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Conserved domains on  [gi|526246788|gb|AGR67510|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Bactrocera latifrons]

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 ...
 1-195 1.54e-124

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: 360.72  E-value: 1.54e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00153  38 ELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00153 118 SGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSL 197

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00153 198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-195 1.54e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 360.72  E-value: 1.54e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00153  38 ELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00153 118 SGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSL 197

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00153 198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-195 5.62e-110

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: 322.90  E-value: 5.62e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:cd01663   31 ELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:cd01663  111 GGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSL 190

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:cd01663  191 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-195 1.69e-61

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 199.20  E-value: 1.69e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPG-TLIGNDQiYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMV 79
Cdd:COG0843   43 QLAGPGlGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  80 ENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLS 159
Cdd:COG0843  121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 526246788 160 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:COG0843  201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-195 1.45e-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: 128.84  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788    1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMve 80
Cdd:pfam00115  27 QLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   81 nGAGTGWTVYPPLssviahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFdRMPLFVWAVVLTALLLLLSL 160
Cdd:pfam00115 104 -GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 526246788  161 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHL 195
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 13-195 4.44e-29

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: 113.03  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   13 QIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPP 92
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   93 LSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLT 172
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248

                         170       180
                  ....*....|....*....|...
gi 526246788  173 DRNLNTSFFDPAGGGDPILYQHL 195
Cdd:TIGR02882 249 DRIFDTAFFTVAHGGMPMLWANL 271
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-195 1.54e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 360.72  E-value: 1.54e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00153  38 ELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00153 118 SGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSL 197

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00153 198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-195 5.62e-110

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: 322.90  E-value: 5.62e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:cd01663   31 ELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:cd01663  111 GGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSL 190

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:cd01663  191 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-195 7.15e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 315.85  E-value: 7.15e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00167  40 ELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00167 120 AGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00167 200 PVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-195 1.61e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 309.73  E-value: 1.61e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00142  38 ELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00142 118 SGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSL 197

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00142 198 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 232
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-195 3.19e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 308.83  E-value: 3.19e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00223  37 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00223 117 SGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSL 196

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00223 197 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 231
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-195 5.73e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 305.86  E-value: 5.73e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00116  40 ELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00116 120 AGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00116 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-195 3.93e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 283.33  E-value: 3.93e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00007  37 ELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00007 117 KGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSL 196

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00007 197 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 231
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-195 1.51e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 281.72  E-value: 1.51e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00037  40 ELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00037 120 SGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00037 200 PVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHL 234
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-195 1.63e-92

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 279.07  E-value: 1.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00103  40 ELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00103 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00103 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-195 5.68e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 277.96  E-value: 5.68e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00183  40 ELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00183 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00183 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-195 1.92e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 276.44  E-value: 1.92e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00077  40 ELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00077 120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00077 200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHL 234
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-195 2.03e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 268.62  E-value: 2.03e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00184  42 ELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00184 122 QGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSL 201

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00184 202 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 236
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-195 3.66e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 268.23  E-value: 3.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00182  42 ELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00182 122 QGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSL 201

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00182 202 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHL 236
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-195 2.68e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 257.69  E-value: 2.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00079  41 ELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVD 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSvIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00079 121 MGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSL 199

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00079 200 PVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHL 234
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-195 1.47e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 248.77  E-value: 1.47e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:MTH00026  41 ELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:MTH00026 121 QGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSL 200

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00026 201 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 235
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-195 6.97e-70

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: 219.32  E-value: 6.97e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVE 80
Cdd:cd00919   29 ELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  81 NGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSL 160
Cdd:cd00919  108 GGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLAL 187

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 526246788 161 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:cd00919  188 PVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHL 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-195 1.69e-61

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 199.20  E-value: 1.69e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   1 ELGNPG-TLIGNDQiYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMV 79
Cdd:COG0843   43 QLAGPGlGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  80 ENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLS 159
Cdd:COG0843  121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 526246788 160 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:COG0843  201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 14-195 1.41e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 175.64  E-value: 1.41e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  14 IYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVenGAGTGWTVYPPL 93
Cdd:MTH00048  54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  94 SSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFdRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTD 173
Cdd:MTH00048 132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                        170       180
                 ....*....|....*....|..
gi 526246788 174 RNLNTSFFDPAGGGDPILYQHL 195
Cdd:MTH00048 211 RNFGSAFFDPLGGGDPVLFQHM 232
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 6-195 9.64e-52

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: 173.15  E-value: 9.64e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   6 GTLIGNDQiYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGT 85
Cdd:cd01662   41 NDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  86 GWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSLPVLAG 165
Cdd:cd01662  119 GWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTA 198

                        170       180       190
                 ....*....|....*....|....*....|
gi 526246788 166 AITMLLTDRNLNTSFFDPAGGGDPILYQHL 195
Cdd:cd01662  199 ALALLELDRYFGTHFFTNALGGNPMLWQHL 228
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-195 1.45e-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: 128.84  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788    1 ELGNPGTLIGNDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMve 80
Cdd:pfam00115  27 QLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   81 nGAGTGWTVYPPLssviahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFdRMPLFVWAVVLTALLLLLSL 160
Cdd:pfam00115 104 -GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 526246788  161 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHL 195
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 15-195 1.22e-33

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 125.82  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  15 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLS 94
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788  95 SVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDR 174
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 526246788 175 NLNTSFFDPAGGGDPILYQHL 195
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 13-195 4.44e-29

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: 113.03  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   13 QIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPP 92
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526246788   93 LSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLT 172
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248

                         170       180
                  ....*....|....*....|...
gi 526246788  173 DRNLNTSFFDPAGGGDPILYQHL 195
Cdd:TIGR02882 249 DRIFDTAFFTVAHGGMPMLWANL 271
 
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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