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Conserved domains on  [gi|10945475|gb|AAG24556|]
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cytochrome oxidase I, partial (mitochondrion) [Basileuterus culicivorus]

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 ...
 1-204 9.31e-146

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: 415.04  E-value: 9.31e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00153 232 LFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00153 312 VPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGF 391

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00153 392 IHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMP 435
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-204 9.31e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 415.04  E-value: 9.31e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00153 232 LFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00153 312 VPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGF 391

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00153 392 IHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMP 435
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-204 3.92e-144

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: 409.95  E-value: 3.92e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:cd01663 225 LFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIA 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:cd01663 305 VPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGF 384

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 10945475 161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:cd01663 385 YYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMP 428
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-204 1.38e-94

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 285.48  E-value: 1.38e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:COG0843 236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIA 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:COG0843 315 VPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGL 394

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 10945475 161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:COG0843 395 YYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMP 438
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-204 3.21e-93

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: 280.65  E-value: 3.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475     1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:TIGR02891 306 VPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAI 385

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 10945475   161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:TIGR02891 386 YYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMP 429
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-204 2.35e-66

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: 209.74  E-value: 2.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475     1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    81 IPTGIKVFSWLATLHGGTIKW-DPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAG 159
Cdd:pfam00115 281 VPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGG 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 10945475   160 FTHWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:pfam00115 361 IYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMP 405
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-204 9.31e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 415.04  E-value: 9.31e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00153 232 LFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00153 312 VPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGF 391

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00153 392 IHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMP 435
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-204 6.74e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 412.95  E-value: 6.74e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00116 234 LFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00116 314 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGF 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00116 394 THWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMP 437
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-204 3.92e-144

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: 409.95  E-value: 3.92e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:cd01663 225 LFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIA 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:cd01663 305 VPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGF 384

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 10945475 161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:cd01663 385 YYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMP 428
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-204 1.18e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 399.82  E-value: 1.18e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00167 234 LFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00167 314 VPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGF 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00167 394 THWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMP 437
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-204 2.81e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 375.85  E-value: 2.81e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00223 231 LFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIA 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00223 311 VPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGF 390

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00223 391 NHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMP 434
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-204 1.82e-127

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 368.83  E-value: 1.82e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00103 234 LFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00103 314 IPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGF 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00103 394 VHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMP 437
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-204 6.67e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 367.13  E-value: 6.67e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00142 232 LFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00142 312 VPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGF 391

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00142 392 IHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMP 435
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-204 3.82e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 365.40  E-value: 3.82e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00183 234 LFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00183 314 IPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAF 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00183 394 VHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMP 437
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-204 1.51e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 363.88  E-value: 1.51e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00077 234 LFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00077 314 IPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGF 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00077 394 VHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMP 437
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-204 1.64e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 346.05  E-value: 1.64e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00037 234 LFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00037 314 VPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGF 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00037 394 THWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMP 437
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-204 3.37e-114

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 334.95  E-value: 3.37e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00007 231 LFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIA 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00007 311 VPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAF 390

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00007 391 NHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMP 434
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-204 4.17e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 308.92  E-value: 4.17e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00079 234 LFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00079 314 VPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGI 393

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00079 394 SLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMP 437
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-204 2.56e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 307.52  E-value: 2.56e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00182 236 LFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00182 316 VPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGF 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00182 396 YYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFP 439
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-204 1.14e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 300.59  E-value: 1.14e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00184 236 LFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:MTH00184 316 VPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGF 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00184 396 YYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLP 439
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-204 1.38e-94

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 285.48  E-value: 1.38e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:COG0843 236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIA 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:COG0843 315 VPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGL 394

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 10945475 161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:COG0843 395 YYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMP 438
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-204 5.68e-94

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: 281.73  E-value: 5.68e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:cd00919 222 LFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIA 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:cd00919 301 VPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGL 380

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 10945475 161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:cd00919 381 YYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMP 424
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-204 3.21e-93

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: 280.65  E-value: 3.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475     1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:TIGR02891 306 VPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAI 385

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 10945475   161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:TIGR02891 386 YYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMP 429
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-204 1.82e-87

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: 265.98  E-value: 1.82e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:cd01662 228 LFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIA 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:cd01662 307 VPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGF 386

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 10945475 161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:cd01662 387 YYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMP 430
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-204 9.66e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 259.95  E-value: 9.66e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00026 235 LFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIA 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGG--TIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILA 158
Cdd:MTH00026 315 VPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFG 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 10945475  159 GFTHWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00026 395 GFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLP 440
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-204 2.68e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 253.06  E-value: 2.68e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:MTH00048 232 MFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIG 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHG-GTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAG 159
Cdd:MTH00048 312 VPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIM 391

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 10945475  160 FTHWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:MTH00048 392 FIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLP 436
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-204 2.35e-66

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: 209.74  E-value: 2.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475     1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIA 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    81 IPTGIKVFSWLATLHGGTIKW-DPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAG 159
Cdd:pfam00115 281 VPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGG 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 10945475   160 FTHWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:pfam00115 361 IYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMP 405
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-203 2.84e-65

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 212.22  E-value: 2.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475     1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKKEpFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:TIGR02843 277 LIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIA 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:TIGR02843 356 IPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGL 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 10945475   161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGM 203
Cdd:TIGR02843 436 TYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGM 478
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-203 1.21e-55

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 186.68  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475    1 LFWFFGHPEVYILILPGFGIISHVVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 80
Cdd:PRK15017 278 LIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIA 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   81 IPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDVALHDTYYVVAHFHYVLSMGAVFAILAGF 160
Cdd:PRK15017 357 IPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGM 436

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 10945475  161 THWFPLFTGYTLHSTWAKAHFGVMFVGVNLTFFPQHFLGLAGM 203
Cdd:PRK15017 437 TYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGM 479
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-204 2.02e-12

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: 65.00  E-value: 2.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475   1 LFWFFGHPEVYILILPGFGIISHVVTYYAGKK---EPFGYMGMVWAMLsigfLGFIVWAHHMFT-VGMDVDTRAYFTSAT 76
Cdd:cd01660 207 LFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLL----FSTPVGFHHQFAdPGIGPGWKFIHMVLT 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10945475  77 MIIAIPTGIKVFSWLATL-HGGTIK-------------WDPPMLWALGF-IFLFTIGGLTGIVLANSSLDVALHDTYYVV 141
Cdd:cd01660 283 FMVALPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVP 362

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10945475 142 AHFHyvLSMGAVFAILA-GFTHWF-PLFTGYTLHSTW-AKAHFGVMFVGVNLTFFPQHFLGLAGMP 204
Cdd:cd01660 363 GHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAP 426
 
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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