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Conserved domains on  [gi|1679341951|gb|QCY50429|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Aleiodes sp. BF002867]

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 ...
 1-197 8.82e-102

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: 302.56  E-value: 8.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00153   40 GQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00153  120 AGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPV 199

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-197 8.82e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 302.56  E-value: 8.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00153   40 GQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00153  120 AGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPV 199

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-197 2.76e-95

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: 285.53  E-value: 2.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:cd01663    33 SQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:cd01663   113 AGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPV 192

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:cd01663   193 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFF 229
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
13-197 3.47e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 180.32  E-value: 3.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  13 YNGMVTLHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGTGWTMYPPLS 92
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  93 SLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAGAITMLLTDR 172
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                         170       180
                  ....*....|....*....|....*
gi 1679341951 173 NLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLFWFF 240
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 11-197 1.63e-29

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: 112.67  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  11 QIYNGMVTLHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGvinTGVGTGWTMYPP 90
Cdd:pfam00115  39 LTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  91 LsslighngISVDMSIFSLHLAGASSIMGAINFISTIFNM--NLMTIKMDqimLLIWSISITPILLLLSLPVLAGAITML 168
Cdd:pfam00115 115 L--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRraPGMTLRMP---LFVWAILATAILILLAFPVLAAALLLL 183

                         170       180
                  ....*....|....*....|....*....
gi 1679341951 169 LTDRNLNTrffdfsGG*DPILFQHLFWFF 197
Cdd:pfam00115 184 LLDRSLGA------GGGDPLLDQHLFWWF 206
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-195 1.67e-27

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: 108.40  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  11 QIYNGMVTLHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGTGWTMYPP 90
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  91 LSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAGAITMLLT 170
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248

                         170       180
                  ....*....|....*....|....*
gi 1679341951 171 DRNLNTRFFDFSGG*DPILFQHLFW 195
Cdd:TIGR02882 249 DRIFDTAFFTVAHGGMPMLWANLFW 273
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-197 8.82e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 302.56  E-value: 8.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00153   40 GQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00153  120 AGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPV 199

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-197 2.76e-95

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: 285.53  E-value: 2.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:cd01663    33 SQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:cd01663   113 AGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPV 192

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:cd01663   193 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFF 229
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-197 2.06e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 276.17  E-value: 2.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00167   42 SQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00167  122 AGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPV 201

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00167  202 LAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-197 3.36e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 275.70  E-value: 3.36e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00223   39 GQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00223  119 VGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPV 198

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00223  199 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 4-197 6.13e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 270.04  E-value: 6.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   4 GSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGT 83
Cdd:MTH00116   45 GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  84 GWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAG 163
Cdd:MTH00116  125 GWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAA 204

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1679341951 164 AITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00116  205 GITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 4-197 2.14e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 260.81  E-value: 2.14e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   4 GSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGT 83
Cdd:MTH00142   43 GSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  84 GWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAG 163
Cdd:MTH00142  123 GWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAG 202

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1679341951 164 AITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00142  203 AITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFF 236
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-197 4.00e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 247.44  E-value: 4.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00037   42 AQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00037  122 AGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPV 201

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00037  202 LAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFF 238
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-197 1.04e-78

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 243.66  E-value: 1.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00007   39 GQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00007  119 VGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPV 198

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00007  199 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-197 1.30e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 243.68  E-value: 1.30e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00183   42 SQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00183  122 AGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPV 201

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00183  202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-197 2.73e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 240.23  E-value: 2.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00077   42 SQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00077  122 AGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPV 201

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00077  202 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFF 238
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 4-197 4.35e-77

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 239.40  E-value: 4.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   4 GSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGT 83
Cdd:MTH00103   45 GTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  84 GWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAG 163
Cdd:MTH00103  125 GWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAA 204

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1679341951 164 AITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00103  205 GITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-197 3.87e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 237.41  E-value: 3.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00182   44 SAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00182  124 AGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPV 203

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00182  204 LAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-197 1.44e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 235.88  E-value: 1.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00184   44 SAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00184  124 AGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPV 203

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00184  204 LAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-197 3.43e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 224.17  E-value: 3.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00079   43 SKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLiGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00079  123 PGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPV 201

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00079  202 LAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFF 238
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-197 5.40e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 216.42  E-value: 5.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:MTH00026   43 SSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:MTH00026  123 AGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPV 202

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00026  203 LAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 239
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-197 2.09e-59

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: 192.36  E-value: 2.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951   1 STSGSILKNDQIYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTG 80
Cdd:cd00919    31 ATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  81 VGTGWTMYPPLSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPV 160
Cdd:cd00919   110 AGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPV 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1679341951 161 LAGAITMLLTDRNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:cd00919   190 LAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
13-197 3.47e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 180.32  E-value: 3.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  13 YNGMVTLHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGTGWTMYPPLS 92
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  93 SLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAGAITMLLTDR 172
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                         170       180
                  ....*....|....*....|....*
gi 1679341951 173 NLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLFWFF 240
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 12-197 1.02e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 178.72  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  12 IYNGMVTLHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVIntGVGTGWTMYPPL 91
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  92 SSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIkMDQIMLLIWSISITPILLLLSLPVLAGAITMLLTD 171
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                         170       180
                  ....*....|....*....|....*.
gi 1679341951 172 RNLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:MTH00048  211 RNFGSAFFDPLGGGDPVLFQHMFWFF 236
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 13-197 7.44e-46

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: 157.74  E-value: 7.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  13 YNGMVTLHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGTGWTMYPPLS 92
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  93 SLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAGAITMLLTDR 172
Cdd:cd01662   128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207

                         170       180
                  ....*....|....*....|....*
gi 1679341951 173 NLNTRFFDFSGG*DPILFQHLFWFF 197
Cdd:cd01662   208 YFGTHFFTNALGGNPMLWQHLFWIF 232
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 11-197 1.63e-29

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: 112.67  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  11 QIYNGMVTLHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGvinTGVGTGWTMYPP 90
Cdd:pfam00115  39 LTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  91 LsslighngISVDMSIFSLHLAGASSIMGAINFISTIFNM--NLMTIKMDqimLLIWSISITPILLLLSLPVLAGAITML 168
Cdd:pfam00115 115 L--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRraPGMTLRMP---LFVWAILATAILILLAFPVLAAALLLL 183

                         170       180
                  ....*....|....*....|....*....
gi 1679341951 169 LTDRNLNTrffdfsGG*DPILFQHLFWFF 197
Cdd:pfam00115 184 LLDRSLGA------GGGDPLLDQHLFWWF 206
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-195 1.67e-27

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: 108.40  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  11 QIYNGMVTLHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGTGWTMYPP 90
Cdd:TIGR02882  90 QHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAP 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  91 LSSLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAGAITMLLT 170
Cdd:TIGR02882 169 LAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTT 248

                         170       180
                  ....*....|....*....|....*
gi 1679341951 171 DRNLNTRFFDFSGG*DPILFQHLFW 195
Cdd:TIGR02882 249 DRIFDTAFFTVAHGGMPMLWANLFW 273
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 13-195 2.15e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 102.32  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  13 YNGMVTLHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLIPSLMLLLISGVINTGVGTGWTMYPPLS 92
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679341951  93 SLIGHNGISVDMSIFSLHLAGASSIMGAINFISTIFNMNLMTIKMDQIMLLIWSISITPILLLLSLPVLAGAITMLLTDR 172
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|...
gi 1679341951 173 NLNTRFFDFSGG*DPILFQHLFW 195
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIW 280
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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