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Conserved domains on  [gi|1169190965|gb|ARB51662|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Barbodes carnaticus]

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 ...
 1-212 2.56e-155

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: 439.69  E-value: 2.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00153  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00153  296 DVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00153  376 HYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQH 427
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 2.56e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 439.69  E-value: 2.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00153  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00153  296 DVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00153  376 HYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQH 427
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 2.04e-152

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: 431.52  E-value: 2.04e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:cd01663   209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:cd01663   289 DVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:cd01663   369 HYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQH 420
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-212 1.49e-101

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 303.59  E-value: 1.49e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   2 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMD 81
Cdd:COG0843   221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGIS 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  82 VDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFH 161
Cdd:COG0843   300 PLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFH 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169190965 162 YVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:COG0843   380 YVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMH 430
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-212 3.90e-99

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: 296.44  E-value: 3.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGM 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:TIGR02891 290 PPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHF 369

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:TIGR02891 370 HYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMH 421
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-212 7.95e-71

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: 221.68  E-value: 7.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   5 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDT 84
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  85 RAYFTSATMIIAIPTGVKVFSWLATLHGGSIKW-ETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYV 163
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169190965 164 LSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMH 397
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 2.56e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 439.69  E-value: 2.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00153  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00153  296 DVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00153  376 HYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQH 427
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-212 1.77e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 432.59  E-value: 1.77e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00116  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00116  298 DVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00116  378 HYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQH 429
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 2.04e-152

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: 431.52  E-value: 2.04e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:cd01663   209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:cd01663   289 DVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:cd01663   369 HYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQH 420
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-212 3.92e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 424.09  E-value: 3.92e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00167  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00167  298 DVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00167  378 HYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQH 429
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-212 1.04e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 397.76  E-value: 1.04e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00183  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00183  298 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00183  378 HYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQH 429
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-212 7.26e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 392.80  E-value: 7.26e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00223  215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGM 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00223  295 DVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHF 374

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00223  375 HYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQH 426
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-212 3.24e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 388.91  E-value: 3.24e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00077  218 TFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00077  298 NVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00077  378 HYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQH 429
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-212 2.90e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 386.39  E-value: 2.90e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00142  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGM 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00142  296 DVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHF 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00142  376 HYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQH 427
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-212 8.69e-134

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 385.00  E-value: 8.69e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00103  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00103  298 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00103  378 HYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQH 429
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-212 6.78e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 362.61  E-value: 6.78e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00037  218 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00037  298 DVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00037  378 HYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQH 429
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-212 1.77e-122

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 356.52  E-value: 1.77e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00007  215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGM 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00007  295 DVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHF 374

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00007  375 HYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQH 426
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-212 6.55e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 326.64  E-value: 6.55e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00079  218 SFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00079  298 DLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00079  378 HYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLH 429
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-212 7.58e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 324.47  E-value: 7.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00182  220 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGM 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00182  300 DVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00182  380 HYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQH 431
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-212 1.59e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 321.01  E-value: 1.59e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00184  220 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGM 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00184  300 DVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00184  380 HYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQH 431
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-212 1.49e-101

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 303.59  E-value: 1.49e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   2 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMD 81
Cdd:COG0843   221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGIS 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  82 VDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFH 161
Cdd:COG0843   300 PLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFH 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169190965 162 YVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:COG0843   380 YVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMH 430
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-212 9.93e-101

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: 299.06  E-value: 9.93e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:cd00919   206 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGL 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:cd00919   285 PVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHF 364

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:cd00919   365 HYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMH 416
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-212 3.90e-99

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: 296.44  E-value: 3.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGM 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:TIGR02891 290 PPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHF 369

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:TIGR02891 370 HYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMH 421
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-212 1.74e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 285.37  E-value: 1.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   1 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 80
Cdd:MTH00026  219 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGM 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  81 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGG--SIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVA 158
Cdd:MTH00026  299 DVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVA 378

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169190965 159 HFHYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00026  379 HFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQH 432
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-212 7.43e-93

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: 280.24  E-value: 7.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   2 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMD 81
Cdd:cd01662   213 FFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAG 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  82 VDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFH 161
Cdd:cd01662   292 ALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFH 371

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169190965 162 YVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:cd01662   372 YVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMH 422
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-212 5.66e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 275.79  E-value: 5.66e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   2 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMD 81
Cdd:MTH00048  217 FFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  82 VDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLL-WALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHF 160
Cdd:MTH00048  297 VKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHF 376

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169190965 161 HYVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:MTH00048  377 HYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMH 428
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-212 7.95e-71

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: 221.68  E-value: 7.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   5 PAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDT 84
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  85 RAYFTSATMIIAIPTGVKVFSWLATLHGGSIKW-ETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYV 163
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169190965 164 LSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMH 397
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 2-210 7.06e-68

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: 219.16  E-value: 7.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   2 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEpFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMD 81
Cdd:TIGR02843 262 FFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAG 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  82 VDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFH 161
Cdd:TIGR02843 341 ANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFH 420

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169190965 162 YVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFP 210
Cdd:TIGR02843 421 NVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMP 469
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-210 5.09e-57

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 190.92  E-value: 5.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965   2 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMD 81
Cdd:PRK15017  263 FFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAG 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  82 VDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFH 161
Cdd:PRK15017  342 ANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFH 421

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1169190965 162 YVLSMGAVFAIMAAFVHWFPLLTGYTLHNAWTKIHFGVMFIGVNLTFFP 210
Cdd:PRK15017  422 NVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMP 470
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 10-212 2.80e-10

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: 58.84  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  10 DPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVwAMMAIGLLGFIVWAHHMFT-VGMDVDTRAYF 88
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169190965  89 TSATMIIAIPTGVKVFSWLATL--------HGGSIKWETPLLW--------ALGFIFlFTVGGLTGIVLSNSSLDIVLHD 152
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169190965 153 TYYVVAHFHyvLSMGAVFAIMA-AFVHWF-PLLTGYTL-HNAWTKIHFGVMFIGVNLTFFPQH 212
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMH 418
 
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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