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Conserved domains on  [gi|226441790|gb|ACO57497|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Amphiacusta mythica]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-211 4.82e-154

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.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 436.61  E-value: 4.82e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00153 285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDII 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00153 365 LHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQS 211
Cdd:MTH00153 445 YTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQN 495
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-211 4.82e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 436.61  E-value: 4.82e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00153 285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDII 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00153 365 LHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQS 211
Cdd:MTH00153 445 YTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQN 495
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 1.09e-130

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 376.44  E-value: 1.09e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:cd01663  278 VWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:cd01663  358 LHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDA 437

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTF-PLNLASSLEW 208
Cdd:cd01663  438 YAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 2.35e-83

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 256.98  E-value: 2.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:COG0843  288 VWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQ 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP-- 158
Cdd:COG0843  368 VHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpe 447

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226441790 159 DAYTSWNMLSSLGSTISLIGILMLIFIVWESMIS-KRQSTFPLNlASSLEWYQSS 212
Cdd:COG0843  448 PGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKgPKAGGNPWG-ARTLEWATPS 501
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-212 1.02e-79

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: 246.37  E-value: 1.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790    1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:TIGR02891 279 VWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQ 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:TIGR02891 359 LHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQ 438

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 226441790  161 --YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQSS 212
Cdd:TIGR02891 439 mgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSS 492
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-174 1.24e-55

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: 182.39  E-value: 1.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790    1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLS-YSPALLWSLGFVFLFTIGGLTGIVLANSSIDI 79
Cdd:pfam00115 254 VWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNY 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   80 ILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYS---- 155
Cdd:pfam00115 334 YVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfi 413

                         170
                  ....*....|....*....
gi 226441790  156 DYPDAYTSWNMLSSLGSTI 174
Cdd:pfam00115 414 ETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-211 4.82e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 436.61  E-value: 4.82e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00153 285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDII 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00153 365 LHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQS 211
Cdd:MTH00153 445 YTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQN 495
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-208 1.09e-130

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 376.44  E-value: 1.09e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:cd01663  278 VWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:cd01663  358 LHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDA 437

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTF-PLNLASSLEW 208
Cdd:cd01663  438 YAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-208 5.40e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 360.06  E-value: 5.40e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00223 284 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIM 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00223 364 LHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDC 443

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEW 208
Cdd:MTH00223 444 YTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-210 6.44e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 360.18  E-value: 6.44e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00116 287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00116 367 LHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDA 446

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQ 210
Cdd:MTH00116 447 YTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIH 496
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-211 9.06e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 354.41  E-value: 9.06e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00142 285 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVV 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00142 365 LHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQS 211
Cdd:MTH00142 445 YTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHR 495
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-208 1.52e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 353.98  E-value: 1.52e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00167 287 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00167 367 LHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEW 208
Cdd:MTH00167 447 YTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEW 494
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-212 8.32e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 321.78  E-value: 8.32e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00037 287 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00037 367 LHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 446

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQSS 212
Cdd:MTH00037 447 YTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSS 498
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-208 2.31e-108

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 320.29  E-value: 2.31e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00103 287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00103 367 LHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDA 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEW 208
Cdd:MTH00103 447 YTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEW 494
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-208 6.15e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 311.45  E-value: 6.15e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00007 284 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDII 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00007 364 LHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDA 443

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEW 208
Cdd:MTH00007 444 YTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEW 491
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-208 7.35e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 311.49  E-value: 7.35e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00077 287 VWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00077 367 LHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEW 208
Cdd:MTH00077 447 YTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEW 494
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-208 3.44e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 309.93  E-value: 3.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00183 287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00183 367 LHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEW 208
Cdd:MTH00183 447 YTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEW 494
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-194 1.40e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 279.64  E-value: 1.40e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00079 287 VWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDII 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00079 367 LHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDV 446

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKR 194
Cdd:MTH00079 447 YSVWNVISSYGSMISVFALFLFIYVLLESFFSYR 480
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-212 3.38e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 274.39  E-value: 3.38e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00182 289 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIV 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00182 369 LHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADA 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQ----STFPLNLASSLEWYQSS 212
Cdd:MTH00182 449 FAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKfigwKEGTGESWASLEWVHSS 504
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-190 6.66e-88

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: 266.32  E-value: 6.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:cd00919  274 VWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIV 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:cd00919  354 LHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDG 433

                        170       180       190
                 ....*....|....*....|....*....|
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESM 190
Cdd:cd00919  434 FAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-212 1.75e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 264.38  E-value: 1.75e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:MTH00184 289 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVV 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:MTH00184 369 LHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDS 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226441790 161 YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLN---LASSLEWYQSS 212
Cdd:MTH00184 449 FAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVEdsgHYPSLEWAQTS 503
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-212 2.35e-83

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 256.98  E-value: 2.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:COG0843  288 VWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQ 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP-- 158
Cdd:COG0843  368 VHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpe 447

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226441790 159 DAYTSWNMLSSLGSTISLIGILMLIFIVWESMIS-KRQSTFPLNlASSLEWYQSS 212
Cdd:COG0843  448 PGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKgPKAGGNPWG-ARTLEWATPS 501
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-212 1.02e-79

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: 246.37  E-value: 1.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790    1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:TIGR02891 279 VWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQ 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:TIGR02891 359 LHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQ 438

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 226441790  161 --YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTFPLNLASSLEWYQSS 212
Cdd:TIGR02891 439 mgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSS 492
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-212 1.33e-71

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: 225.54  E-value: 1.33e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:cd01662  280 VWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQ 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP-- 158
Cdd:cd01662  360 VHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpg 439

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226441790 159 DAYTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQSTF--PLNlASSLEWYQSS 212
Cdd:cd01662  440 PGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATgdPWG-ARTLEWATSS 494
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-204 3.19e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 225.66  E-value: 3.19e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGS--QLSYSPALLWSLGFVFLFTIGGLTGIVLANSSID 78
Cdd:MTH00026 288 VWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLD 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  79 IILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP 158
Cdd:MTH00026 368 ILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYP 447

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226441790 159 DAYTSWNMLSSLGSTISLIGILMLIFIVWESMIskRQSTFPLNLAS 204
Cdd:MTH00026 448 DNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--REEPFDINIMA 491
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-194 4.43e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 216.85  E-value: 4.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYS-PALLWSLGFVFLFTIGGLTGIVLANSSIDI 79
Cdd:MTH00048 285 VWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDN 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  80 ILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPD 159
Cdd:MTH00048 365 VLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEP 444

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226441790 160 AYTSWNMLSSLGSTISLIGILMLIFIVWESMISKR 194
Cdd:MTH00048 445 SYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-174 1.24e-55

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: 182.39  E-value: 1.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790    1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLS-YSPALLWSLGFVFLFTIGGLTGIVLANSSIDI 79
Cdd:pfam00115 254 VWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNY 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   80 ILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYS---- 155
Cdd:pfam00115 334 YVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfi 413

                         170
                  ....*....|....*....
gi 226441790  156 DYPDAYTSWNMLSSLGSTI 174
Cdd:pfam00115 414 ETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-212 1.61e-45

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: 159.63  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790    1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:TIGR02882 323 VWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQ 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDY--P 158
Cdd:TIGR02882 403 YHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspS 482

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226441790  159 DAYTSWNMLSSLGSTISLIGILMLIF-IVWESMISKRQSTFPLNLASSLEWYQSS 212
Cdd:TIGR02882 483 DGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREATGDPWNGRTLEWATAS 537
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-212 8.51e-40

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 143.92  E-value: 8.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790   1 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSYSPALLWSLGFVFLFTIGGLTGIVLANSSIDII 80
Cdd:PRK15017 330 VWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFV 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  81 LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLLTGLMMNPKWLNIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA 160
Cdd:PRK15017 410 LHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDP 489

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226441790 161 -YTSWNMLSSLGSTISLIGILMLIFIVWESMISKRQS---TFPLNLASSLEWYQSS 212
Cdd:PRK15017 490 qFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNrdlTGDPWGGRTLEWATSS 545
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 23-190 2.03e-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: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  23 TMIIAVPTGIKIFSWLATL-------HGSQL-SYSPALLWS----LGFVF---LFTIGGLTGIVLANSSIDIILHDTYYV 87
Cdd:cd01660  282 TFMVALPSLLTAFTVFASLeiagrlrGGKGLfGWIRALPWGdpmfLALFLamlMFIPGGAGGIINASYQLNYVVHNTAWV 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441790  88 VAHFHyvLSMGAVFAIMAGFIHWY--PLLTGLMMNPKWLNI-QFVIMFVGVNLTFFPQHFLGLAGMPRR--YSDYPDAY- 161
Cdd:cd01660  362 PGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPa 439

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226441790 162 ----TSWNMLSSLGSTISLIGILMLIFIVWESM 190
Cdd:cd01660  440 agewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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