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Conserved domains on  [gi|50659940|gb|AAT80674|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Varecia variegata]

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 ...
 1-181 1.49e-127

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 MTH00116:

Pssm-ID: 469701  Cd Length: 515  Bit Score: 367.88  E-value: 1.49e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00116  44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00116 124 TGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00116 204 AGITMLLTDRNLNTTFFDPAG 224
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-181 1.49e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 367.88  E-value: 1.49e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00116  44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00116 124 TGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00116 204 AGITMLLTDRNLNTTFFDPAG 224
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-181 1.58e-100

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: 298.24  E-value: 1.58e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:cd01663  35 PGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAG 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:cd01663 115 TGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLA 194

                       170       180
                ....*....|....*....|.
gi 50659940 161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:cd01663 195 GAITMLLTDRNFNTSFFDPAG 215
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-181 4.86e-52

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 173.77  E-value: 4.86e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:COG0843  47 PGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAAD 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:COG0843 126 VGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLA 205

                       170       180
                ....*....|....*....|.
gi 50659940 161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:COG0843 206 AALLLLLLDRSLGTHFFDPAG 226
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-180 7.13e-33

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: 121.14  E-value: 7.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940     1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMveaGAG 80
Cdd:pfam00115  31 PGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GAT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    81 TGWTVYPPLAGnlahagasVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQyQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:pfam00115 107 TGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLA 177

                         170       180
                  ....*....|....*....|
gi 50659940   161 AGITMLLTDRNLNTTFFDPA 180
Cdd:pfam00115 178 AALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 7-180 4.79e-30

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: 114.95  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940     7 DDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVY 86
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    87 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITML 166
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170
                  ....*....|....
gi 50659940   167 LTDRNLNTTFFDPA 180
Cdd:TIGR02882 247 TTDRIFDTAFFTVA 260
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-181 1.49e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 367.88  E-value: 1.49e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00116  44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00116 124 TGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00116 204 AGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-181 9.99e-117

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 340.32  E-value: 9.99e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00103  44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00103 124 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00103 204 AGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-181 1.06e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 335.37  E-value: 1.06e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00077  44 PGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00077 124 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00077 204 AGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-181 1.10e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 335.35  E-value: 1.10e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00183  44 PGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00183 124 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00183 204 AGITMLLTDRNLNTTFFDPAG 224
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-181 1.75e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 319.12  E-value: 1.75e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00153  42 PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00153 122 TGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLA 201

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00153 202 GAITMLLTDRNLNTSFFDPAG 222
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-181 3.57e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 305.83  E-value: 3.57e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00167  44 PGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00167 124 TGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00167 204 AAITMLLTDRNLNTTFFDPAG 224
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-181 1.58e-100

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: 298.24  E-value: 1.58e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:cd01663  35 PGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAG 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:cd01663 115 TGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLA 194

                       170       180
                ....*....|....*....|.
gi 50659940 161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:cd01663 195 GAITMLLTDRNFNTSFFDPAG 215
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-181 1.21e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 283.92  E-value: 1.21e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00142  42 PGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00142 122 TGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLA 201

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00142 202 GAITMLLTDRNFNTSFFDPAG 222
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-181 1.05e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 281.48  E-value: 1.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00223  41 PGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00223 121 TGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLA 200

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00223 201 GAITMLLTDRNFNTSFFDPAG 221
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-181 1.67e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 257.84  E-value: 1.67e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00037  44 PGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00037 124 TGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00037 204 GAITMLLTDRNINTTFFDPAG 224
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-181 1.14e-81

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 250.59  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00007  41 PGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00007 121 TGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLA 200

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00007 201 GAITMLLTDRNLNTSFFDPAG 221
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-181 2.38e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 245.12  E-value: 2.38e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00182  46 PGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00182 126 TGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLA 205

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00182 206 GAITMLLTDRNFNTTFFDPAG 226
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-181 4.34e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 241.65  E-value: 4.34e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00184  46 PGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00184 126 TGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLA 205

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00184 206 GAITMLLTDRNFNTTFFDPAG 226
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-181 1.46e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 227.59  E-value: 1.46e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00026  45 PGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00026 125 TGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLA 204

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00026 205 GAITMLLTDRNFNTTFFDPAG 225
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-181 5.61e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 225.33  E-value: 5.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:MTH00079  45 PGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   81 TGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:MTH00079 125 TSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLA 203

                        170       180
                 ....*....|....*....|.
gi 50659940  161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:MTH00079 204 GAITMLLTDRNLNTSFFDPST 224
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-181 3.33e-60

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: 193.90  E-value: 3.33e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPlMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:cd00919  33 PGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:cd00919 112 TGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLA 191

                       170       180
                ....*....|....*....|.
gi 50659940 161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:cd00919 192 AALVMLLLDRNFGTSFFDPAG 212
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-181 4.86e-52

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 173.77  E-value: 4.86e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAG 80
Cdd:COG0843  47 PGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAAD 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  81 TGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:COG0843 126 VGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLA 205

                       170       180
                ....*....|....*....|.
gi 50659940 161 AGITMLLTDRNLNTTFFDPAG 181
Cdd:COG0843 206 AALLLLLLDRSLGTHFFDPAG 226
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 10-181 5.31e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 157.53  E-value: 5.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   10 IYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVeaGAGTGWTVYPPL 89
Cdd:MTH00048  54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   90 AGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSqYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTD 169
Cdd:MTH00048 132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                        170
                 ....*....|..
gi 50659940  170 RNLNTTFFDPAG 181
Cdd:MTH00048 211 RNFGSAFFDPLG 222
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 11-181 3.31e-44

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: 152.74  E-value: 3.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  11 YNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLA 90
Cdd:cd01662  49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940  91 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTDR 170
Cdd:cd01662 128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207

                       170
                ....*....|.
gi 50659940 171 NLNTTFFDPAG 181
Cdd:cd01662 208 YFGTHFFTNAL 218
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-180 7.13e-33

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: 121.14  E-value: 7.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940     1 PGALLGDDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMveaGAG 80
Cdd:pfam00115  31 PGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GAT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    81 TGWTVYPPLAGnlahagasVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQyQTPLFVWSVMITAVLLLLSLPVLA 160
Cdd:pfam00115 107 TGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLA 177

                         170       180
                  ....*....|....*....|
gi 50659940   161 AGITMLLTDRNLNTTFFDPA 180
Cdd:pfam00115 178 AALLLLLLDRSLGAGGGDPL 197
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 11-177 5.86e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 120.43  E-value: 5.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   11 YNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLA 90
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940   91 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTDR 170
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                 ....*..
gi 50659940  171 NLNTTFF 177
Cdd:PRK15017 258 YLGTHFF 264
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 7-180 4.79e-30

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: 114.95  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940     7 DDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVY 86
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50659940    87 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTVINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITML 166
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170
                  ....*....|....
gi 50659940   167 LTDRNLNTTFFDPA 180
Cdd:TIGR02882 247 TTDRIFDTAFFTVA 260
 
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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