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Conserved domains on  [gi|998446779|gb|AMK43346|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Platygastridae sp. BOLD:ACL8018]

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 ...
 1-200 6.62e-106

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: 313.34  E-value: 6.62e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNiahSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-200 6.62e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 313.34  E-value: 6.62e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNiahSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-200 9.78e-99

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: 294.39  E-value: 9.78e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLT---NPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF 210
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-200 3.99e-51

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 172.23  E-value: 3.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   2 LYFLFGI*AGMIGSSLSMIIRLE-VGTSSTLIGNDQiYNSIVTAHAFIMIFFMIMPlMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQlAGPGLGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLT---NPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:COG0843   99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:COG0843  179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHF 221
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-198 2.80e-33

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 123.07  E-value: 2.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779    2 LYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPlMLGGFGNWLIPLMMSAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   82 NNMSFWLLPPSIMLLIYSnifGMGTGTGWTLYPPLslltnPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSFKMeK 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLAS---FGGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-R 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 998446779  162 MSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT 198
Cdd:pfam00115 155 MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA 191
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 14-200 3.19e-25

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: 102.24  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   14 GSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGgFGNWLIPLMMSAPDMAFPRMNNMSFWLLPPSI 93
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   94 MLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSFKMEKMSLFSWSIF 170
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAgpeFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190
                  ....*....|....*....|....*....|
gi 998446779  171 ITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAF 256
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-200 6.62e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 313.34  E-value: 6.62e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNiahSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-200 9.78e-99

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: 294.39  E-value: 9.78e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLT---NPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF 210
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-200 7.68e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 287.73  E-value: 7.68e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00167  17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00167  97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNlahAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTF 219
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-200 1.41e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 271.97  E-value: 1.41e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00116  17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00116  97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAgnlAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-200 6.13e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 270.06  E-value: 6.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00142  15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00142  95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSsnlAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSF 217
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-200 7.57e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 267.23  E-value: 7.57e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00223  14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00223  94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNlahAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSF 216
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-200 1.79e-79

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 245.58  E-value: 1.79e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00007  14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00007  94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLAsnlAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSF 216
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-200 1.57e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 243.29  E-value: 1.57e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00183  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00183  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-200 1.97e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 243.31  E-value: 1.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00077  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00077  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-200 2.60e-78

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 242.87  E-value: 2.60e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00103  17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00103  97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-200 9.23e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 238.96  E-value: 9.23e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00037  17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00037  97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSsniAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTF 219
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-200 3.20e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 237.42  E-value: 3.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00184  19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00184  99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIqahSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTF 221
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-200 7.77e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 236.12  E-value: 7.77e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00079  18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLTNP--SIDMGIFSLHLAGISSILGSINFICTIINMCPNSFK 158
Cdd:MTH00079  98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPgsSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 998446779 159 MEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00079 178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSF 219
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-200 2.22e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 232.79  E-value: 2.22e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00182  19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00182  99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIqahSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTF 221
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-200 1.71e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 210.25  E-value: 1.71e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:MTH00026  18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLL---TNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:MTH00026  98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIqahSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTF 220
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-200 6.24e-61

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: 196.60  E-value: 6.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   1 TLYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPlMMSAPDMAFPR 80
Cdd:cd00919    6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLT---NPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:cd00919   85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSyssGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:cd00919  165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSF 207
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-200 3.99e-51

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 172.23  E-value: 3.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   2 LYFLFGI*AGMIGSSLSMIIRLE-VGTSSTLIGNDQiYNSIVTAHAFIMIFFMIMPlMLGGFGNWLIPLMMSAPDMAFPR 80
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQlAGPGLGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLT---NPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:COG0843   99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:COG0843  179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHF 221
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-200 8.91e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 165.62  E-value: 8.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   2 LYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGGFGNWLIPLMMSAPDMAFPRM 81
Cdd:MTH00048  19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  82 NNMSFWLLPPSIMLLIYSNIFgmGTGTGWTLYPPLSLLTNPS---IDMGIFSLHLAGISSILGSINFICTIINMCPNSFk 158
Cdd:MTH00048  99 NALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSswgVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV- 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 998446779 159 MEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:MTH00048 176 FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAF 217
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-200 5.45e-39

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: 139.25  E-value: 5.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   2 LYFLFGI*AGMIGSSLSMIIRLEVGT-SSTLIGNDQiYNSIVTAHAFIMIFFMIMPLMLGgFGNWLIPLMMSAPDMAFPR 80
Cdd:cd01662   13 MYIITAFVFFLRGGVDALLMRTQLALpGNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  81 MNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLSLLTN---PSIDMGIFSLHLAGISSILGSINFICTIINMCPNSF 157
Cdd:cd01662   91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYspgVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998446779 158 KMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:cd01662  171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHF 213
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-198 2.80e-33

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 123.07  E-value: 2.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779    2 LYFLFGI*AGMIGSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPlMLGGFGNWLIPLMMSAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   82 NNMSFWLLPPSIMLLIYSnifGMGTGTGWTLYPPLslltnPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSFKMeK 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLAS---FGGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-R 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 998446779  162 MSLFSWSIFITTILLLLSLPVLAGAITMLLADRNLNT 198
Cdd:pfam00115 155 MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA 191
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 38-200 1.56e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 103.09  E-value: 1.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779  38 YNSIVTAHAFIMIFFMIMPLMLGgFGNWLIPLMMSAPDMAFPRMNNMSFWLLPPSIMLLIYSNIFGMGTGTGWTLYPPLS 117
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779 118 LLT---NPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSFKMEKMSLFSWSIFITTILLLLSLPVLAGAITMLLADR 194
Cdd:PRK15017 178 GIEyspGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257


                 ....*.
gi 998446779 195 NLNT*F 200
Cdd:PRK15017 258 YLGTHF 263
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 14-200 3.19e-25

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: 102.24  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   14 GSSLSMIIRLEVGTSSTLIGNDQIYNSIVTAHAFIMIFFMIMPLMLGgFGNWLIPLMMSAPDMAFPRMNNMSFWLLPPSI 93
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998446779   94 MLLIYSNIFGMGTGTGWTLYPPLS---LLTNPSIDMGIFSLHLAGISSILGSINFICTIINMCPNSFKMEKMSLFSWSIF 170
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAgpeFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190
                  ....*....|....*....|....*....|
gi 998446779  171 ITTILLLLSLPVLAGAITMLLADRNLNT*F 200
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAF 256
 
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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