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Conserved domains on  [gi|1829740870|gb|QIX11871|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Formica sp. FCUN49]

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 ...
 1-200 2.18e-111

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: 327.60  E-value: 2.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00153   21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:MTH00153  101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00153  181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-200 2.18e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 327.60  E-value: 2.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00153   21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:MTH00153  101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00153  181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-200 2.03e-104

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: 309.03  E-value: 2.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:cd01663    14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:cd01663    94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:cd01663   174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 2.52e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 180.71  E-value: 2.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLEL-GSSNSLINNDQiYNSLVTNHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMS 79
Cdd:COG0843    26 AFVFLLIGGLLALLMRLQLaGPGLGLLSPET-YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  80 FWLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKI 159
Cdd:COG0843   104 FWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRM 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1829740870 160 PLLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:COG0843   184 PLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-200 4.51e-36

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: 130.39  E-value: 4.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:pfam00115  10 ALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSnfiNDGTGTGWTIYPPLasnifhngPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIdKIP 160
Cdd:pfam00115  89 WLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 8-198 9.49e-29

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 112.25  E-value: 9.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   8 GSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPSI 87
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  88 TLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLLVWSIL 167
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1829740870 168 ITAILLLLSLPVLAGAITMLLTDRNLNTSFF 198
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-200 2.18e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 327.60  E-value: 2.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00153   21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:MTH00153  101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00153  181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-200 2.03e-104

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: 309.03  E-value: 2.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:cd01663    14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:cd01663    94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:cd01663   174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-200 9.56e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 295.05  E-value: 9.56e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   2 IWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00167   24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  82 LLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPL 161
Cdd:MTH00167  104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1829740870 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00167  184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDP 222
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 3-200 1.50e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 286.99  E-value: 1.50e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   3 WAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00116   25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  83 LPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLL 162
Cdd:MTH00116  105 LPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLF 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1829740870 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00116  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-200 6.09e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 280.33  E-value: 6.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00223   20 GMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:MTH00223  100 WLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLP 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00223  180 LFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 219
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-200 1.30e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 276.99  E-value: 1.30e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   2 IWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00142   22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  82 LLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPL 161
Cdd:MTH00142  102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1829740870 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00142  182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDP 220
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-200 2.51e-86

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 263.30  E-value: 2.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   2 IWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00007   21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  82 LLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPL 161
Cdd:MTH00007  101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1829740870 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00007  181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDP 219
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 3-200 3.76e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 257.93  E-value: 3.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   3 WAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00183   25 WAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  83 LPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLL 162
Cdd:MTH00183  105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1829740870 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00183  185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 3-200 1.13e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 256.79  E-value: 1.13e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   3 WAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00077   25 WAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  83 LPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLL 162
Cdd:MTH00077  105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1829740870 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00077  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 3-200 1.20e-82

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 254.04  E-value: 1.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   3 WAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00103   25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  83 LPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLL 162
Cdd:MTH00103  105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1829740870 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00103  185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 3-200 1.30e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 253.98  E-value: 1.30e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   3 WAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00037   25 WAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  83 LPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLL 162
Cdd:MTH00037  105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1829740870 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00037  185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDP 222
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-200 7.49e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 244.35  E-value: 7.49e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   2 IWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00184   26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  82 LLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPL 161
Cdd:MTH00184  106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1829740870 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00184  186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-200 2.57e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 237.80  E-value: 2.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   2 IWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00182   26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  82 LLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPL 161
Cdd:MTH00182  106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1829740870 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00182  186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-200 6.83e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 236.50  E-value: 6.83e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00079   24 GLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLaSNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:MTH00079  104 WLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMS 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00079  183 LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDP 222
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 4-200 3.12e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 219.88  E-value: 3.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   4 AGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWLL 83
Cdd:MTH00026   27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  84 PPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLLV 163
Cdd:MTH00026  107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1829740870 164 WSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00026  187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDP 223
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-200 4.14e-66

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 209.69  E-value: 4.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPlMLGSPDMAYPRMNNMSF 80
Cdd:cd00919    12 AFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIP 160
Cdd:cd00919    91 WLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMP 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:cd00919   171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDP 210
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-200 2.36e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 182.96  E-value: 2.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   2 IWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00048   25 VWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  82 LLPPSITLLLLSNFIndGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIdKIPL 161
Cdd:MTH00048  105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSI 181

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1829740870 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:MTH00048  182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDP 220
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 2.52e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 180.71  E-value: 2.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLEL-GSSNSLINNDQiYNSLVTNHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMS 79
Cdd:COG0843    26 AFVFLLIGGLLALLMRLQLaGPGLGLLSPET-YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  80 FWLLPPSITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKI 159
Cdd:COG0843   104 FWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRM 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1829740870 160 PLLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:COG0843   184 PLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-200 2.10e-42

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 148.50  E-value: 2.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   7 IGSSMSMIIRLELGS-SNSLINNDQiYNSLVTNHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPP 85
Cdd:cd01662    24 RGGVDALLMRTQLALpGNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  86 SITLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLLVWS 165
Cdd:cd01662   102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1829740870 166 ILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:cd01662   182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTN 216
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-200 4.51e-36

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: 130.39  E-value: 4.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   1 AIWAGMIGSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:pfam00115  10 ALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  81 WLLPPSITLLLLSnfiNDGTGTGWTIYPPLasnifhngPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIdKIP 160
Cdd:pfam00115  89 WLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1829740870 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 8-198 9.49e-29

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 112.25  E-value: 9.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870   8 GSSMSMIIRLELGSSNSLINNDQIYNSLVTNHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPSI 87
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  88 TLLLLSNFINDGTGTGWTIYPPLASNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLLVWSIL 167
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1829740870 168 ITAILLLLSLPVLAGAITMLLTDRNLNTSFF 198
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 32-198 5.75e-28

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 110.03  E-value: 5.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870  32 YNSLVTNHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPSITLLLLSNFINDGTGTGWTIYPPLA 111
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829740870 112 SNIFHNGPSVDLTIFSLHIAGMSSILGAINFISTILNMHHKNFSIDKIPLLVWSILITAILLLLSLPVLAGAITMLLTDR 191
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                  ....*..
gi 1829740870 192 NLNTSFF 198
Cdd:PRK15017  258 YLGTHFF 264
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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