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Conserved domains on  [gi|1576836196|gb|QBF06813|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Telenomus sp. BIOUG21213-F08]

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 ...
 1-190 5.66e-93

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: 279.83  E-value: 5.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00153   18 FIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW- 156
Cdd:MTH00153   98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLd 177

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 157 --SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00153  178 rmPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNL 213
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-190 5.66e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 279.83  E-value: 5.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00153   18 FIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW- 156
Cdd:MTH00153   98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLd 177

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 157 --SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00153  178 rmPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNL 213
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 1.41e-88

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: 267.81  E-value: 1.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:cd01663    11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW- 156
Cdd:cd01663    91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLe 170

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 157 --SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:cd01663   171 kmPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNF 206
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-190 1.17e-42

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 149.51  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:COG0843    23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNWS 157
Cdd:COG0843   102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 158 ---LFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:COG0843   182 rmpLFTWAALVTSILILLAFPVLAAALLLLLLDRSL 217
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-190 1.29e-30

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: 115.36  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMlGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:pfam00115   7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSnifGMGTGTGWTIYPPLssqinPSIDLTIFSLHVAGISSILSSINFICTIFNM--SFATNNWSL 158
Cdd:pfam00115  86 LSFWLVVLGAVLLLAS---FGGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRraPGMTLRMPL 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1576836196 159 FSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSL 189
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 17-188 2.21e-24

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: 99.16  E-value: 2.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  17 MIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWIVPLMINAPDMAFPRLNNMSFWLLIPSLMLLIYS 96
Cdd:TIGR02882  74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  97 NIFGMGTGTGWTIYPPLSS---QINPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW---SLFSWSIFITTILL 170
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLmqmPMFTWTTLITTLII 232

                         170
                  ....*....|....*...
gi 1576836196 171 LLSLPVLAGGITMILSDR 188
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDR 250
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-190 5.66e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 279.83  E-value: 5.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00153   18 FIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW- 156
Cdd:MTH00153   98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLd 177

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 157 --SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00153  178 rmPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNL 213
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 1.41e-88

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: 267.81  E-value: 1.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:cd01663    11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW- 156
Cdd:cd01663    91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLe 170

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 157 --SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:cd01663   171 kmPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNF 206
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-190 3.92e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 259.99  E-value: 3.92e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00167   20 FIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATN 154
Cdd:MTH00167  100 MSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGSINFITTIINMkppGITQY 179

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00167  180 QTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNL 215
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-190 9.06e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 253.86  E-value: 9.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00116   20 LIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATN 154
Cdd:MTH00116  100 MSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGAINFITTCINMkppAMSQY 179

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00116  180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNL 215
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-189 1.51e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 242.96  E-value: 1.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00223   17 LIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATN 154
Cdd:MTH00223   97 MSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLahaGPSVDLAIFSLHLAGVSSILGAINFITTIINMrspGMQLE 176

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRN 189
Cdd:MTH00223  177 RLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRN 211
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-190 1.13e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 238.08  E-value: 1.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00142   18 FLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATN 154
Cdd:MTH00142   98 MSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLahsGGSVDLAIFSLHLAGVSSILGAINFITTVINMragGMKFE 177

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00142  178 RVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNF 213
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 3-190 4.52e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 223.65  E-value: 4.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   3 FGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNNMS 82
Cdd:MTH00183   22 FGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  83 FWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATNNW 156
Cdd:MTH00183  102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTIINMkppAISQYQT 181

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1576836196 157 SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00183  182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNL 215
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 3-190 4.69e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 223.66  E-value: 4.69e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   3 FGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNNMS 82
Cdd:MTH00077   22 FGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  83 FWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATNNW 156
Cdd:MTH00077  102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINFITTSINMkppSMSQYQT 181

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1576836196 157 SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00077  182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNL 215
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-190 3.08e-70

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 221.29  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00103   20 LLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLS---SQINPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATN 154
Cdd:MTH00103  100 MSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMkppAMSQY 179

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00103  180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNL 215
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-190 3.59e-70

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 221.31  E-value: 3.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00007   17 FILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFA---TN 154
Cdd:MTH00007   97 MSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLahaGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKglrLE 176

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00007  177 RIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNL 212
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-190 1.72e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 219.70  E-value: 1.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00037   20 LIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATN 154
Cdd:MTH00037  100 MSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIahaGGSVDLAIFSLHLAGASSILASINFITTIINMrtpGMTFD 179

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00037  180 RLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNI 215
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-190 4.37e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 210.69  E-value: 4.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00079   21 FLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQINP--SIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW-- 156
Cdd:MTH00079  101 LSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPgsSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLeh 180

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1576836196 157 -SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00079  181 mSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNL 215
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-190 1.64e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 206.60  E-value: 1.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00184   22 LLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSS---QINPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNWS 157
Cdd:MTH00184  102 ISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiqaHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMD 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 158 ---LFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00184  182 rmpLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNF 217
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 3-189 9.11e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 205.06  E-value: 9.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   3 FGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNNMS 82
Cdd:MTH00182   24 FGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  83 FWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSS---QINPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATNNW 156
Cdd:MTH00182  104 FWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSiqaHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMrapGVTFNRL 183

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1576836196 157 SLFSWSIFITTILLLLSLPVLAGGITMILSDRN 189
Cdd:MTH00182  184 PLFVWSILITAFLLLLSLPVLAGAITMLLTDRN 216
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-190 1.22e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 184.06  E-value: 1.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   3 FGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNNMS 82
Cdd:MTH00026   23 FGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNIS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  83 FWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSS---QINPSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATNNW 156
Cdd:MTH00026  103 FWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASiqaHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMrtpGMTMSRI 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1576836196 157 SLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:MTH00026  183 PLFVWSVFITAILLLLSLPVLAGAITMLLTDRNF 216
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-190 5.72e-52

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: 172.72  E-value: 5.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPlMINAPDMAFPRLNN 80
Cdd:cd00919     9 LIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMS---FATN 154
Cdd:cd00919    88 LSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSyssGVGVDLAILGLHLAGVSSILGAINFITTILNMRapgMTLD 167

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 155 NWSLFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:cd00919   168 KMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNF 203
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-189 4.36e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 155.61  E-value: 4.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:MTH00048   21 TLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFgmGTGTGWTIYPPLSSQINPS---IDLTIFSLHVAGISSILSSINFICTIfnMSFATNNW- 156
Cdd:MTH00048  101 LSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSswgVDFLMFSLHLAGVSSLFGSINFICTI--YSAFMTNVf 176

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 157 ---SLFSWSIFITTILLLLSLPVLAGGITMILSDRN 189
Cdd:MTH00048  177 srtSIILWSYLFTSILLLLSLPVLAAAITMLLFDRN 212
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-190 1.17e-42

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 149.51  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:COG0843    23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLSSQI---NPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNWS 157
Cdd:COG0843   102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1576836196 158 ---LFSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:COG0843   182 rmpLFTWAALVTSILILLAFPVLAAALLLLLLDRSL 217
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 10-188 1.02e-33

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: 124.62  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  10 LGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWIVPLMINAPDMAFPRLNNMSFWLLIPS 89
Cdd:cd01662    24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  90 LMLLIYSNIFGMGTGTGWTIYPPLSSQIN---PSIDLTIFSLHVAGISSILSSINFICTIFNM---SFATNNWSLFSWSI 163
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYspgVGVDYWILGLQFSGIGTLLGAINFIVTILKMrapGMTLMRMPIFTWTT 182

                         170       180
                  ....*....|....*....|....*
gi 1576836196 164 FITTILLLLSLPVLAGGITMILSDR 188
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDR 207
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-190 1.29e-30

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: 115.36  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196   1 FFFGMW*GMLGS*MSSMIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMlGGFGNWIVPLMINAPDMAFPRLNN 80
Cdd:pfam00115   7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAFPRLNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  81 MSFWLLIPSLMLLIYSnifGMGTGTGWTIYPPLssqinPSIDLTIFSLHVAGISSILSSINFICTIFNM--SFATNNWSL 158
Cdd:pfam00115  86 LSFWLVVLGAVLLLAS---FGGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRraPGMTLRMPL 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1576836196 159 FSWSIFITTILLLLSLPVLAGGITMILSDRNL 190
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSL 189
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 17-188 2.21e-24

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: 99.16  E-value: 2.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  17 MIRMELSIPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWIVPLMINAPDMAFPRLNNMSFWLLIPSLMLLIYS 96
Cdd:TIGR02882  74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  97 NIFGMGTGTGWTIYPPLSS---QINPSIDLTIFSLHVAGISSILSSINFICTIFNMSFATNNW---SLFSWSIFITTILL 170
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLmqmPMFTWTTLITTLII 232

                         170
                  ....*....|....*...
gi 1576836196 171 LLSLPVLAGGITMILSDR 188
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDR 250
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 35-190 1.02e-20

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 88.84  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196  35 YNSIVTSHAFIMIFFMVMPIMLGgFGNWIVPLMINAPDMAFPRLNNMSFWLLIPSLMLLIYSNIFGMGTGTGWTIYPPLS 114
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576836196 115 S-QINP--SIDLTIFSLHVAGISSILSSINFICTIFNM---SFATNNWSLFSWSIFITTILLLLSLPVLAGGITMILSDR 188
Cdd:PRK15017  178 GiEYSPgvGVDYWIWSLQLSGIGTTLTGINFFVTILKMrapGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                  ..
gi 1576836196 189 NL 190
Cdd:PRK15017  258 YL 259
 
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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