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Conserved domains on  [gi|1696031745|gb|QDH09782|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Trichinella pseudospiralis]

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 ...
 1-130 1.12e-74

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 229.68  E-value: 1.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:cd01663   228 FFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPT 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:cd01663   308 GIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-130 1.12e-74

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: 229.68  E-value: 1.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:cd01663   228 FFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPT 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:cd01663   308 GIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-128 3.11e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 218.58  E-value: 3.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00153  235 FFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLD 128
Cdd:MTH00153  315 GIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSID 362
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-129 2.46e-47

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 159.14  E-value: 2.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:COG0843   239 FFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDL 129
Cdd:COG0843   318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDY 366
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-130 8.97e-33

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: 118.83  E-value: 8.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:pfam00115 205 WFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPS 283

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696031745  81 GVKIFSWLATLYGSHIKM-TPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:pfam00115 284 GVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYY 334
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-130 1.12e-74

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: 229.68  E-value: 1.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:cd01663   228 FFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPT 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:cd01663   308 GIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-128 3.11e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 218.58  E-value: 3.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00153  235 FFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLD 128
Cdd:MTH00153  315 GIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSID 362
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-130 6.50e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 212.53  E-value: 6.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00223  234 FFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 313

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00223  314 GIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIM 363
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-130 9.47e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 201.83  E-value: 9.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00079  237 FFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPT 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00079  317 GVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDII 366
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-129 2.04e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 196.05  E-value: 2.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00167  237 FFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 316

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDL 129
Cdd:MTH00167  317 GIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDI 365
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-130 5.32e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 192.23  E-value: 5.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00116  237 FFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPT 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00116  317 GIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIV 366
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-130 6.63e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 189.16  E-value: 6.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00142  235 FFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPT 314

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00142  315 GIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVV 364
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-130 5.79e-55

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 178.92  E-value: 5.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00103  237 FFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPT 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00103  317 GVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIV 366
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-130 1.82e-54

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 177.79  E-value: 1.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00007  234 FFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 313

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00007  314 GIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDII 363
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-129 3.08e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 174.63  E-value: 3.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00037  237 FFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 316

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDL 129
Cdd:MTH00037  317 GIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDV 365
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-130 3.92e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 171.93  E-value: 3.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00182  239 FFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00182  319 GIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIV 368
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-130 4.54e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 171.64  E-value: 4.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00183  237 FFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPT 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00183  317 GVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIV 366
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-130 4.41e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 168.85  E-value: 4.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00184  239 FFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00184  319 GIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVV 368
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-130 1.59e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 167.43  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00077  237 FFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPT 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00077  317 GVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIV 366
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-130 2.39e-48

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: 160.77  E-value: 2.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:cd00919   225 FFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPT 303

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:cd00919   304 GIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIV 353
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-129 2.46e-47

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 159.14  E-value: 2.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:COG0843   239 FFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDL 129
Cdd:COG0843   318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDY 366
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-128 4.06e-46

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: 155.43  E-value: 4.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:cd01662   231 IFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPT 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1696031745  81 GVKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLD 128
Cdd:cd01662   310 GVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPAD 357
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-130 6.83e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 155.56  E-value: 6.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00026  238 FFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPT 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1696031745  81 GVKIFSWLATLYGS--HIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00026  318 GIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDIL 369
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-130 2.83e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 148.29  E-value: 2.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKFKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:MTH00048  235 FFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPT 314

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696031745  81 GVKIFSWLATLYGSHIKMT-PAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:MTH00048  315 GIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNV 365
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-130 8.97e-33

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: 118.83  E-value: 8.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   1 FFGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPT 80
Cdd:pfam00115 205 WFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPS 283

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696031745  81 GVKIFSWLATLYGSHIKM-TPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:pfam00115 284 GVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYY 334
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-130 2.96e-32

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 119.27  E-value: 2.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696031745   2 FGHPEVYILVLPAFGVVSEALMLMSGKfKVFGPLGMIYAMMSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTG 81
Cdd:PRK15017  282 WGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1696031745  82 VKIFSWLATLYGSHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLL 130
Cdd:PRK15017  361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFV 409
 
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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