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Conserved domains on  [gi|29171281|gb|AAO62211|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Lasiopogon sp. SLB-2003]

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 ...
 2-208 5.77e-140

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 400.40  E-value: 5.77e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-208 5.77e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 400.40  E-value: 5.77e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-208 1.62e-121

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: 352.94  E-value: 1.62e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:cd01663  15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:cd01663  95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 29171281 162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:cd01663 175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 221
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
6-208 1.27e-66

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 213.45  E-value: 1.27e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   6 MVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 85
Cdd:COG0843  31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  86 SLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLFVWS 165
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 29171281 166 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLL 232
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-208 1.50e-39

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: 140.02  E-value: 1.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281     5 GMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 84
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    85 PSLTLLLASSMvenGAGTGWTVYPPLSAgiahggasVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFdRMPLFVW 164
Cdd:pfam00115  93 LGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 29171281   165 SVLITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPVL 208
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLL 198
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-208 7.39e-33

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: 124.20  E-value: 7.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    12 SILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 91
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    92 ASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLFVWSVLITAI 171
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 29171281   172 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPML 267
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-208 5.77e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 400.40  E-value: 5.77e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-208 1.62e-121

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: 352.94  E-value: 1.62e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:cd01663  15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:cd01663  95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 29171281 162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:cd01663 175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 221
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-208 1.70e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 348.59  E-value: 1.70e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00167  24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-208 6.12e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 339.39  E-value: 6.12e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00142  22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00142 102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00142 182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 228
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 3-208 2.33e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 338.11  E-value: 2.33e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    3 WSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 82
Cdd:MTH00223  22 WSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   83 LPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLF 162
Cdd:MTH00223 102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 29171281  163 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00223 182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 227
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-208 2.89e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 337.83  E-value: 2.89e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00116  24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00116 104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00116 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-208 1.31e-104

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 310.66  E-value: 1.31e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00103  24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00103 104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00103 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-208 1.75e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 310.22  E-value: 1.75e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00037  24 AWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00037 104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00037 184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPIL 230
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-208 1.35e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 308.01  E-value: 1.35e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00183  24 AWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00183 104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00183 184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-208 1.48e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 308.02  E-value: 1.48e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00077  24 AWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00077 104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00077 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVL 230
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-208 7.28e-102

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 303.36  E-value: 7.28e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00007  21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00007 101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00007 181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 227
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-208 2.75e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 289.42  E-value: 2.75e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00184  26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00184 106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00184 186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 232
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-208 3.82e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 289.41  E-value: 3.82e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00182  26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00182 106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00182 186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 232
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-208 3.26e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 273.48  E-value: 3.26e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    3 WSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 82
Cdd:MTH00079  26 WSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   83 LPPSLTLLLASSMVENGAGTGWTVYPPLSAgIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLF 162
Cdd:MTH00079 106 LPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLF 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 29171281  163 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00079 185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLL 230
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-208 1.88e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 267.26  E-value: 1.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    2 AWSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 81
Cdd:MTH00026  25 ALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   82 LLPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPL 161
Cdd:MTH00026 105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171281  162 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00026 185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 231
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 3-208 3.30e-76

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 236.27  E-value: 3.30e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   3 WSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWL 82
Cdd:cd00919  14 VALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWL 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  83 LPPSLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLF 162
Cdd:cd00919  93 FPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLF 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 29171281 163 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:cd00919 173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVL 218
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
6-208 1.27e-66

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 213.45  E-value: 1.27e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   6 MVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 85
Cdd:COG0843  31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  86 SLTLLLASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLFVWS 165
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 29171281 166 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLL 232
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 3-208 5.31e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 192.97  E-value: 5.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    3 WSGMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 82
Cdd:MTH00048  26 WSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   83 LPPSLTLLLASSMVenGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFdRMPLF 162
Cdd:MTH00048 106 LVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSII 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 29171281  163 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:MTH00048 183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVL 228
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 13-208 3.96e-53

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 177.39  E-value: 3.96e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  13 ILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLA 92
Cdd:cd01662  30 LLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  93 SSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLFVWSVLITAIL 172
Cdd:cd01662 109 SLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSIL 188

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 29171281 173 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:cd01662 189 ILFAFPVLTAALALLELDRYFGTHFFTNALGGNPML 224
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-208 1.50e-39

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: 140.02  E-value: 1.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281     5 GMVGTSFSILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 84
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    85 PSLTLLLASSMvenGAGTGWTVYPPLSAgiahggasVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFdRMPLFVW 164
Cdd:pfam00115  93 LGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 29171281   165 SVLITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPVL 208
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLL 198
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 32-205 2.47e-33

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 125.43  E-value: 2.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281   32 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLS 111
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281  112 AGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 191
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170
                 ....*....|....
gi 29171281  192 NLNTSFFDPAGGGD 205
Cdd:PRK15017 258 YLGTHFFTNDMGGN 271
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-208 7.39e-33

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: 124.20  E-value: 7.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    12 SILIRAELGHAGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 91
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171281    92 ASSMVENGAGTGWTVYPPLSAGIAHGGASVDLTIFSLHLAGVSSILGAVNFITTVINMRSKGITFDRMPLFVWSVLITAI 171
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 29171281   172 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVL 208
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPML 267
 
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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