|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
8.73e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 418.89 E-value: 8.73e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-226 |
4.17e-130 |
|
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: 375.28 E-value: 4.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 8 TNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 88 PDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNFITTVI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 262073320 168 NMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-226 |
4.51e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 235.79 E-value: 4.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWL 80
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-220 |
1.24e-42 |
|
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: 148.88 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 12 DIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 92 FPRMNNMSFWLLPPSLCLLLVSSmveMGVGTGWTVYPPLssnvahsgPSVDLAIFSLHLAGISSILGAVNFITTVINMRT 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 262073320 172 IGMNFdRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDP 220
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-226 |
1.20e-37 |
|
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: 138.45 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 2 NKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGgFGNWLL 81
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 82 PLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVN 161
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262073320 162 FITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMP 265
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
8.73e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 418.89 E-value: 8.73e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-226 |
4.17e-130 |
|
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: 375.28 E-value: 4.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 8 TNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 88 PDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNFITTVI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 262073320 168 NMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
4.20e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 371.32 E-value: 4.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00167 3 INRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00167 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00167 163 NFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
1.31e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 365.18 E-value: 1.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00116 3 ITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00116 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00116 163 NFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
1.71e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 364.43 E-value: 1.71e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 226
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
3-226 |
3.21e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 358.91 E-value: 3.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 3 KWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 83 LMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262073320 163 ITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 225
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
8.69e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 334.88 E-value: 8.69e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-226 |
5.39e-113 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 332.64 E-value: 5.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 3 KWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 83 LMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262073320 163 ITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 225
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
3.21e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 325.74 E-value: 3.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-226 |
6.87e-110 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 324.91 E-value: 6.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00103 3 INRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00103 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00103 163 NFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
7.42e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 322.26 E-value: 7.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
3-226 |
4.09e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 310.60 E-value: 4.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 3 KWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 83 LMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262073320 163 ITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
5.57e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 307.52 E-value: 5.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
6.13e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 299.29 E-value: 6.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00079 4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSnVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNP 228
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
3-226 |
3.10e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 280.36 E-value: 3.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 3 KWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 83 LMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262073320 163 ITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 229
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
10-226 |
3.69e-81 |
|
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: 249.76 E-value: 3.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 10 HKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLlPLMIGAPD 89
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 90 MAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNFITTVINM 169
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 262073320 170 RTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDP 216
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-226 |
4.51e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 235.79 E-value: 4.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 1 MNKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWL 80
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAV 160
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262073320 161 NFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-226 |
1.34e-67 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 216.08 E-value: 1.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 4 WLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPL 83
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 84 MIGAPDMAFPRMNNMSFWLLPPSLCLLLVSsmVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNFI 163
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262073320 164 TTVINMRTIGMNFdRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDP 226
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
4-226 |
2.07e-58 |
|
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: 192.03 E-value: 2.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 4 WLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGgFGNWLLPL 83
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 84 MIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVNFI 163
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262073320 164 TTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNP 222
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-220 |
1.24e-42 |
|
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: 148.88 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 12 DIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 92 FPRMNNMSFWLLPPSLCLLLVSSmveMGVGTGWTVYPPLssnvahsgPSVDLAIFSLHLAGISSILGAVNFITTVINMRT 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 262073320 172 IGMNFdRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDP 220
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDP 196
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-226 |
1.20e-37 |
|
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: 138.45 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 2 NKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIELAQPGPFLMNDQLYNVIVTSHAFIMIFFMVMPIMIGgFGNWLL 81
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 82 PLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILGAVN 161
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262073320 162 FITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDP 226
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMP 265
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-225 |
7.68e-35 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 130.44 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 2 NKWLFSTNHKDIGTLYFLFGIWSGMVGMMLSMIIRIE--LAQPGPF-LMNDQLYNVIVTSHAFIMIFFMVMPIMIGgFGN 78
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262073320 79 WLLPLMIGAPDMAFPRMNNMSFWLLPPSLCLLLVSSMVEMGVGTGWTVYPPLSSNVAHSGPSVDLAIFSLHLAGISSILG 158
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262073320 159 AVNFITTVINMRTIGMNFDRTPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGD 225
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGN 271
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