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Conserved domains on  [gi|300226172|gb|ADJ84679|]
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cytochrome oxidase subunit 1, partial [Mytilus edulis]

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 ...
 1-217 1.73e-117

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 MTH00223:

Pssm-ID: 469701  Cd Length: 512  Bit Score: 343.88  E-value: 1.73e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00223  17 LIFGMWSGLVGTSLSLLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00223  96 NMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00223 176 ERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-217 1.73e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 343.88  E-value: 1.73e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00223  17 LIFGMWSGLVGTSLSLLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00223  96 NMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00223 176 ERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 1.60e-112

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: 330.21  E-value: 1.60e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLkSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:cd01663   11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLG-NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:cd01663   90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:cd01663  170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 6.72e-61

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 198.81  E-value: 6.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMN 80
Cdd:COG0843   23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE-TYNQLFTMHGTIMIFFFATPFLAG-FGNYLVPLQIGARDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:COG0843  101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:COG0843  181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 6.96e-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: 130.77  E-value: 6.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172    1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMN 80
Cdd:pfam00115   7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL-TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   81 NLSYWLSPNALYLLMLSFStdkGVGAGWTIYPPLsvypyhsgPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMkG 160
Cdd:pfam00115  85 ALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-T 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172  161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNttffdpAGGGDPVLFQHLF 217
Cdd:pfam00115 153 LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-217 1.73e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 343.88  E-value: 1.73e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00223  17 LIFGMWSGLVGTSLSLLIRAELGQPGA-LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00223  96 NMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00223 176 ERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-217 1.60e-112

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: 330.21  E-value: 1.60e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLkSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:cd01663   11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLG-NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:cd01663   90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:cd01663  170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 4-217 8.70e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 303.71  E-value: 8.70e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00153  21 GAWSGMVGTSLSLLIRAELGQPGS-LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 4-217 3.06e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 279.28  E-value: 3.06e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00116  23 GAWAGMVGTALSLLIRAELGQPGT-LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00116 102 FWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQT 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00116 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 4-217 5.87e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 275.79  E-value: 5.87e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00167  23 GAWAGMVGTALSLLIRAELSQPGSL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00167 102 FWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQT 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00167 182 PLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 4-217 2.53e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 266.59  E-value: 2.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00142  21 GAWAGMVGTGLSLLIRAELGQPGS-LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00142 100 FWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERV 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00142 180 PLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 4-217 3.29e-85

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 261.37  E-value: 3.29e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00007  20 GVWGGLLGTSMSLLIRIELGQPGA-FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00007  99 FWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERI 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00007 179 PLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-217 4.03e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 253.06  E-value: 4.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   3 SGVWGGLFGASLSLMIRMQLGHPGaVFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNL 82
Cdd:MTH00079  23 FGLWSGMVGTSLSLIIRLELSKPG-LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  83 SYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPyHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGER 162
Cdd:MTH00079 102 SFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEH 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300226172 163 AELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00079 181 MSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-217 4.14e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 250.63  E-value: 4.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00077  20 LVFGAWAGMVGTALSLLIRAELSQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00077  99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00077 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 2.45e-79

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 246.33  E-value: 2.45e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00103  20 LLFGAWAGMVGTALSLLIRAELGQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00103  99 NMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00103 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 1.04e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 244.45  E-value: 1.04e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00183  20 LVFGAWAGMVGTALSLLIRAELSQPGAL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00183  99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQ 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00183 179 YQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 4-217 6.52e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 242.43  E-value: 6.52e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAvFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00037  23 GAWAGMVGTAMSVIIRTELAQPGS-LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00037 102 FWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00037 182 PLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 4-217 1.10e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 239.72  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00182  25 GAGAGMIGTAFSMLIRLELSAPGAM-LGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNIS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERA 163
Cdd:MTH00182 104 FWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00182 184 PLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-217 1.26e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 239.34  E-value: 1.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00184  22 LLFGAFAGMIGTAFSMLIRLELSAPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00184 101 NISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITM 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00184 181 DRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-217 8.10e-71

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: 222.79  E-value: 8.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLvGGKDMIYPRMN 80
Cdd:cd00919    9 LIFAFVALLLGGLLALLIRLELATPGSLFLDPQ-LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFPRLN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:cd00919   87 NLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTL 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:cd00919  167 DKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-217 2.76e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 220.66  E-value: 2.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVfLKSDWFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMN 80
Cdd:MTH00026  21 LVFGALSGAIGTAFSMLIRLELSSPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:MTH00026 100 NISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTM 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00026 180 SRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 4-217 2.90e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 206.84  E-value: 2.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   4 GVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGAFGNWLIPLLVGGKDMIYPRMNNLS 83
Cdd:MTH00048  24 GVWSGFVGLSLSLLIRLNFLDPYYNVISLD-VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  84 YWLSPNALYLLMLSFStdKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGeRA 163
Cdd:MTH00048 103 AWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RT 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300226172 164 ELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:MTH00048 180 SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-217 6.72e-61

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 198.81  E-value: 6.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMN 80
Cdd:COG0843   23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE-TYNQLFTMHGTIMIFFFATPFLAG-FGNYLVPLQIGARDMAFPRLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  81 NLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKG 160
Cdd:COG0843  101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172 161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:COG0843  181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 9-217 2.68e-48

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: 165.06  E-value: 2.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   9 LFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMNNLSYWLSP 88
Cdd:cd01662   23 LRGGVDALLMRTQLALPGNDFLSPE-HYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  89 NALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERAELYVL 168
Cdd:cd01662  101 FGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTW 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 300226172 169 SISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLF 217
Cdd:cd01662  181 TTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-217 6.96e-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: 130.77  E-value: 6.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172    1 LYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDwFYNVVVTTHALMMIFFAVMPILIGaFGNWLIPLLVGGKDMIYPRMN 80
Cdd:pfam00115   7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL-TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   81 NLSYWLSPNALYLLMLSFStdkGVGAGWTIYPPLsvypyhsgPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMkG 160
Cdd:pfam00115  85 ALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-T 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300226172  161 ERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNttffdpAGGGDPVLFQHLF 217
Cdd:pfam00115 153 LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-216 1.20e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 103.86  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172   9 LFGASLSLMIRMQ--LGHPGAVFLKSDWFYNVVVTTHALMMIFFAVMPILIGAFgNWLIPLLVGGKDMIYPRMNNLSYWL 86
Cdd:PRK15017  70 LRGFADAIMMRSQqaLASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLM-NLVVPLQIGARDVAFPFLNNLSFWF 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300226172  87 SPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERAELY 166
Cdd:PRK15017 149 TVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVF 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300226172 167 VLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHL 216
Cdd:PRK15017 229 TWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278
 
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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