|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
1.22e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 473.97 E-value: 1.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00153 220 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00153 300 RAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVL 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00153 380 SMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP 442
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-223 |
9.12e-165 |
|
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: 463.49 E-value: 9.12e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:cd01663 213 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:cd01663 293 RAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVL 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:cd01663 373 SMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYP 435
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-223 |
1.97e-111 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 329.40 E-value: 1.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:COG0843 224 PAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:COG0843 303 KAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:COG0843 383 IGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYP 445
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-223 |
2.55e-110 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 325.33 E-value: 2.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:TIGR02891 215 PARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:TIGR02891 294 LAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:TIGR02891 374 VGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYP 436
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-221 |
2.32e-79 |
|
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: 244.02 E-value: 2.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKW-DPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYV 159
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2410970676 160 LSMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSD 221
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
1.22e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 473.97 E-value: 1.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00153 220 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00153 300 RAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVL 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00153 380 SMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP 442
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-223 |
9.12e-165 |
|
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: 463.49 E-value: 9.12e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:cd01663 213 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:cd01663 293 RAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVL 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:cd01663 373 SMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYP 435
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
4.98e-164 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 462.64 E-value: 4.98e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00116 222 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00116 302 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00116 382 SMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 444
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
6.30e-160 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 452.21 E-value: 6.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00167 222 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00167 302 RAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00167 382 SMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYP 444
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
5.96e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 424.00 E-value: 5.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00223 219 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDT 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00223 299 RAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVL 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00223 379 SMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYP 441
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
2.50e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 414.89 E-value: 2.50e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00142 220 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00142 300 RAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVL 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00142 380 SMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYP 442
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-223 |
9.02e-144 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 411.20 E-value: 9.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00103 222 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00103 302 RAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00103 382 SMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYP 444
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
1.43e-142 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 408.16 E-value: 1.43e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00183 222 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00183 302 RAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00183 382 SMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYP 444
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
5.16e-142 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 406.63 E-value: 5.16e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00077 222 PAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00077 302 RAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00077 382 SMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYP 444
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
3.10e-134 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 386.88 E-value: 3.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00037 222 PAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00037 302 RAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00037 382 SMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYP 444
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-223 |
5.68e-130 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 375.78 E-value: 5.68e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00007 219 PAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDT 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00007 299 RAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVL 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00007 379 SMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYP 441
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
1.16e-121 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 354.76 E-value: 1.16e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00079 222 PSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00079 302 RAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00079 382 SLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYP 444
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
3.59e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 346.42 E-value: 3.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00182 224 PAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00182 304 RAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVL 383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00182 384 SMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFA 446
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
2.80e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 341.42 E-value: 2.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00184 224 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:MTH00184 304 RAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVL 383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00184 384 SMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFH 446
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-223 |
8.56e-112 |
|
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: 327.95 E-value: 8.56e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:cd00919 210 PAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDT 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:cd00919 289 RAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:cd00919 369 SGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYP 431
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-223 |
1.97e-111 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 329.40 E-value: 1.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:COG0843 224 PAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:COG0843 303 KAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:COG0843 383 IGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYP 445
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-223 |
2.55e-110 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 325.33 E-value: 2.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:TIGR02891 215 PARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:TIGR02891 294 LAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:TIGR02891 374 VGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYP 436
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-223 |
2.16e-101 |
|
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: 302.58 E-value: 2.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:cd01662 216 NALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 160
Cdd:cd01662 295 NAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVL 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 161 SMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:cd01662 375 IGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYL 437
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-223 |
8.18e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 296.92 E-value: 8.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00026 223 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGG--TIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHY 158
Cdd:MTH00026 303 RAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHF 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2410970676 159 VLSMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP 223
Cdd:MTH00026 383 VLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYP 447
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-222 |
1.68e-96 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 290.43 E-value: 1.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:MTH00048 220 PLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHG-GTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYV 159
Cdd:MTH00048 300 AVFFSSVTMIIGVPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYV 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2410970676 160 LSMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDY 222
Cdd:MTH00048 380 LSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVY 442
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-221 |
2.32e-79 |
|
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: 244.02 E-value: 2.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 1 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDT 80
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 81 RAYFTSATMIIAIPTGIKVFSWLATLHGGTIKW-DPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYV 159
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2410970676 160 LSMGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSD 221
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-222 |
4.88e-73 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 233.41 E-value: 4.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 2 AGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKKEpFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTR 81
Cdd:TIGR02843 266 EAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVN 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 82 AYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLS 161
Cdd:TIGR02843 345 AFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVII 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2410970676 162 MGAVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDY 222
Cdd:TIGR02843 425 GGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHY 485
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
4-220 |
1.04e-61 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 203.63 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 4 GGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAY 83
Cdd:PRK15017 269 GGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAF 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 84 FTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPLLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMG 163
Cdd:PRK15017 348 FGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGG 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2410970676 164 AVFAILAGLTHWFPLFTGYTLNQSWAKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYS 220
Cdd:PRK15017 428 VVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
6-223 |
2.77e-15 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 73.86 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 6 DPILYQHLFWFFGHPEVYILILPGFGIISHVVAYHAGKK---EPFGYMGMVWAMLsigfLGFIVWAHHMFT-VGMDVDTR 81
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLL----FSTPVGFHHQFAdPGIGPGWK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 82 AYFTSATMIIAIPTGIKVFSWLATL-HGGTIK-------------WDPPLLWALGF-IFLFTIGGLTGIVLANSSLDIAL 146
Cdd:cd01660 276 FIHMVLTFMVALPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410970676 147 HDTYYVVAHFHyvLSMGAVFAILA-GLTHWF-PLFTGYTLNQSW-AKAHFGVMFTGVNLTFFPQHFLGLAGMPRR--YSD 221
Cdd:cd01660 356 HNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQ 433
|
..
gi 2410970676 222 YP 223
Cdd:cd01660 434 YG 435
|
|
|