|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.05e-143 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 410.80 E-value: 1.05e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00153 13 IGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-225 |
2.27e-134 |
|
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: 386.45 E-value: 2.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:cd01663 6 IGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-225 |
1.06e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 237.72 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAF 80
Cdd:COG0843 18 IGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:COG0843 97 PRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:COG0843 177 GMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-225 |
1.37e-46 |
|
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: 159.28 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAF 80
Cdd:pfam00115 2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIvdsGVGTGWTVYPPLAGpiahsgaaVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMdQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFG 225
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-225 |
2.22e-39 |
|
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: 143.07 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAF 80
Cdd:TIGR02882 53 IGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:TIGR02882 132 PVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAP 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:TIGR02882 212 GMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.05e-143 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 410.80 E-value: 1.05e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00153 13 IGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-225 |
2.27e-134 |
|
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: 386.45 E-value: 2.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:cd01663 6 IGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.00e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 377.87 E-value: 1.00e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00167 15 IGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00167 95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00167 175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
8.19e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 373.27 E-value: 8.19e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00116 15 IGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00116 95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00116 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.91e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 361.60 E-value: 2.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00223 12 IGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00223 92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00223 172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
6.45e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 357.88 E-value: 6.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00142 13 IGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00142 93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00142 173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
5.78e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 337.96 E-value: 5.78e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00037 15 IGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00037 95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00037 175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
5.51e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 332.68 E-value: 5.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00077 15 IGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00077 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00077 175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.22e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 331.50 E-value: 2.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00183 15 IGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00183 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00183 175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-225 |
3.17e-112 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 330.69 E-value: 3.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00103 15 IGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00103 95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00103 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-225 |
3.78e-107 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 317.61 E-value: 3.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00007 12 IGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00007 92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00007 172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
5.36e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 317.92 E-value: 5.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00182 17 IGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00182 97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00182 177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.39e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 310.99 E-value: 2.39e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00184 17 IGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00184 97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00184 177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
1.92e-101 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 303.14 E-value: 1.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00079 16 IGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGpIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00079 96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
2.00e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 285.75 E-value: 2.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00026 16 IGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00026 96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00026 176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-225 |
3.95e-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: 257.07 E-value: 3.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPlMIGAPDMAF 80
Cdd:cd00919 4 IGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:cd00919 83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:cd00919 163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-225 |
1.06e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 237.72 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAF 80
Cdd:COG0843 18 IGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:COG0843 97 PRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:COG0843 177 GMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-225 |
4.96e-67 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 214.54 E-value: 4.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 80
Cdd:MTH00048 16 IGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVdsGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:MTH00048 96 PRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMdQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:MTH00048 174 NVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-225 |
6.26e-61 |
|
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: 198.19 E-value: 6.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAF 80
Cdd:cd01662 10 IGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:cd01662 89 PRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:cd01662 169 GMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-225 |
1.37e-46 |
|
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: 159.28 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMAF 80
Cdd:pfam00115 2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIvdsGVGTGWTVYPPLAGpiahsgaaVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMdQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFG 225
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-225 |
2.22e-39 |
|
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: 143.07 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 1 IGTLYFIFGAWAGLVGTALSMIIRMELSVPGHLINDDQMYNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAF 80
Cdd:TIGR02882 53 IGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 81 PRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLAGPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAP 160
Cdd:TIGR02882 132 PVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAP 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057720314 161 EMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:TIGR02882 212 GMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
40-225 |
1.38e-34 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 129.67 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 40 YNVVVTAHAFIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLISSSIVDSGVGTGWTVYPPLA 119
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057720314 120 GPIAHSGAAVDLAIFSLHLAGVSSILGAINFITTTINMKAPEMNMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDR 199
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
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170 180
....*....|....*....|....*.
gi 1057720314 200 NINTSFFDPAGGGDPILYQHLFWFFG 225
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWG 283
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