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Conserved domains on  [gi|1769324458|gb|QFS20490|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Carcinus maenas]

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 ...
 2-197 2.32e-125

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: 363.03  E-value: 2.32e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00153   22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-197 2.32e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 363.03  E-value: 2.32e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00153   22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-197 2.41e-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: 324.05  E-value: 2.41e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   1 SAWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSF 80
Cdd:cd01663    14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  81 WLLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMP 160
Cdd:cd01663    94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1769324458 161 LFVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:cd01663   174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF 210
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-197 2.76e-55

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 183.02  E-value: 2.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   4 AGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWLL 83
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  84 PPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFV 163
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1769324458 164 WAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHF 221
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-198 2.29e-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: 128.46  E-value: 2.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   1 SAWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSF 80
Cdd:pfam00115  10 ALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  81 WLLPPSLTLLLMSGMvesGVGTGWTVYPPLAGaiahagasVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMdQMP 160
Cdd:pfam00115  89 WLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1769324458 161 LFVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFG 198
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGG 194
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-197 2.18e-30

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 116.88  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  12 SLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPSLTLLL 91
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  92 MSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAVFITAI 171
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180
                  ....*....|....*....|....*.
gi 1769324458 172 LLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAF 256
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-197 2.32e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 363.03  E-value: 2.32e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00153   22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-197 2.41e-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: 324.05  E-value: 2.41e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   1 SAWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSF 80
Cdd:cd01663    14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  81 WLLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMP 160
Cdd:cd01663    94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1769324458 161 LFVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:cd01663   174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF 210
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-197 1.03e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 320.47  E-value: 1.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00167   24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00167  104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00167  184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTF 219
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-197 8.87e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 310.50  E-value: 8.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00142   22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00142  102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00142  182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSF 217
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-197 4.25e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 308.94  E-value: 4.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00116   24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00116  104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00116  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 3-197 1.93e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 301.90  E-value: 1.93e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   3 WAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWL 82
Cdd:MTH00223   22 WSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  83 LPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLF 162
Cdd:MTH00223  102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1769324458 163 VWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00223  182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSF 216
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-197 3.35e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 283.70  E-value: 3.35e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00103   24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00103  104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00103  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-197 1.00e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 282.49  E-value: 1.00e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00037   24 AWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00037  104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00037  184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTF 219
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-197 1.66e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 281.81  E-value: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00183   24 AWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00183  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00183  184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-197 1.77e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 281.83  E-value: 1.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00077   24 AWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00077  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00077  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-197 6.74e-91

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 274.86  E-value: 6.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00007   21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00007  101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00007  181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSF 216
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-197 6.40e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 256.92  E-value: 6.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   1 SAWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSF 80
Cdd:MTH00079   24 GLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  81 WLLPPSLTLLLMSGMVESGVGTGWTVYPPLAgAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMP 160
Cdd:MTH00079  104 WLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMS 182

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1769324458 161 LFVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00079  183 LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSF 219
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-197 9.93e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 254.37  E-value: 9.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00184   26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00184  106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00184  186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTF 221
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-197 1.30e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 253.98  E-value: 1.30e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00182   26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00182  106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00182  186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTF 221
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-197 2.32e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 232.98  E-value: 2.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   2 AWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFW 81
Cdd:MTH00026   25 ALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  82 LLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPL 161
Cdd:MTH00026  105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1769324458 162 FVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00026  185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTF 220
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-197 2.25e-65

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: 207.77  E-value: 2.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   1 SAWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGGPDMAFPRMNNMSF 80
Cdd:cd00919    12 AFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  81 WLLPPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMP 160
Cdd:cd00919    91 WLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMP 170

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1769324458 161 LFVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:cd00919   171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSF 207
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-197 2.76e-55

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 183.02  E-value: 2.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   4 AGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWLL 83
Cdd:COG0843    29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  84 PPSLTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFV 163
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1769324458 164 WAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHF 221
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-197 4.33e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 161.00  E-value: 4.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   3 WAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGGPDMAFPRMNNMSFWL 82
Cdd:MTH00048   26 WSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  83 LPPSLTLLLMSgmVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMdQMPLF 162
Cdd:MTH00048  106 LVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSII 182

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1769324458 163 VWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:MTH00048  183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAF 217
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-197 1.15e-44

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: 154.66  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   8 GTSLSLIIRAELGQP-GTLIGNDQiYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPS 86
Cdd:cd01662    25 GGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  87 LTLLLMSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAV 166
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1769324458 167 FITAILLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDRYFGTHF 213
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-198 2.29e-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: 128.46  E-value: 2.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458   1 SAWAGMVGTSLSLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGGPDMAFPRMNNMSF 80
Cdd:pfam00115  10 ALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  81 WLLPPSLTLLLMSGMvesGVGTGWTVYPPLAGaiahagasVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMdQMP 160
Cdd:pfam00115  89 WLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1769324458 161 LFVWAVFITAILLLLSLPVLAGAITMLLTDRNLNTSFG 198
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGG 194
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 32-197 5.49e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 121.20  E-value: 5.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  32 YNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLA 111
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458 112 GAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAVFITAILLLLSLPVLAGAITMLLTDR 191
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                  ....*.
gi 1769324458 192 NLNTSF 197
Cdd:PRK15017  258 YLGTHF 263
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-197 2.18e-30

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 116.88  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  12 SLIIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGGPDMAFPRMNNMSFWLLPPSLTLLL 91
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769324458  92 MSGMVESGVGTGWTVYPPLAGAIAHAGASVDLGIFSLHLAGVSSILGAVNFMTTIINMRSFGMTMDQMPLFVWAVFITAI 171
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180
                  ....*....|....*....|....*.
gi 1769324458 172 LLLLSLPVLAGAITMLLTDRNLNTSF 197
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAF 256
 
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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