|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
3.92e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 339.92 E-value: 3.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00153 21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-206 |
4.45e-110 |
|
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: 323.67 E-value: 4.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:cd01663 14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:cd01663 94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:cd01663 174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-206 |
4.60e-59 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 193.42 E-value: 4.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:COG0843 26 AFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:COG0843 105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:COG0843 185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-200 |
1.32e-36 |
|
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: 132.31 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:pfam00115 10 ALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSnfiNEGSGTGWTVYPPLasnifhsgPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLeKIP 160
Cdd:pfam00115 89 WLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
8-206 |
2.81e-31 |
|
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: 119.57 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 8 GSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPSI 87
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 88 SLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLLVWSIL 167
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190
....*....|....*....|....*....|....*....
gi 1740141090 168 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMP 265
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
3.92e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 339.92 E-value: 3.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00153 21 GAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-206 |
4.45e-110 |
|
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: 323.67 E-value: 4.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:cd01663 14 GLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:cd01663 94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:cd01663 174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
2-206 |
8.68e-101 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 300.83 E-value: 8.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 2 IWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00167 24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 82 LLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPL 161
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1740141090 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-206 |
9.24e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 293.15 E-value: 9.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 3 WAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00116 25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 83 LPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLL 162
Cdd:MTH00116 105 LPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLF 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1740141090 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00116 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
3.06e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 291.50 E-value: 3.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00223 20 GMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:MTH00223 100 WLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00223 180 LFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 225
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-206 |
1.59e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 284.69 E-value: 1.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 2 IWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00142 22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 82 LLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPL 161
Cdd:MTH00142 102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1740141090 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00142 182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 226
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
2-206 |
2.76e-89 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 271.39 E-value: 2.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 2 IWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00007 21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 82 LLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPL 161
Cdd:MTH00007 101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1740141090 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00007 181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 225
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
3-206 |
8.29e-87 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 264.86 E-value: 8.29e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 3 WAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00183 25 WAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 83 LPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLL 162
Cdd:MTH00183 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1740141090 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00183 185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
3-206 |
9.45e-87 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 264.88 E-value: 9.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 3 WAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00077 25 WAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 83 LPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLL 162
Cdd:MTH00077 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1740141090 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00077 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-206 |
9.95e-86 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 262.13 E-value: 9.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 3 WAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00103 25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 83 LPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLL 162
Cdd:MTH00103 105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1740141090 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00103 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-206 |
2.72e-84 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 258.61 E-value: 2.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 3 WAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWL 82
Cdd:MTH00037 25 WAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 83 LPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLL 162
Cdd:MTH00037 105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1740141090 163 VWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00037 185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-206 |
1.71e-81 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 251.28 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 2 IWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00184 26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 82 LLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPL 161
Cdd:MTH00184 106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1740141090 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00184 186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-206 |
5.46e-80 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 247.29 E-value: 5.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:MTH00079 24 GLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLaSNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:MTH00079 104 WLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00079 183 LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNP 228
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-206 |
3.90e-79 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 245.50 E-value: 3.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 2 IWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00182 26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 82 LLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPL 161
Cdd:MTH00182 106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1740141090 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00182 186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
4-206 |
1.93e-73 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 231.06 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 4 AGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFWLL 83
Cdd:MTH00026 27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 84 PPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLLV 163
Cdd:MTH00026 107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1740141090 164 WSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 229
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-206 |
2.34e-70 |
|
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: 220.87 E-value: 2.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPlMLGSPDMAYPRMNNMSF 80
Cdd:cd00919 12 AFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:cd00919 91 WLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:cd00919 171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDP 216
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-206 |
4.60e-59 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 193.42 E-value: 4.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:COG0843 26 AFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIP 160
Cdd:COG0843 105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:COG0843 185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-206 |
3.82e-56 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 185.27 E-value: 3.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 2 IWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPDMAYPRMNNMSFW 81
Cdd:MTH00048 25 VWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 82 LLPPSISLLILSNFIneGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTlEKIPL 161
Cdd:MTH00048 105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1740141090 162 LVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDP 226
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-206 |
1.07e-47 |
|
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: 162.75 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 7 MGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPS 86
Cdd:cd01662 24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 87 ISLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLLVWSI 166
Cdd:cd01662 103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1740141090 167 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:cd01662 183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNP 222
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-200 |
1.32e-36 |
|
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: 132.31 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 1 AIWAGMMGSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMAYPRMNNMSF 80
Cdd:pfam00115 10 ALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 81 WLLPPSISLLILSnfiNEGSGTGWTVYPPLasnifhsgPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLeKIP 160
Cdd:pfam00115 89 WLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1740141090 161 LLVWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFFDP 200
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
8-206 |
2.81e-31 |
|
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: 119.57 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 8 GSSMSMIIRLELGSSNSLINNDQTFNSLVTSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPSI 87
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 88 SLLILSNFINEGSGTGWTVYPPLASNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLLVWSIL 167
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190
....*....|....*....|....*....|....*....
gi 1740141090 168 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSRGGDP 206
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMP 265
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
32-205 |
1.23e-30 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 117.73 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 32 FNSLVTSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPDMAYPRMNNMSFWLLPPSISLLILSNFINEGSGTGWTVYPPLA 111
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740141090 112 SNIFHSGPSIDLTIFSLHIAGMSSILGAINFISTILNMHNINMTLEKIPLLVWSILITAILLLLSLPVLAGAITMLLTDR 191
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170
....*....|....
gi 1740141090 192 NLNTSFFDPSRGGD 205
Cdd:PRK15017 258 YLGTHFFTNDMGGN 271
|
|
|