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Conserved domains on  [gi|821663822|gb|AKH52877|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Chloealtis sp. BOLD:AAG5330]

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 ...
 1-186 1.99e-127

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: 367.66  E-value: 1.99e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00153  37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAG 222
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-186 1.99e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 367.66  E-value: 1.99e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00153  37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAG 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-186 2.70e-112

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: 328.29  E-value: 2.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:cd01663   30 LELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:cd01663  110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:cd01663  190 LPVLAGAITMLLTDRNFNTSFFDPAG 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-186 5.59e-57

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 187.26  E-value: 5.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:COG0843   42 LQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:COG0843  121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:COG0843  201 FPVLAAALLLLLLDRSLGTHFFDPAG 226
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-185 2.33e-35

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: 128.07  E-value: 2.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822    1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMv 80
Cdd:pfam00115  26 LQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   81 dsGVGTGWTVYPPLasniahsgASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLdQTPLFFWSVGITALLLLLS 160
Cdd:pfam00115 104 --GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180
                  ....*....|....*....|....*
gi 821663822  161 LPVLAGAITMLLTDRNLNTSFFDPA 185
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-185 7.78e-30

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: 114.57  E-value: 7.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   12 DDQIYNVIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVDSGVGTGWTVY 91
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   92 PPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSLPVLAGAITML 171
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170
                  ....*....|....
gi 821663822  172 LTDRNLNTSFFDPA 185
Cdd:TIGR02882 247 TTDRIFDTAFFTVA 260
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-186 1.99e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 367.66  E-value: 1.99e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00153  37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAG 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-186 2.70e-112

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: 328.29  E-value: 2.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:cd01663   30 LELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:cd01663  110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:cd01663  190 LPVLAGAITMLLTDRNFNTSFFDPAG 215
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-186 2.53e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 324.35  E-value: 2.53e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00116  39 AELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00116 119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00116 199 LPVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-186 2.88e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 323.94  E-value: 2.88e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00167  39 AELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00167 119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLS 198

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00167 199 LPVLAAAITMLLTDRNLNTTFFDPAG 224
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-186 3.26e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 311.27  E-value: 3.26e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   2 ELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVD 81
Cdd:MTH00142  38 ELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  82 SGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSL 161
Cdd:MTH00142 118 SGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSL 197

                        170       180
                 ....*....|....*....|....*
gi 821663822 162 PVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00142 198 PVLAGAITMLLTDRNFNTSFFDPAG 222
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-186 4.10e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 310.76  E-value: 4.10e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00223  36 AELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00223 116 ESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLS 195

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00223 196 LPVLAGAITMLLTDRNFNTSFFDPAG 221
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-186 3.56e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 290.63  E-value: 3.56e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00103  39 AELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00103 119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00103 199 LPVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-186 4.82e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 287.61  E-value: 4.82e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   2 ELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVD 81
Cdd:MTH00077  40 ELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  82 SGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSL 161
Cdd:MTH00077 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180
                 ....*....|....*....|....*
gi 821663822 162 PVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00077 200 PVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-186 3.90e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 285.66  E-value: 3.90e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   2 ELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVD 81
Cdd:MTH00183  40 ELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  82 SGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSL 161
Cdd:MTH00183 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSL 199

                        170       180
                 ....*....|....*....|....*
gi 821663822 162 PVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00183 200 PVLAAGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-186 1.89e-93

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 281.02  E-value: 1.89e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00007  36 IELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00007 116 EKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLS 195

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00007 196 LPVLAGAITMLLTDRNLNTSFFDPAG 221
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-186 3.96e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 280.18  E-value: 3.96e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00037  39 TELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00037 119 ESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLS 198

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00037 199 LPVLAGAITMLLTDRNINTTFFDPAG 224
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-186 7.43e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 264.38  E-value: 7.43e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00182  41 LELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00182 121 EQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLS 200

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00182 201 LPVLAGAITMLLTDRNFNTTFFDPAG 226
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-186 3.41e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 262.46  E-value: 3.41e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00184  41 LELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00184 121 EQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLS 200

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00184 201 LPVLAGAITMLLTDRNFNTTFFDPAG 226
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-186 2.10e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 249.98  E-value: 2.10e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00079  40 LELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLaSNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00079 120 DMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLS 198

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00079 199 LPVLAGAITMLLTDRNLNTSFFDPST 224
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-186 2.46e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 245.31  E-value: 2.46e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:MTH00026  40 LELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:MTH00026 120 EQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLS 199

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00026 200 LPVLAGAITMLLTDRNFNTTFFDPAG 225
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-186 1.63e-66

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: 210.46  E-value: 1.63e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:cd00919   28 LELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:cd00919  107 GGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLA 186

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:cd00919  187 LPVLAAALVMLLLDRNFGTSFFDPAG 212
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-186 5.59e-57

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 187.26  E-value: 5.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMV 80
Cdd:COG0843   42 LQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  81 DSGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLS 160
Cdd:COG0843  121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                        170       180
                 ....*....|....*....|....*.
gi 821663822 161 LPVLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:COG0843  201 FPVLAAALLLLLLDRSLGTHFFDPAG 226
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-186 6.98e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 167.93  E-value: 6.98e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   3 LGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVds 82
Cdd:MTH00048  42 FLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL-- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  83 GVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLdQTPLFFWSVGITALLLLLSLP 162
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                        170       180
                 ....*....|....*....|....
gi 821663822 163 VLAGAITMLLTDRNLNTSFFDPAG 186
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLG 222
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 16-186 1.06e-42

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: 148.88  E-value: 1.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  16 YNVIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVDSGVGTGWTVYPPLA 95
Cdd:cd01662   49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  96 SNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSLPVLAGAITMLLTDR 175
Cdd:cd01662  128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207

                        170
                 ....*....|.
gi 821663822 176 NLNTSFFDPAG 186
Cdd:cd01662  208 YFGTHFFTNAL 218
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-185 2.33e-35

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: 128.07  E-value: 2.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822    1 MELGQPGYLIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMv 80
Cdd:pfam00115  26 LQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   81 dsGVGTGWTVYPPLasniahsgASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLdQTPLFFWSVGITALLLLLS 160
Cdd:pfam00115 104 --GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180
                  ....*....|....*....|....*
gi 821663822  161 LPVLAGAITMLLTDRNLNTSFFDPA 185
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-185 7.78e-30

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: 114.57  E-value: 7.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   12 DDQIYNVIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVDSGVGTGWTVY 91
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822   92 PPLASNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSLPVLAGAITML 171
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170
                  ....*....|....
gi 821663822  172 LTDRNLNTSFFDPA 185
Cdd:TIGR02882 247 TTDRIFDTAFFTVA 260
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 16-182 1.70e-29

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 113.88  E-value: 1.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  16 YNVIITSHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMVDSGVGTGWTVYPPLA 95
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821663822  96 SNIAHSGASVDLAIFSLHLAGISSILGAVNFITTTINMQSESMTLDQTPLFFWSVGITALLLLLSLPVLAGAITMLLTDR 175
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                 ....*..
gi 821663822 176 NLNTSFF 182
Cdd:PRK15017 258 YLGTHFF 264
 
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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