|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.37e-142 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 407.33 E-value: 2.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00153 17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00153 97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00153 177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-225 |
2.21e-132 |
|
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: 381.06 E-value: 2.21e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:cd01663 10 YLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:cd01663 90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:cd01663 170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-225 |
6.06e-76 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 238.10 E-value: 6.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:COG0843 22 YLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:COG0843 101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:COG0843 181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-225 |
7.64e-48 |
|
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: 162.74 E-value: 7.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:pfam00115 6 YLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIvdsGVGTGWTVYPPLAGpiahsgvaVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:pfam00115 85 ALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 dQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHLEV 225
Cdd:pfam00115 154 -RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
12-225 |
2.05e-40 |
|
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: 145.77 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 12 GTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 91
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 92 ILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVM 171
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254575737 172 ITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.37e-142 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 407.33 E-value: 2.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00153 17 YFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00153 97 NMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00153 177 DRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-225 |
2.21e-132 |
|
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: 381.06 E-value: 2.21e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:cd01663 10 YLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:cd01663 90 NLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:cd01663 170 EKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
3.84e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 374.01 E-value: 3.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00167 19 YFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00167 99 NMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQ 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00167 179 YQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
8.79e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 370.58 E-value: 8.79e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00116 19 YLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00116 99 NMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQ 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00116 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.86e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 356.21 E-value: 2.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00223 16 YLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00223 96 NMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00223 176 ERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.63e-121 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 354.03 E-value: 2.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00142 17 YFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00142 97 NMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00142 177 ERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
7.10e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 335.26 E-value: 7.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00037 19 YLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00037 99 NMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00037 179 DRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
3.27e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 330.75 E-value: 3.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00077 19 YLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00077 99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQ 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00077 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.20e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 328.81 E-value: 2.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00183 19 YLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00183 99 NMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQ 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00183 179 YQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-225 |
3.20e-111 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 328.38 E-value: 3.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00103 19 YLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00103 99 NMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQ 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00103 179 YQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-225 |
6.27e-106 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 314.53 E-value: 6.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00007 16 YFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00007 96 NMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00007 176 ERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.38e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 313.68 E-value: 2.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00182 21 YLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00182 101 NISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTF 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00182 181 NRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
4.55e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 307.52 E-value: 4.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00184 21 YLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00184 101 NISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITM 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00184 181 DRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.31e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 300.83 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00079 20 YFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGpIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00079 100 NLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00079 179 EHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.67e-93 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 283.44 E-value: 1.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00026 20 YLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00026 100 NISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTM 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00026 180 SRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-225 |
6.56e-84 |
|
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: 256.69 E-value: 6.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMN 80
Cdd:cd00919 8 YLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:cd00919 87 NLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:cd00919 167 DKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-225 |
6.06e-76 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 238.10 E-value: 6.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:COG0843 22 YLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:COG0843 101 ALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 DQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:COG0843 181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.23e-67 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 216.08 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:MTH00048 20 YTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIVdsGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:MTH00048 100 ALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 dQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:MTH00048 178 -RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
10-225 |
6.23e-62 |
|
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: 200.89 E-value: 6.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 10 LVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 89
Cdd:cd01662 23 LRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 90 SLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWS 169
Cdd:cd01662 102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254575737 170 VMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:cd01662 182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-225 |
7.64e-48 |
|
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: 162.74 E-value: 7.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 1 FFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMN 80
Cdd:pfam00115 6 YLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 81 NMSFWLLPPSLILLISSSIvdsGVGTGWTVYPPLAGpiahsgvaVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNM 160
Cdd:pfam00115 85 ALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254575737 161 dQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHLEV 225
Cdd:pfam00115 154 -RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
12-225 |
2.05e-40 |
|
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: 145.77 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 12 GTALSMIIRMELSVPGHLINDDQIYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 91
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 92 ILLISSSIVDSGVGTGWTVYPPLAGPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVM 171
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254575737 172 ITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
36-225 |
4.18e-37 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 136.99 E-value: 4.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 36 YNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLA 115
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254575737 116 GPIAHSGVAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDR 195
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190
....*....|....*....|....*....|
gi 254575737 196 NINTSFFDPAGGGDPILYQHLFWFFGHLEV 225
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287
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