|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
1.56e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 373.82 E-value: 1.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00153 34 LIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00153 114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00153 194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-200 |
7.23e-116 |
|
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: 337.92 E-value: 7.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:cd01663 27 LIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:cd01663 107 ALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:cd01663 187 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-200 |
8.09e-64 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 205.75 E-value: 8.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:COG0843 39 LMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLIS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:COG0843 118 LFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILI 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:COG0843 198 LLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-200 |
3.82e-36 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 130.77 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:pfam00115 23 LIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GlveSGVGTGWTVYPPL*saiahagaSVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMdQMPLFVWAVFITA*LL 160
Cdd:pfam00115 102 F---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILI 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 200
Cdd:pfam00115 170 LLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-200 |
8.73e-32 |
|
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: 120.73 E-value: 8.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:TIGR02882 74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLII 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
1.56e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 373.82 E-value: 1.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00153 34 LIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00153 114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00153 194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-200 |
7.23e-116 |
|
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: 337.92 E-value: 7.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:cd01663 27 LIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:cd01663 107 ALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:cd01663 187 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
4.30e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 332.03 E-value: 4.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00167 36 LIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00167 116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00167 196 LLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
4.59e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 321.67 E-value: 4.59e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00142 34 LIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00142 114 AAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00142 194 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
7.52e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 318.57 E-value: 7.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00116 36 LIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00116 116 STVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00116 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
1.70e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 314.99 E-value: 1.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00223 33 LIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00223 113 SAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00223 193 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
2.51e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 291.73 E-value: 2.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00037 36 IIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00037 116 AGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00037 196 LLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-200 |
7.58e-97 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 290.26 E-value: 7.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00007 33 LIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00007 113 AAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00007 193 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-200 |
4.03e-96 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 288.70 E-value: 4.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00103 36 LIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00103 116 SMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00103 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
1.09e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 287.59 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00183 36 LIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00183 116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00183 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
3.31e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 286.07 E-value: 3.31e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00077 36 LIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00077 116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00077 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
1.06e-89 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 272.47 E-value: 1.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00182 38 LIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00182 118 AFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00182 198 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
4.72e-89 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 270.54 E-value: 4.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00184 38 LIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00184 118 AFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00184 198 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
4.34e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 267.70 E-value: 4.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00079 37 IIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00079 117 CFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00079 196 VLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
1.58e-82 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 254.17 E-value: 1.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00026 37 LIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:MTH00026 117 SLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00026 197 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-200 |
4.83e-71 |
|
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: 222.41 E-value: 4.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:cd00919 25 LIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:cd00919 104 VLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:cd00919 184 LLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-200 |
8.09e-64 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 205.75 E-value: 8.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:COG0843 39 LMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLIS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:COG0843 118 LFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILI 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:COG0843 198 LLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-200 |
5.14e-53 |
|
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: 176.62 E-value: 5.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQP-GTLIGNDQiYNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLM 79
Cdd:cd01662 31 LMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 80 SGLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*L 159
Cdd:cd01662 109 SLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSIL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1950492001 160 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:cd01662 189 ILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-200 |
5.47e-53 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 176.79 E-value: 5.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:MTH00048 37 LIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVesGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMdQMPLFVWAVFITA*LL 160
Cdd:MTH00048 117 MCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:MTH00048 194 LLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-200 |
3.82e-36 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 130.77 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:pfam00115 23 LIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GlveSGVGTGWTVYPPL*saiahagaSVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMdQMPLFVWAVFITA*LL 160
Cdd:pfam00115 102 F---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILI 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 200
Cdd:pfam00115 170 LLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
19-199 |
2.73e-32 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 122.35 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 19 YNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMSGLVESGVGTGWTVYPPL* 98
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 99 SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LLLLSLPVLAGAITMLLTDR 178
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|.
gi 1950492001 179 NLNTSFFDPAGGGDPILYQHL 199
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-200 |
8.73e-32 |
|
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: 120.73 E-value: 8.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 1 IIRAELGQPGTLIGNDQIYNVVVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNN*SFWLLPPSLTLLLMS 80
Cdd:TIGR02882 74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950492001 81 GLVESGVGTGWTVYPPL*SAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMMMDQMPLFVWAVFITA*LL 160
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLII 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1950492001 161 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 200
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|