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Conserved domains on  [gi|808155393|gb|AKC97025|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Arthropoda sp. NZAC 03010149]

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 ...
 1-207 1.73e-131

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: 378.83  E-value: 1.73e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00153  27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00153 107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00153 187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-207 1.73e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 378.83  E-value: 1.73e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00153  27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00153 107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00153 187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-207 1.34e-118

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: 345.24  E-value: 1.34e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:cd01663   20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:cd01663  100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:cd01663  180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-207 2.57e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 209.98  E-value: 2.57e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   2 GLGLSMIIRSELINCG-DFIGDDQiYNVIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:COG0843   33 GGLLALLMRLQLAGPGlGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:COG0843  111 GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:COG0843  191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-207 1.85e-38

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: 137.32  E-value: 1.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393    2 GLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSL 81
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   82 ILLLVSGlveSGVGTGWTVYPPLasgvahsgASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLeSIPLFVWSVF 161
Cdd:pfam00115  96 VLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808155393  162 ITAILLLLSLPVLAGAITMLLTDRNINTsffdpsGGGDPILYQHLF 207
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 6-207 7.37e-32

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: 121.11  E-value: 7.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393    6 SMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLILLL 85
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   86 VSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSVFITAI 165
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 808155393  166 LLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-207 1.73e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 378.83  E-value: 1.73e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00153  27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00153 107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00153 187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-207 1.34e-118

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: 345.24  E-value: 1.34e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:cd01663   20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:cd01663  100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:cd01663  180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-207 1.38e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 335.88  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00167  29 VGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00167 109 LLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSI 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00167 189 LVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-207 1.05e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 328.59  E-value: 1.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00116  29 VGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00116 109 FLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00116 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-207 1.78e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 327.84  E-value: 1.78e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   2 GLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSL 81
Cdd:MTH00142  28 GTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  82 ILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSVF 161
Cdd:MTH00142 108 LLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVK 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 808155393 162 ITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00142 188 ITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-207 7.16e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 326.55  E-value: 7.16e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00223  26 VGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00223 106 LYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSV 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00223 186 KVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-207 6.96e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 301.05  E-value: 6.96e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00007  26 LGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00007 106 LILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAV 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00007 186 VITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-207 1.36e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 300.59  E-value: 1.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00037  29 VGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00037 109 FLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00037 189 FITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-207 6.92e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 293.37  E-value: 6.92e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00183  29 VGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00183 109 FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00183 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-207 7.32e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 290.63  E-value: 7.32e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00103  29 VGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00103 109 FLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00103 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-207 1.23e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 290.30  E-value: 1.23e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00077  29 VGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00077 109 FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00077 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-207 7.87e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 278.24  E-value: 7.87e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00182  31 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00182 111 LILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSI 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00182 191 LITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-207 2.97e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 276.71  E-value: 2.97e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00184  31 IGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00184 111 LTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSI 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00184 191 LVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-207 2.90e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 271.17  E-value: 2.90e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00079  30 VGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLaSGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00079 110 LFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00079 189 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-207 5.27e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 261.10  E-value: 5.27e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00026  30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:MTH00026 110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00026 190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-207 1.82e-74

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: 231.65  E-value: 1.82e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:cd00919   18 LGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:cd00919   97 LLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSV 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:cd00919  177 LVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-207 2.57e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 209.98  E-value: 2.57e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   2 GLGLSMIIRSELINCG-DFIGDDQiYNVIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:COG0843   33 GGLLALLMRLQLAGPGlGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSV 160
Cdd:COG0843  111 GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:COG0843  191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-207 1.21e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 191.81  E-value: 1.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 80
Cdd:MTH00048  30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  81 LILLLVSGLVesGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESiPLFVWSV 160
Cdd:MTH00048 110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SIILWSY 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 808155393 161 FITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:MTH00048 187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-207 8.97e-53

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: 176.23  E-value: 8.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   1 MGLGLSMIIRSEL-INCGDFIGDDQiYNVIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 79
Cdd:cd01662   24 RGGVDALLMRTQLaLPGNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  80 SLILLLVSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWS 159
Cdd:cd01662  102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 808155393 160 VFITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:cd01662  182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-207 1.85e-38

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: 137.32  E-value: 1.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393    2 GLGLSMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSL 81
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   82 ILLLVSGlveSGVGTGWTVYPPLasgvahsgASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLeSIPLFVWSVF 161
Cdd:pfam00115  96 VLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808155393  162 ITAILLLLSLPVLAGAITMLLTDRNINTsffdpsGGGDPILYQHLF 207
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 6-207 7.37e-32

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: 121.11  E-value: 7.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393    6 SMIIRSELINCGDFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLILLL 85
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393   86 VSGLVESGVGTGWTVYPPLASGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSVFITAI 165
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 808155393  166 LLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF 207
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 26-206 1.34e-31

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 120.81  E-value: 1.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393  26 YNVIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLILLLVSGLVESGVGTGWTVYPPLA 105
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808155393 106 SGVAHSGASVDLAIFSLHLAGASSILGAVNFITTVINMRSNGINLESIPLFVWSVFITAILLLLSLPVLAGAITMLLTDR 185
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 808155393 186 NINTSFFDPSGGGDPILYQHL 206
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 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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