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Conserved domains on  [gi|1576636044|gb|RZO84883|]
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cytochrome c oxidase subunit I, partial [OM182 bacterium]

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 ...
 1-147 8.98e-80

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 244.31  E-value: 8.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:cd01663   342 GGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHF 421

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWEGAKGLEWTL 147
Cdd:cd01663   422 LGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSLEWTL 488
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-147 8.98e-80

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: 244.31  E-value: 8.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:cd01663   342 GGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHF 421

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWEGAKGLEWTL 147
Cdd:cd01663   422 LGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-166 1.72e-77

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 239.64  E-value: 1.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:COG0843   352 GGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHI 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQ--FADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWeGAKGLEWTLPSPAPYHSFTH 158
Cdd:COG0843   432 LGLLGMPRRYATYPPEpgWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPW-GARTLEWATPSPPPLYNFAS 510


                  ....*...
gi 1576636044 159 PPVVKDEE 166
Cdd:COG0843   511 IPVVRSRD 518
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-156 8.47e-74

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: 229.42  E-value: 8.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1576636044  81 SGLAGMPRRIPDYPLQ--FADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWeGAKGLEWTLPSPAPYHSF 156
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPW-GATTLEWTTSSPPPAHNF 499
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-163 1.49e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 171.78  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00167  351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSwEGAKGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00167  431 LGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVE-LTSTNVEWLHGCPPPHHTWEEPP 509


                  ...
gi 1576636044 161 VVK 163
Cdd:MTH00167  510 FVQ 512
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-110 4.41e-44

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: 150.42  E-value: 4.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:pfam00115 319 GGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHI 398

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1576636044  81 SGLAGMPRRIPDYPL----QFADFNMISSVGAFI 110
Cdd:pfam00115 399 LGLLGMPRRYAPPFIetvpAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-147 8.98e-80

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: 244.31  E-value: 8.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:cd01663   342 GGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHF 421

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWEGAKGLEWTL 147
Cdd:cd01663   422 LGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-166 1.72e-77

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 239.64  E-value: 1.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:COG0843   352 GGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHI 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQ--FADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWeGAKGLEWTLPSPAPYHSFTH 158
Cdd:COG0843   432 LGLLGMPRRYATYPPEpgWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPW-GARTLEWATPSPPPLYNFAS 510


                  ....*...
gi 1576636044 159 PPVVKDEE 166
Cdd:COG0843   511 IPVVRSRD 518
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-156 8.47e-74

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: 229.42  E-value: 8.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1576636044  81 SGLAGMPRRIPDYPLQ--FADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWeGAKGLEWTLPSPAPYHSF 156
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPW-GATTLEWTTSSPPPAHNF 499
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-156 1.02e-61

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: 198.19  E-value: 1.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:cd01662   344 GGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHI 423

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1576636044  81 SGLAGMPRRIPDYP--LQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSG-QPAEGRSWeGAKGLEWTLPSPAPYHSF 156
Cdd:cd01662   424 LGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGkRDATGDPW-GARTLEWATSSPPPAYNF 501
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-126 1.26e-59

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: 191.59  E-value: 1.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:cd00919   338 GGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHF 417

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSI 126
Cdd:cd00919   418 LGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-163 1.49e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 171.78  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00167  351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSwEGAKGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00167  431 LGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVE-LTSTNVEWLHGCPPPHHTWEEPP 509


                  ...
gi 1576636044 161 VVK 163
Cdd:MTH00167  510 FVQ 512
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-162 4.31e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 165.04  E-value: 4.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00153  349 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHF 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGrSWEGAKGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00153  429 LGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF-SLNLSSSIEWLQNLPPAEHSYSELP 507


                  ..
gi 1576636044 161 VV 162
Cdd:MTH00153  508 LL 509
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-162 1.33e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 161.41  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00116  351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVI---IKSIRSGQPAEGRSwegaKGLEWTLPSPAPYHSFT 157
Cdd:MTH00116  431 LGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIweaFSSKRKVLQPELTT----TNIEWIHGCPPPYHTFE 506


                  ....*
gi 1576636044 158 HPPVV 162
Cdd:MTH00116  507 EPAFV 511
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-162 1.24e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 153.82  E-value: 1.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00182  353 GGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHF 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEG---RSWEGAKGLEWTLPSPAPYHSFT 157
Cdd:MTH00182  433 LGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGwkeGTGESWASLEWVHSSPPLFHTYN 512


                  ....*
gi 1576636044 158 HPPVV 162
Cdd:MTH00182  513 ELPFV 517
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-162 1.27e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 153.44  E-value: 1.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00184  353 GGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHF 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGrsWEGAKG----LEWTLPSPAPYHSF 156
Cdd:MTH00184  433 LGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVG--WVEDSGhypsLEWAQTSPPAHHTY 510


                  ....*.
gi 1576636044 157 THPPVV 162
Cdd:MTH00184  511 NELPYV 516
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-110 4.41e-44

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: 150.42  E-value: 4.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:pfam00115 319 GGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHI 398

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1576636044  81 SGLAGMPRRIPDYPL----QFADFNMISSVGAFI 110
Cdd:pfam00115 399 LGLLGMPRRYAPPFIetvpAFQPLNWIRTIGGVL 432
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-162 5.23e-44

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 151.67  E-value: 5.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00223  348 GGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHF 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAegrSWEGAKG--LEWTLPSPAPYHSFTH 158
Cdd:MTH00223  428 LGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSV---VWSGHLStsLEWDNLLPADFHNNSE 504


                  ....
gi 1576636044 159 PPVV 162
Cdd:MTH00223  505 TGAL 508
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-166 1.68e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 147.76  E-value: 1.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00183  351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWEgAKGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00183  431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELT-STNVEWLHGCPPPYHTFEEPA 509


                  ....*.
gi 1576636044 161 VVKDEE 166
Cdd:MTH00183  510 FVQVQS 515
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-163 2.38e-41

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 144.64  E-value: 2.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00103  351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSwEGAKGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00103  431 LGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVE-LTTTNLEWLHGCPPPYHTFEEPT 509


                  ...
gi 1576636044 161 VVK 163
Cdd:MTH00103  510 YVK 512
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-162 3.15e-41

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 144.48  E-value: 3.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00142  349 GGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHF 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWeGAKGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00142  429 LGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSH-LSTSLEWSHRLPPDFHTYDELP 507


                  ..
gi 1576636044 161 VV 162
Cdd:MTH00142  508 IL 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-159 3.65e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 141.62  E-value: 3.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00077  351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHF 430

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWEgAKGLEWTLPSPAPYHSFTHP 159
Cdd:MTH00077  431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELT-STNIEWLHGCPPPYHTFEEP 508
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-162 4.89e-39

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 138.42  E-value: 4.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00037  351 GGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSwEGAKGLEWTLPS-PAPYHSFTHP 159
Cdd:MTH00037  431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPE-FSSSSLEWQYSSfPPSHHTFDET 509


                  ...
gi 1576636044 160 PVV 162
Cdd:MTH00037  510 PST 512
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-162 1.17e-38

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 137.34  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00007  348 GGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHF 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWEGAkGLEWTLPSPAPYHSFTHPP 160
Cdd:MTH00007  428 LGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSS-SLEWQDTLPLDFHNLPETG 506


                  ..
gi 1576636044 161 VV 162
Cdd:MTH00007  507 II 508
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-162 3.70e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 136.30  E-value: 3.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00026  354 GGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHF 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGRSWegAKG--------------LEWT 146
Cdd:MTH00026  434 LGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPFDINIM--AKGplipfscqpahfdtLEWS 511

                         170
                  ....*....|....*.
gi 1576636044 147 LPSPAPYHSFTHPPVV 162
Cdd:MTH00026  512 LTSPPEHHTYNELPYI 527
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-128 4.74e-37

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 132.88  E-value: 4.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00079  351 GGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHF 430

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRS 128
Cdd:MTH00079  431 AGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFS 478
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-164 4.00e-34

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: 125.94  E-value: 4.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:TIGR02843 393 GGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYI 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIPDY-PLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRS---GQPAEGRSWeGAKGLEWTLPSPAPYHSF 156
Cdd:TIGR02843 473 LGFMGMTRRLNHYdNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDrdqNRDTTGDPW-GGRTLEWSTSSPPPFYNF 551


                  ....*...
gi 1576636044 157 THPPVVKD 164
Cdd:TIGR02843 552 AVIPKVQD 559
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-155 4.99e-30

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 114.00  E-value: 4.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:MTH00048  350 GGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHY 429

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1576636044  81 SGLAGMPRRIPDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEGrSWEGAKGLEWTLPSPAPYHS 155
Cdd:MTH00048  430 FGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG-LWGSSSCVVNVLMSPVPYHN 503
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-166 3.24e-26

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 103.86  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGKMYDETLGKIHFWLSFVGVNVTFFPQHF 80
Cdd:PRK15017  394 GGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYA 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  81 SGLAGMPRRIP-DYPLQFADFNMISSVGAFIFG---LSQVFFLYVIIKSIRSGQPAEGRSWeGAKGLEWTLPSPAPYHSF 156
Cdd:PRK15017  474 LGFMGMTRRLSqQIDPQFHTMLMIAASGAALIAlgiLCQVIQMYVSIRDRDQNRDLTGDPW-GGRTLEWATSSPPPFYNF 552

                         170
                  ....*....|
gi 1576636044 157 THPPVVKDEE 166
Cdd:PRK15017  553 AVVPHVHERD 562
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-127 8.31e-15

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 70.78  E-value: 8.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   1 GGFSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPKWTGK-MYDETLGKIHFWLSFVGVNVTFFPQH 79
Cdd:cd01660   339 GGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGReLAAKRLALAQPWLWFVGMTIMSTAMH 418

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1576636044  80 FSGLAGMPRRI-------PDYPLQFADFNMISSVGAFIFGLSQVFFLYVIIKSIR 127
Cdd:cd01660   419 VAGLLGAPRRTaeaqyggLPAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
PRK14485 PRK14485
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
 3-134 1.96e-07

putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional


Pssm-ID: 184703 [Multi-domain]  Cd Length: 712  Bit Score: 49.69  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   3 FSGLMLAITPVDYQYHDTYFVVAHFHYvlvpGAL----FSIIAAVYFWFPK-WTGKMYDETLGKIHFWLSFVGVNVTFFP 77
Cdd:PRK14485  321 FEGPMLSLKNVNAIAHYTDWIIAHVHV----GALgwngFLTFGMLYWLLPRlFKTKLYSTKLANFHFWIGTLGIILYALP 396

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044  78 QHFSGL--AGMPRRI-PDYPLQFADF----------NMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAEG 134
Cdd:PRK14485  397 MYVAGFtqGLMWKEFtPDGTLAYPNFletvlairpmYWMRAIGGSLYLVGMIVMAYNIIKTVRAGSAVEN 466
PRK14488 PRK14488
cbb3-type cytochrome c oxidase subunit I; Provisional
 3-133 2.92e-06

cbb3-type cytochrome c oxidase subunit I; Provisional


Pssm-ID: 237726  Cd Length: 473  Bit Score: 46.05  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   3 FSGLMLAITPVDYQYHDTYFVVAHFHyvlvPGAL----FSIIAAVYFWFPKWTGK--MYDETLGKIHFWLSFVGVNVTFF 76
Cdd:PRK14488  321 FEGPMMSIKTVNALSHYTDWTIGHVH----SGALgwvgMISIGALYHLIPRLWGRerMYSLKLVNWHFWLATIGIVLYIA 396

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1576636044  77 PQHFSGLAG--MPRRIPDY---PLQFAD-------FNMISSVGAFIFGLSQVFFLYVIIKSIRSGQPAE 133
Cdd:PRK14488  397 SMWVAGIMQglMWRAVDEDgtlTYSFVEtveamhpYYVIRALGGLLFLSGMLIMAYNVWKTIRAGKALP 465
cbb3_Oxidase_I cd01661
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the ...
 3-83 1.77e-05

Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the respiratory chains of proteobacteria, is a multi-chain transmembrane protein located in the cell membrane. Like other cytochrome oxidases, it catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Found mainly in proteobacteria, cbb3 is believed to be a modern enzyme that has evolved independently to perform a specialized function in microaerobic energy metabolism. 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 to the binuclear center. The cbb3 operon contains four genes (ccoNOQP or fixNOQP), with ccoN coding for subunit I. Instead of a CuA-containing subunit II analogous to other cytochrome oxidases, cbb3 utilizes subunits ccoO and ccoP, which contain one and two hemes, respectively, to transfer electrons to the binuclear center. The fourth subunit (ccoQ) has been shown to protect the core complex from proteolytic degradation by serine proteases. 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. The polar residues that form the D- and K-pathways in subunit I of other cytochrome c and ubiquinol oxidases are absent in cbb3. The proton pathways remain undefined. A pathway for the transfer of pumped protons beyond the binuclear center also remains undefined. It is believed that electrons are passed from cytochrome c (the electron donor) to the low-spin heme via ccoP and ccoO, respectively, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238831  Cd Length: 493  Bit Score: 43.88  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636044   3 FSGLMLAITPVDYQYHDTYFVVAHFHYVLVPGALFSIIAAVYFWFPK-WTGKMYDETLGKIHFWLSFVGVNVTFFPQHFS 81
Cdd:cd01661   357 FEGSFMAIRAVNSLSHYTDWTVGHVHLGALGWVGFITFGAIYFLVPRiWKREWPSPKLVEWHFWLATIGIVIYFVAMWIS 436


                  ..
gi 1576636044  82 GL 83
Cdd:cd01661   437 GI 438
 
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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