61e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 183.99  E-value: 6.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00077 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITA 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00077 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-123 2.53e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 182.43  E-value: 2.53e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00183 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITA 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00183 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-123 2.85e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 182.33  E-value: 2.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00182 115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITA 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00182 195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-123 2.03e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 180.03  E-value: 2.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00037 113 LASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITA 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00037 193 FLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-123 3.63e-55

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 179.33  E-value: 3.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00007 110 VSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITV 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00007 190 VLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-123 7.83e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 178.48  E-value: 7.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00184 115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTT 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00184 195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-123 4.28e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 166.01  E-value: 4.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   3 SSIVDSGAGTGWTVYPPLAGpIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAIL 82
Cdd:MTH00079 116 SCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 821680801  83 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00079 195 LVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-123 7.27e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 165.57  E-value: 7.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:MTH00026 114 LGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITA 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00026 194 ILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-123 7.90e-48

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: 158.85  E-value: 7.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:cd00919  101 LSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTA 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:cd00919  181 ILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-123 4.91e-43

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 147.58  E-value: 4.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   1 ISSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITA 80
Cdd:COG0843  115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 821680801  81 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:COG0843  195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 9-123 9.47e-36

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 127.49  E-value: 9.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   9 GAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMdQLPLFVWSVMITAILLLLSLP 88
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 821680801  89 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-123 1.66e-33

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: 121.53  E-value: 1.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801   2 SSSIVDSGAGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAI 81
Cdd:cd01662  108 ASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSI 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 821680801  82 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 123
Cdd:cd01662  188 LILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 9-123 5.72e-22

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: 89.17  E-value: 5.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801    9 GAGTGWTVYPPLAGpiahsgaaVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMdQLPLFVWSVMITAILLLLSLP 88
Cdd:pfam00115 104 GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 821680801   89 VLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 123
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 10-122 2.20e-19

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 82.29  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821680801  10 AGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAILLLLSLPV 89
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100       110
                 ....*....|....*....|....*....|...
gi 821680801  90 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 122
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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