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Conserved domains on  [gi|60099333|emb|CAI56318|]
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cytochrome oxidase 1, partial (mitochondrion) [Clavelina gemmae]

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 ...
 1-199 7.08e-124

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 MTH00167:

Pssm-ID: 469701  Cd Length: 512  Bit Score: 359.38  E-value: 7.08e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00167  24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDP 222
 
Name Accession Description Interval E-value
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-199 7.08e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 359.38  E-value: 7.08e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00167  24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDP 222
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-199 3.15e-115

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: 336.38  E-value: 3.15e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:cd01663  15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:cd01663  95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 60099333 161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:cd01663 175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-199 1.67e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 204.59  E-value: 1.67e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   5 LVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPvMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWLLPP 84
Cdd:COG0843  31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  85 ALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFCWS 164
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 60099333 165 VVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-199 3.50e-40

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: 141.56  E-value: 3.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333     5 LVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPvMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWLLPP 84
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    85 ALFLLVLSVfngDGVGTGWTIYPPLSGilahssgaVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYnNLSLFCWS 164
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 60099333   165 VVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-197 1.83e-29

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: 114.18  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    11 SMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGgFGNWLLPMMVGSPDMAFPRLNNMSFWLLPPALFLLV 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    91 LSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFCWSVVVTTI 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180
                  ....*....|....*....|....*..
gi 60099333   171 LLVLSLPVLAAAITMLL*DRNLNTSFF 197
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFF 257
 
Name Accession Description Interval E-value
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-199 7.08e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 359.38  E-value: 7.08e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00167  24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDP 222
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-199 1.92e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 340.31  E-value: 1.92e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 220
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-199 3.15e-115

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: 336.38  E-value: 3.15e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:cd01663  15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:cd01663  95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 60099333 161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:cd01663 175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 213
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-199 2.11e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 304.59  E-value: 2.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00223  21 MWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00223 101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00223 181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDP 219
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-199 9.45e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 302.78  E-value: 9.45e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    2 YSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWL 81
Cdd:MTH00116  25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   82 LPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLF 161
Cdd:MTH00116 105 LPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLF 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60099333  162 CWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00116 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-199 6.89e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 295.48  E-value: 6.89e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00142  22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00142 102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00142 182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDP 220
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-199 6.99e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 270.16  E-value: 6.99e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    2 YSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWL 81
Cdd:MTH00037  25 WAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   82 LPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLF 161
Cdd:MTH00037 105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60099333  162 CWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00037 185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDP 222
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-199 1.62e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 269.38  E-value: 1.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00182  26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00182 106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00182 186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-199 5.78e-88

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 267.54  E-value: 5.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00007  21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00007 101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00007 181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDP 219
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-199 2.82e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 266.02  E-value: 2.82e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    2 YSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWL 81
Cdd:MTH00183  25 WAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   82 LPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLF 161
Cdd:MTH00183 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60099333  162 CWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00183 185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-199 1.05e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 264.38  E-value: 1.05e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00184  26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00184 106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00184 186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDP 224
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-199 2.77e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 263.34  E-value: 2.77e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    2 YSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWL 81
Cdd:MTH00077  25 WAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   82 LPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLF 161
Cdd:MTH00077 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60099333  162 CWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00077 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-199 6.66e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 261.92  E-value: 6.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00079  25 LWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSgILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:MTH00079 105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00079 184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDP 222
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-199 1.82e-85

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 260.97  E-value: 1.82e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    2 YSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWL 81
Cdd:MTH00103  25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   82 LPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLF 161
Cdd:MTH00103 105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60099333  162 CWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00103 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDP 222
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-199 1.94e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 238.37  E-value: 1.94e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    3 SALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWLL 82
Cdd:MTH00026  27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   83 PPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFC 162
Cdd:MTH00026 107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 60099333  163 WSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDP 223
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-199 1.55e-72

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: 226.26  E-value: 1.55e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMmVGSPDMAFPRLNNMSFW 80
Cdd:cd00919  13 FVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFW 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  81 LLPPALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSL 160
Cdd:cd00919  92 LFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPL 171

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 60099333 161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:cd00919 172 FVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDP 210
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-199 1.67e-63

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 204.59  E-value: 1.67e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   5 LVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPvMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWLLPP 84
Cdd:COG0843  31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  85 ALFLLVLSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFCWS 164
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 60099333 165 VVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDP 224
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-199 2.27e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 196.05  E-value: 2.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    1 IYSALVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGGFGNWLLPMMVGSPDMAFPRLNNMSFW 80
Cdd:MTH00048  25 VWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   81 LLPPALFLLVLSVFNGDGVgtGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNlSL 160
Cdd:MTH00048 105 LLVPSIVFLLLSMCLGAGV--GWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SI 181

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60099333  161 FCWSVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDP 220
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 5-199 9.24e-46

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: 157.36  E-value: 9.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   5 LVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGgFGNWLLPMMVGSPDMAFPRLNNMSFWLLPP 84
Cdd:cd01662  23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  85 ALFLLVLSVFNGDGVGTGWTIYPPLSGiLAHSSGA-VDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFCW 163
Cdd:cd01662 102 GGLLLNASLLIGGFPDAGWFAYPPLSG-LEYSPGVgVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTW 180

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 60099333 164 SVVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:cd01662 181 TTLVTSILILFAFPVLTAALALLELDRYFGTHFFTN 216
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-199 3.50e-40

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: 141.56  E-value: 3.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333     5 LVGTGLSMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPvMIGGFGNWLLPMMVGSPDMAFPRLNNMSFWLLPP 84
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    85 ALFLLVLSVfngDGVGTGWTIYPPLSGilahssgaVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYnNLSLFCWS 164
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 60099333   165 VVVTTILLVLSLPVLAAAITMLL*DRNLNTSFFDP 199
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 31-197 4.37e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 127.36  E-value: 4.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333   31 YNVVVTAHALLMIFFFIMPVMIGgFGNWLLPMMVGSPDMAFPRLNNMSFWLLPPALFLLVLSVFNGDGVGTGWTIYPPLS 110
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333  111 GILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFCWSVVVTTILLVLSLPVLAAAITMLL*DR 190
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                 ....*..
gi 60099333  191 NLNTSFF 197
Cdd:PRK15017 258 YLGTHFF 264
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-197 1.83e-29

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: 114.18  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    11 SMIIRTELSQTGQLIGNGQIYNVVVTAHALLMIFFFIMPVMIGgFGNWLLPMMVGSPDMAFPRLNNMSFWLLPPALFLLV 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60099333    91 LSVFNGDGVGTGWTIYPPLSGILAHSSGAVDMGIFSLHLAGVSSILGSVNFLVTMSNMKLKGFDYNNLSLFCWSVVVTTI 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180
                  ....*....|....*....|....*..
gi 60099333   171 LLVLSLPVLAAAITMLL*DRNLNTSFF 197
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFF 257
 
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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