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Conserved domains on  [gi|339635594|gb|AEJ84497|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Mugil liza]

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 ...
 1-202 1.13e-132

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 MTH00183:

Pssm-ID: 469701  Cd Length: 516  Bit Score: 381.96  E-value: 1.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00183  33 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00183 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00183 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
 
Name Accession Description Interval E-value
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-202 1.13e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 381.96  E-value: 1.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00183  33 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00183 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00183 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-202 1.65e-119

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: 347.55  E-value: 1.65e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:cd01663   24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:cd01663  104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:cd01663  184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-202 6.36e-67

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 213.84  E-value: 6.36e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:COG0843   36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:COG0843  115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:COG0843  195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-202 1.58e-41

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: 145.02  E-value: 1.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594    1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   81 LASSGveaGAGTGWTVYPPLasnlahagASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQyQTPLFVWAVLITA 160
Cdd:pfam00115  99 LASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 339635594  161 VLLLLSLPVLAAGITMLLTDRNLNtsffdpAGGGDPILYQHL 202
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-202 1.05e-34

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: 129.20  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594    2 SLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 81
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   82 ASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITAV 161
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 339635594  162 LLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANL 271
 
Name Accession Description Interval E-value
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-202 1.13e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 381.96  E-value: 1.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00183  33 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00183 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00183 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-202 8.90e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 379.67  E-value: 8.90e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00077  33 LSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00077 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00077 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHL 234
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-202 2.64e-131

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 378.46  E-value: 2.64e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00103  33 LSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00103 113 LASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00103 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-202 1.01e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 371.51  E-value: 1.01e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00153  31 LSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00153 111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00153 191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-202 3.62e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 362.87  E-value: 3.62e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00116  33 LSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00116 113 LASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00116 193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-202 4.43e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 354.75  E-value: 4.43e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00167  33 LSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00167 113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTT 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00167 193 ILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-202 1.65e-119

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: 347.55  E-value: 1.65e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:cd01663   24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:cd01663  104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:cd01663  184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-202 8.39e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 328.61  E-value: 8.39e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00142  31 LSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00142 111 LSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITA 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00142 191 ILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 232
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-202 5.32e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 326.55  E-value: 5.32e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00223  30 LSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00223 110 LSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTA 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00223 190 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 231
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-202 4.12e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 296.36  E-value: 4.12e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00037  33 MSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00037 113 LASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00037 193 FLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHL 234
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-202 7.18e-98

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 292.96  E-value: 7.18e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00007  30 MSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00007 110 VSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITV 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00007 190 VLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 231
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-202 2.22e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 279.40  E-value: 2.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00182  35 FSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00182 115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITA 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00182 195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHL 236
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-202 1.21e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 277.48  E-value: 1.21e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00184  35 FSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00184 115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTT 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00184 195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 236
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-202 1.63e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 263.85  E-value: 1.63e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00079  34 LSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLaSNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00079 114 LDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTV 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00079 193 FLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHL 234
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-202 9.95e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 257.25  E-value: 9.95e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00026  34 FSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:MTH00026 114 LGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITA 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00026 194 ILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 235
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-202 3.10e-75

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: 233.58  E-value: 3.10e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:cd00919   22 LALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:cd00919  101 LSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTA 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:cd00919  181 ILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHL 222
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-202 6.36e-67

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 213.84  E-value: 6.36e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:COG0843   36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:COG0843  115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:COG0843  195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-202 5.98e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 189.89  E-value: 5.98e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:MTH00048  34 LSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASsgVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSqYQTPLFVWAVLITA 160
Cdd:MTH00048 114 LLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTS 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:MTH00048 191 ILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHM 232
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-202 3.56e-56

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: 185.09  E-value: 3.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:cd01662   28 DALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  81 LASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITA 160
Cdd:cd01662  107 NASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTS 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 339635594 161 VLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:cd01662  187 ILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHL 228
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-202 1.58e-41

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: 145.02  E-value: 1.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594    1 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 80
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   81 LASSGveaGAGTGWTVYPPLasnlahagASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQyQTPLFVWAVLITA 160
Cdd:pfam00115  99 LASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 339635594  161 VLLLLSLPVLAAGITMLLTDRNLNtsffdpAGGGDPILYQHL 202
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 22-202 1.59e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 131.60  E-value: 1.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594  22 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLA 101
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594 102 SNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDR 181
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 339635594 182 NLNTSFFDPAGGGDPILYQHL 202
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-202 1.05e-34

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: 129.20  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594    2 SLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLL 81
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339635594   82 ASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWAVLITAV 161
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 339635594  162 LLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHL 202
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANL 271
 
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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