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Conserved domains on  [gi|365776566|gb|AEW91688|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Fergusonina taylori]

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 ...
 1-220 8.85e-159

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: 448.93  E-value: 8.85e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFPIQ 220
Cdd:MTH00153 426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLN 485
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 8.85e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 448.93  E-value: 8.85e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFPIQ 220
Cdd:MTH00153 426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLN 485
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-219 5.40e-138

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: 395.31  E-value: 5.40e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:cd01663  259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:cd01663  339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFPI 219
Cdd:cd01663  419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-213 9.56e-82

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 253.13  E-value: 9.56e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:COG0843  269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:COG0843  349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 365776566 161 QHFLGLAGMPRRYSDYP--DAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQR 213
Cdd:COG0843  429 MHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-215 5.70e-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: 244.83  E-value: 5.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566    1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:TIGR02891 340 FVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFP 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 365776566  161 QHFLGLAGMPRRYSDYPDA--YSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQV 215
Cdd:TIGR02891 420 MHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-193 7.76e-54

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: 178.15  E-value: 7.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566    1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSF-SPAILWSLGFVF 79
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAF 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   80 LFTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFF 159
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 365776566  160 PQHFLGLAGMPRRYS----DYPDAYSLWNIVSSIGSMI 193
Cdd:pfam00115 395 PMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 8.85e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 448.93  E-value: 8.85e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFPIQ 220
Cdd:MTH00153 426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLN 485
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-219 5.40e-138

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: 395.31  E-value: 5.40e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:cd01663  259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:cd01663  339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFPI 219
Cdd:cd01663  419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-217 1.11e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 375.17  E-value: 1.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00167 268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00167 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLF 217
Cdd:MTH00167 428 QHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-218 1.96e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 374.31  E-value: 1.96e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00223 265 FGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFL 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00223 345 FTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFP 424

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFP 218
Cdd:MTH00223 425 QHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWS 482
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-218 8.07e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 372.89  E-value: 8.07e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00116 268 FGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00116 348 FTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFP 218
Cdd:MTH00116 428 QHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQP 485
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-218 1.21e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 367.13  E-value: 1.21e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00142 266 FGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFL 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00142 346 FTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFP 425

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFP 218
Cdd:MTH00142 426 QHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWS 483
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-217 1.67e-114

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 336.47  E-value: 1.67e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00103 268 FGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00103 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLF 217
Cdd:MTH00103 428 QHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-216 5.90e-113

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 332.25  E-value: 5.90e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00007 265 FGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFL 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00007 345 FTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFP 424

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVL 216
Cdd:MTH00007 425 QHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-217 9.22e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 331.89  E-value: 9.22e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00183 268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00183 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLF 217
Cdd:MTH00183 428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-218 1.86e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 328.71  E-value: 1.86e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00037 268 FGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00037 348 FTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVLFP 218
Cdd:MTH00037 428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISP 485
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-216 7.52e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 327.28  E-value: 7.52e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00077 268 FGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00077 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVL 216
Cdd:MTH00077 428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVL 483
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-216 8.73e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 303.53  E-value: 8.73e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00079 268 FGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00079 348 FTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFP 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVL 216
Cdd:MTH00079 428 LHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVL 483
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-216 6.44e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 291.73  E-value: 6.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00182 270 FGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFL 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00182 350 FTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFP 429

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVL 216
Cdd:MTH00182 430 QHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFI 485
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-212 4.57e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 281.72  E-value: 4.57e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:MTH00184 270 FGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFL 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:MTH00184 350 FTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFP 429

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQ 212
Cdd:MTH00184 430 QHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVRE 481
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-209 1.31e-87

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: 265.93  E-value: 1.31e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:cd00919  255 FGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFL 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:cd00919  335 FTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFP 414

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 365776566 161 QHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESM 209
Cdd:cd00919  415 MHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-213 9.56e-82

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 253.13  E-value: 9.56e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:COG0843  269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:COG0843  349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 365776566 161 QHFLGLAGMPRRYSDYP--DAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQR 213
Cdd:COG0843  429 MHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-215 5.70e-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: 244.83  E-value: 5.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566    1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:TIGR02891 340 FVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFP 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 365776566  161 QHFLGLAGMPRRYSDYPDA--YSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQV 215
Cdd:TIGR02891 420 MHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-208 5.60e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 243.38  E-value: 5.60e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGT--QLSFSPAILWSLGFV 78
Cdd:MTH00026 269 FGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFI 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  79 FLFTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTF 158
Cdd:MTH00026 349 FLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITF 428

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 365776566 159 FPQHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWES 208
Cdd:MTH00026 429 FPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-209 1.35e-74

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: 233.63  E-value: 1.35e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:cd01662  261 FGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVT 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:cd01662  341 FVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFP 420

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 365776566 161 QHFLGLAGMPRRYSDYP--DAYSLWNIVSSIGSMISFLSIIFLIMILWESM 209
Cdd:cd01662  421 MHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-216 1.57e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 233.80  E-value: 1.57e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFS-PAILWSLGFVF 79
Cdd:MTH00048 266 FGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIV 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  80 LFTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFF 159
Cdd:MTH00048 346 LFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFF 425

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 365776566 160 PQHFLGLAGMPRRYSDYPDAYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQVL 216
Cdd:MTH00048 426 PMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-193 7.76e-54

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: 178.15  E-value: 7.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566    1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSF-SPAILWSLGFVF 79
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAF 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   80 LFTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFF 159
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 365776566  160 PQHFLGLAGMPRRYS----DYPDAYSLWNIVSSIGSMI 193
Cdd:pfam00115 395 PMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-208 2.13e-48

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: 167.72  E-value: 2.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566    1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:TIGR02882 304 FGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPN 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:TIGR02882 384 FLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFP 463

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 365776566  161 QHFLGLAGMPRRYSDY--PDAYSLWNIVSSIGSMISFLSIIFLIMILWES 208
Cdd:TIGR02882 464 MYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYS 513
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-214 2.80e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 156.63  E-value: 2.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566   1 FGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQLSFSPAILWSLGFVFL 80
Cdd:PRK15017 311 FGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVT 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  81 FTVGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQMWLK*QFTMMFIGVNLTFFP 160
Cdd:PRK15017 391 FSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMP 470

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 365776566 161 QHFLGLAGMPRRYSDYPD-AYSLWNIVSSIGSMISFLSIIFLIMILWESMISQRQ 214
Cdd:PRK15017 471 LYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQ 525
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 50-209 5.43e-13

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: 66.93  E-value: 5.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566  50 GIKIFSWLATFHGTQLSFSPAILWSLGFVFlftvGGLTGVILANSSLDIILHDTYYVVAHFHyvLSMGAVFAIMAGFIHW 129
Cdd:cd01660  309 GKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFMAVAY 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365776566 130 Y--PLFTGLTLNQMWL-K*QFTMMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----SLWNIVSSIGSMISFLSII 199
Cdd:cd01660  383 WlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGA 462

                        170
                 ....*....|
gi 365776566 200 FLIMILWESM 209
Cdd:cd01660  463 LFLYILFRTL 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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