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Conserved domains on  [gi|1139421365|gb|APZ76997|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Apoidea sp. GE_VE84]

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 ...
 1-201 4.57e-118

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: 344.54  E-value: 4.57e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00153   37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00153  197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-201 4.57e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 344.54  E-value: 4.57e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00153   37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00153  197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-201 2.40e-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: 329.06  E-value: 2.40e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:cd01663    30 LELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:cd01663   190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 9.65e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 203.05  E-value: 9.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFmIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:COG0843    42 LQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:COG0843   121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:COG0843   201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-201 9.12e-37

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: 132.31  E-value: 9.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFmIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSsil 80
Cdd:pfam00115  26 LQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS--- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLssimyhssISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYdQIPLFPWSVKITAILLLLA 160
Cdd:pfam00115 102 FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTsffdpsGGGDPILYQHLFWFFG 201
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFG 207
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-201 7.67e-36

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: 132.29  E-value: 7.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:TIGR02882  77 AQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVI 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:TIGR02882 156 GGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFA 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:TIGR02882 236 FPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-201 4.57e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 344.54  E-value: 4.57e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00153   37 AELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00153  197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-201 2.40e-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: 329.06  E-value: 2.40e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:cd01663    30 LELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:cd01663   190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-201 4.56e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 311.23  E-value: 4.56e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00167   39 AELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00167  119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLS 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00167  199 LPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-201 4.12e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 301.13  E-value: 4.12e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00223   36 AELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00223  116 ESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLS 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00223  196 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-201 5.63e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 298.54  E-value: 5.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00116   39 AELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00116  119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00116  199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-201 1.71e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 289.32  E-value: 1.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   2 ELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSILS 81
Cdd:MTH00142   38 ELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  82 SGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLAL 161
Cdd:MTH00142  118 SGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSL 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1139421365 162 PVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00142  198 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-201 6.28e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 272.58  E-value: 6.28e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   2 ELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSILS 81
Cdd:MTH00077   40 ELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  82 SGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLAL 161
Cdd:MTH00077  120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSL 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1139421365 162 PVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00077  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-201 6.63e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 272.57  E-value: 6.63e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   2 ELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSILS 81
Cdd:MTH00183   40 ELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  82 SGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLAL 161
Cdd:MTH00183  120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSL 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1139421365 162 PVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00183  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-201 7.07e-89

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 269.83  E-value: 7.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00103   39 AELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00103  119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00103  199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-201 1.15e-86

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 264.46  E-value: 1.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00007   36 IELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00007  116 EKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLS 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00007  196 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-201 1.78e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 261.30  E-value: 1.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00037   39 TELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00037  119 ESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLS 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00037  199 LPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-201 2.97e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 255.52  E-value: 2.97e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00184   41 LELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00184  121 EQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLS 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00184  201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-201 3.98e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 255.52  E-value: 3.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00182   41 LELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00182  121 EQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLS 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00182  201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-201 5.07e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 252.29  E-value: 5.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00079   40 LELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSiMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00079  120 DMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLS 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00079  199 LPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-201 2.09e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 241.07  E-value: 2.09e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:MTH00026   40 LELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:MTH00026  120 EQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLS 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00026  200 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-201 1.08e-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: 224.33  E-value: 1.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:cd00919    28 LELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:cd00919   107 GGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLA 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:cd00919   187 LPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 9.65e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 203.05  E-value: 9.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFmIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:COG0843    42 LQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:COG0843   121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:COG0843   201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 15-201 1.70e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 191.43  E-value: 1.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  15 IYNTIITSHAFIMIFFMVMPFMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSsiLSSGSGTGWTVYPPL 94
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  95 SSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYdQIPLFPWSVKITAILLLLALPVLAGAITMLLTD 174
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                         170       180
                  ....*....|....*....|....*..
gi 1139421365 175 RNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:MTH00048  211 RNFGSAFFDPLGGGDPVLFQHMFWFFG 237
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-201 5.62e-53

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: 176.62  E-value: 5.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   2 ELSTPGN-WINNDQiYNTIITSHAFIMIFFMVMPFMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:cd01662    35 QLALPGNdFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:cd01662   113 GGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:cd01662   193 FPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-201 9.12e-37

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: 132.31  E-value: 9.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFmIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSsil 80
Cdd:pfam00115  26 LQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS--- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLssimyhssISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYdQIPLFPWSVKITAILLLLA 160
Cdd:pfam00115 102 FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTsffdpsGGGDPILYQHLFWFFG 201
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFG 207
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-201 7.67e-36

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: 132.29  E-value: 7.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365   1 MELSTPGNWINNDQIYNTIITSHAFIMIFFMVMPFMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSIL 80
Cdd:TIGR02882  77 AQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVI 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  81 SSGSGTGWTVYPPLSSIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLA 160
Cdd:TIGR02882 156 GGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFA 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1139421365 161 LPVLAGAITMLLTDRNMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:TIGR02882 236 FPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 16-201 2.54e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 128.13  E-value: 2.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  16 YNTIITSHAFIMIFFMVMPFMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLIPSLFMLLMSSILSSGSGTGWTVYPPLS 95
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139421365  96 SIMYHSSISVDCTIFSLHIAGISSIMGAINFIVSILLMKNISINYDQIPLFPWSVKITAILLLLALPVLAGAITMLLTDR 175
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|....*.
gi 1139421365 176 NMNTSFFDPSGGGDPILYQHLFWFFG 201
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWG 283
 
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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