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Conserved domains on  [gi|1877817264|gb|QLL26110|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Actinopterygii sp. IOU50]

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 ...
 1-198 2.63e-133

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: 383.06  E-value: 2.63e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00153   34 LIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00153  114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00153  194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-198 2.63e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 383.06  E-value: 2.63e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00153   34 LIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00153  114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00153  194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-198 4.43e-124

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: 358.72  E-value: 4.43e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:cd01663    27 LIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:cd01663   107 ALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLL 186

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:cd01663   187 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 224
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-198 2.46e-67

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 214.61  E-value: 2.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:COG0843    39 LMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:COG0843   118 LFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILI 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:COG0843   198 LLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-198 5.61e-43

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: 148.88  E-value: 5.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:pfam00115  23 LIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGveaGAGTGWTVYPPLAAnlahagasVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQyQTPLFVWAVLITAVLL 160
Cdd:pfam00115 102 FG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILI 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQH 198
Cdd:pfam00115 170 LLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-196 1.11e-35

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: 131.90  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:TIGR02882  74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLII 232

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 196
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-198 2.63e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 383.06  E-value: 2.63e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00153   34 LIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00153  114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00153  194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-198 2.13e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 368.27  E-value: 2.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00116   36 LIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00116  116 STVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00116  196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-198 2.87e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 362.84  E-value: 2.87e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00167   36 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00167  116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00167  196 LLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-198 4.43e-124

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: 358.72  E-value: 4.43e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:cd01663    27 LIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:cd01663   107 ALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLL 186

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:cd01663   187 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 224
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-198 1.35e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 343.44  E-value: 1.35e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00183   36 LIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00183  116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00183  196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-198 2.39e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 342.69  E-value: 2.39e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00077   36 LIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00077  116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00077  196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQH 233
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-198 1.69e-116

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 340.71  E-value: 1.69e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00103   36 LIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00103  116 SMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00103  196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-198 1.37e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 335.41  E-value: 1.37e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00223   33 LIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00223  113 SAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLL 192

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00223  193 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 230
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-198 2.09e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 335.15  E-value: 2.09e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00142   34 LIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00142  114 AAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILL 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00142  194 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 231
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-198 2.59e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 309.45  E-value: 2.59e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00037   36 IIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00037  116 AGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00037  196 LLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQH 233
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-198 7.01e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 297.97  E-value: 7.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00007   33 LIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00007  113 AAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLL 192

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00007  193 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 230
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-198 2.33e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 289.42  E-value: 2.33e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00184   38 LIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00184  118 AFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLL 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00184  198 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-198 5.44e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 288.64  E-value: 5.44e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00182   38 LIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00182  118 AFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLL 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00182  198 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQH 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-198 5.17e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 268.42  E-value: 5.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00026   37 LIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00026  117 SLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILL 196

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00026  197 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH 234
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-198 8.85e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 261.54  E-value: 8.85e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00079   37 IIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLaANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00079  117 CFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLL 195

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00079  196 VLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQH 233
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-198 4.54e-76

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: 235.50  E-value: 4.54e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:cd00919    25 LIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:cd00919   104 VLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILL 183

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:cd00919   184 LLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQH 221
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-198 2.46e-67

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 214.61  E-value: 2.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:COG0843    39 LMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:COG0843   118 LFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILI 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:COG0843   198 LLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-198 3.28e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 192.97  E-value: 3.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:MTH00048   37 LIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 sgVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAmLQYQTPLFVWAVLITAVLL 160
Cdd:MTH00048  117 --MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIILWSYLFTSILL 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:MTH00048  194 LLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQH 231
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-198 3.99e-55

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: 182.01  E-value: 3.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:cd01662    31 LMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNAS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:cd01662   110 LLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILI 189

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 198
Cdd:cd01662   190 LFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQH 227
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-198 5.61e-43

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: 148.88  E-value: 5.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:pfam00115  23 LIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGveaGAGTGWTVYPPLAAnlahagasVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQyQTPLFVWAVLITAVLL 160
Cdd:pfam00115 102 FG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILI 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQH 198
Cdd:pfam00115 170 LLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 19-196 1.47e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 134.29  E-value: 1.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  19 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLASSGVEAGAGTGWTVYPPLA 98
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  99 ANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDR 178
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170
                  ....*....|....*...
gi 1877817264 179 NLNTTFFDPAGGGDPILY 196
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMY 275
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-196 1.11e-35

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: 131.90  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264   1 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFVLLLAS 80
Cdd:TIGR02882  74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877817264  81 SGVEAGAGTGWTVYPPLAANLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMTSPAMLQYQTPLFVWAVLITAVLL 160
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLII 232

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1877817264 161 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILY 196
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLW 268
 
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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