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Conserved domains on  [gi|2177158286|gb|UIR90809|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pterocladiella capillacea]

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 ...
 1-224 1.37e-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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 379.13  E-value: 1.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:cd01663    85 FPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:cd01663   165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
 
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 ...
 1-224 1.37e-131

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: 379.13  E-value: 1.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:cd01663    85 FPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:cd01663   165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-224 2.94e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 371.51  E-value: 2.94e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00153   92 FPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00153  172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-224 8.73e-79

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 245.42  E-value: 8.73e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMA 80
Cdd:COG0843    19 GIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:COG0843    96 FPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:COG0843   176 PGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-224 4.80e-47

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: 160.43  E-value: 4.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMA 80
Cdd:pfam00115   3 GLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMyRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWF 224
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWW 205
 
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 ...
 1-224 1.37e-131

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: 379.13  E-value: 1.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:cd01663    85 FPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:cd01663   165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-224 2.94e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 371.51  E-value: 2.94e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00153   92 FPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00153  172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-224 8.97e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 339.73  E-value: 8.97e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00167   16 GTLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00167   94 FPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00167  174 PGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-224 6.42e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 332.44  E-value: 6.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00116   16 GTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00116   94 FPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00116  174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-224 5.89e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 330.02  E-value: 5.89e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00223   13 GTLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00223   91 FPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRS 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00223  171 PGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 234
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-224 5.31e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 322.44  E-value: 5.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00142   14 GTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00142   92 FPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00142  172 GGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-224 1.07e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 309.44  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00182   18 GTLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00182   96 FPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00182  176 PGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWF 239
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-224 5.06e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 304.83  E-value: 5.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00184   18 GTLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00184   96 FPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00184  176 PGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-224 5.93e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 304.45  E-value: 5.93e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00037   16 GTLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00037   94 FPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00037  174 PGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWF 237
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-224 1.28e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 298.72  E-value: 1.28e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00103   16 GTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00103   94 FPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00103  174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-224 1.86e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 298.01  E-value: 1.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00077   16 GTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00077   94 FPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00077  174 PSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWF 237
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-224 4.96e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 294.52  E-value: 4.96e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00183   16 GTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00183   94 FPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00183  174 PAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-224 7.86e-98

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 293.73  E-value: 7.86e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00007   13 GTLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00007   91 FPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRW 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00007  171 KGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 234
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-224 1.64e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 280.03  E-value: 1.64e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00079   17 GTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSiQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00079   95 FPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRS 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00079  174 SSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-224 3.27e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 280.36  E-value: 3.27e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00026   17 GSLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00026   95 FPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRT 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00026  175 PGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-224 6.24e-83

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: 253.99  E-value: 6.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPiMIGSPDMA 80
Cdd:cd00919     5 GLLYLIFAFVALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:cd00919    82 FPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:cd00919   162 PGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-224 8.73e-79

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 245.42  E-value: 8.73e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMA 80
Cdd:COG0843    19 GIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:COG0843    96 FPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:COG0843   176 PGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-224 2.47e-65

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: 209.74  E-value: 2.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMA 80
Cdd:cd01662    11 GIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:cd01662    88 FPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:cd01662   168 PGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWI 231
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-224 3.52e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 199.13  E-value: 3.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMA 80
Cdd:MTH00048   17 GVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALVevGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:MTH00048   95 LPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFM 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PgQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWF 224
Cdd:MTH00048  173 T-NVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-224 4.80e-47

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: 160.43  E-value: 4.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMA 80
Cdd:pfam00115   3 GLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  81 FPRLNNISFWLLPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRN 160
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2177158286 161 PGQTMyRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWF 224
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWW 205
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-223 1.42e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 135.45  E-value: 1.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286   1 GTLYLIFGAFSGILGGCMSILIRME--LAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPD 78
Cdd:PRK15017   58 GIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARD 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158286  79 MAFPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNM 158
Cdd:PRK15017  136 VAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKM 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2177158286 159 RNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFW 223
Cdd:PRK15017  216 RAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
 
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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