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Conserved domains on  [gi|1913595463|gb|QOH28392|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Turbinaria tricostata]

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 ...
 1-208 9.09e-122

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 353.33  E-value: 9.09e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:cd01663    18 GLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:cd01663    96 LPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLF 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:cd01663   176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 9.09e-122

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: 353.33  E-value: 9.09e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:cd01663    18 GLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:cd01663    96 LPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLF 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:cd01663   176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-208 6.00e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 341.85  E-value: 6.00e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00153  103 LPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLF 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00153  183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-208 3.01e-72

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 228.09  E-value: 3.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   2 VLGTAMSVLIRLQLASPGNMFLGGnyQLYNVIVTAHAFLMIFFMVMPvLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLL 81
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSP--ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  82 PPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLFV 161
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1913595463 162 WSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQ 234
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-208 4.15e-42

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: 146.95  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFLGgnYQLYNVIVTAHAFLMIFFMVMPVlIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFLS--PLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSlveAGAGTGWTVYPPLSGiqahsgpsVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMhRLPLF 160
Cdd:pfam00115  91 VVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNttffdpAGGGDPVLYQ 208
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQ 200
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-207 2.21e-38

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 139.60  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   4 GTAMSVLIRLQLASPGNMFLGGNYqlYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPP 83
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  84 SLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLFVWS 163
Cdd:TIGR02882 145 GAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWT 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1913595463 164 VLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLY 207
Cdd:TIGR02882 225 TLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 9.09e-122

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: 353.33  E-value: 9.09e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:cd01663    18 GLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:cd01663    96 LPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLF 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:cd01663   176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-208 6.00e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 341.85  E-value: 6.00e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00153  103 LPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLF 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00153  183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-208 3.56e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 314.61  E-value: 3.56e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGnMFLGGNyQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00223   24 GLVGTSLSLLIRAELGQPG-ALLGDD-QLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00223  102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00223  182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 229
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-208 4.81e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 314.31  E-value: 4.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00167   27 GMVGTALSLLIRAELSQPGSLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00167  105 LPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00167  185 VWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-208 2.74e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 309.72  E-value: 2.74e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00116   27 GMVGTALSLLIRAELGQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00116  105 LPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00116  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-208 2.33e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 302.03  E-value: 2.33e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00142   25 GMVGTGLSLLIRAELGQPGSLL--GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00142  103 LPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLF 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00142  183 VWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 230
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-208 1.15e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 295.58  E-value: 1.15e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00182   29 GMIGTAFSMLIRLELSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00182  107 LPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLF 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00182  187 VWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQ 234
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-208 2.63e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 289.42  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00184   29 GMIGTAFSMLIRLELSAPGSML--GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00184  107 LPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLF 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00184  187 VWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQ 234
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-208 5.00e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 283.76  E-value: 5.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00077   27 GMVGTALSLLIRAELSQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00077  105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00077  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQ 232
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-208 1.69e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 279.89  E-value: 1.69e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00183   27 GMVGTALSLLIRAELSQPGALL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00183  105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00183  185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-208 2.46e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 279.41  E-value: 2.46e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00037   27 GMVGTAMSVIIRTELAQPGSLL--QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00037  105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00037  185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQ 232
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-208 3.08e-92

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 279.07  E-value: 3.08e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00103   27 GMVGTALSLLIRAELGQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00103  105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00103  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-208 1.38e-90

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 274.47  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNmFLGGNyQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00007   24 GLLGTSMSLLIRIELGQPGA-FLGSD-QLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00007  102 LPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLF 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00007  182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 229
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-208 3.03e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 264.18  E-value: 3.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00026   28 GAIGTAFSMLIRLELSSPGSML--GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00026  106 LPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLF 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00026  186 VWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQ 233
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-208 1.37e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 256.53  E-value: 1.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGnmFLGGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00079   28 GMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSgIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:MTH00079  106 LPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLF 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00079  185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQ 232
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-208 4.05e-76

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: 235.89  E-value: 4.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFLggNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPlMIGAPDMAFPRMNNISFWL 80
Cdd:cd00919    16 LLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:cd00919    93 FPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLF 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:cd00919   173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQ 220
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-208 3.01e-72

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 228.09  E-value: 3.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   2 VLGTAMSVLIRLQLASPGNMFLGGnyQLYNVIVTAHAFLMIFFMVMPvLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLL 81
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSP--ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  82 PPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLFV 161
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1913595463 162 WSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQ 234
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-208 1.25e-60

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: 197.03  E-value: 1.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   2 VLGTAMSVLIRLQLASPGNMFLGGnyQLYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDMAFPRMNNISFWLL 81
Cdd:cd01662    23 LRGGVDALLMRTQLALPGNDFLSP--EHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  82 PPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLFV 161
Cdd:cd01662   100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1913595463 162 WSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:cd01662   180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQ 226
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-208 2.80e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 180.64  E-value: 2.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFLggNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:MTH00048   28 GFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVeaGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSmHRLPLF 160
Cdd:MTH00048  106 LVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSII 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLYQ 208
Cdd:MTH00048  183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQ 230
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-208 4.15e-42

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: 146.95  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   1 GVLGTAMSVLIRLQLASPGNMFLGgnYQLYNVIVTAHAFLMIFFMVMPVlIGGFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFLS--PLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSlveAGAGTGWTVYPPLSGiqahsgpsVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMhRLPLF 160
Cdd:pfam00115  91 VVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNttffdpAGGGDPVLYQ 208
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQ 200
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-207 2.21e-38

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 139.60  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   4 GTAMSVLIRLQLASPGNMFLGGNYqlYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPP 83
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  84 SLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLFVWS 163
Cdd:TIGR02882 145 GAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWT 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1913595463 164 VLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLY 207
Cdd:TIGR02882 225 TLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 4-207 4.59e-37

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 136.22  E-value: 4.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463   4 GTAMSVLIRLQ--LASPGNM-FLGGNYqlYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDMAFPRMNNISFWL 80
Cdd:PRK15017   72 GFADAIMMRSQqaLASAGEAgFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595463  81 LPPSLILLLASSLVEAGAGTGWTVYPPLSGIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPGMSMHRLPLF 160
Cdd:PRK15017  149 TVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVF 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1913595463 161 VWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPVLY 207
Cdd:PRK15017  229 TWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMY 275
 
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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