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Conserved domains on  [gi|2095906925|gb|UAW21659|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Clausilocola apostropha]

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 ...
 144-259 7.66e-24

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 cd00919:

Pssm-ID: 469701  Cd Length: 463  Bit Score: 99.53  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 144 GWTFITPFSSNLKYTGIGSqDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITPI 223
Cdd:cd00919   113 GWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMT--LDKMPLFVWSVLVTAILLLLALPV 189

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2095906925 224 LGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:cd00919   190 LAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 144-259 7.66e-24

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: 99.53  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 144 GWTFITPFSSNLKYTGIGSqDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITPI 223
Cdd:cd00919   113 GWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMT--LDKMPLFVWSVLVTAILLLLALPV 189

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2095906925 224 LGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:cd00919   190 LAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
142-259 1.53e-20

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 90.19  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 142 TSGWTFITPFSSNLKYTGIGsQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIIT 221
Cdd:COG0843   125 DVGWTFYPPLSGLEASPGVG-VDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR--MPLFTWAALVTSILILLAF 201

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2095906925 222 PILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:COG0843   202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 143-259 2.65e-19

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 86.57  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGIgSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLrNRKFLLPF---ITISTFLALRMLai 219
Cdd:MTH00223  121 TGWTVYPPLSSNLAHAGP-SVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM-QLERLPLFvwsVKVTAFLLLLSL-- 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2095906925 220 itPILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00223  197 --PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 234
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 142-259 8.56e-10

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: 58.35  E-value: 8.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 142 TSGWTFitpfssnlkYTGIGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKFLLPFITISTFLalrMLAIIT 221
Cdd:pfam00115 106 TTGWTE---------YPPLVGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAI---LILLAF 173

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2095906925 222 PILGASMIMIIFDRHWQTSffeyayGGDPILSQHLFWF 259
Cdd:pfam00115 174 PVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWW 205
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 144-259 7.66e-24

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: 99.53  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 144 GWTFITPFSSNLKYTGIGSqDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITPI 223
Cdd:cd00919   113 GWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITTILNMRAPGMT--LDKMPLFVWSVLVTAILLLLALPV 189

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2095906925 224 LGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:cd00919   190 LAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
142-259 1.53e-20

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 90.19  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 142 TSGWTFITPFSSNLKYTGIGsQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIIT 221
Cdd:COG0843   125 DVGWTFYPPLSGLEASPGVG-VDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR--MPLFTWAALVTSILILLAF 201

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2095906925 222 PILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:COG0843   202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 143-259 2.65e-19

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 86.57  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGIgSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLrNRKFLLPF---ITISTFLALRMLai 219
Cdd:MTH00223  121 TGWTVYPPLSSNLAHAGP-SVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM-QLERLPLFvwsVKVTAFLLLLSL-- 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2095906925 220 itPILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00223  197 --PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 234
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 144-259 8.57e-19

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: 85.23  E-value: 8.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 144 GWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIITPI 223
Cdd:cd01663   116 GWTVYPPLSSILAHSG-PSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK--MPLFVWSVLITAFLLLLSLPV 192

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2095906925 224 LGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:cd01663   193 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 143-259 1.10e-18

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 84.73  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITP 222
Cdd:MTH00167  124 TGWTVYPPLAGNLAHAG-ASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGIT--QYQTPLFVWSILVTTILLLLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00167  201 VLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 143-259 1.97e-17

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 81.31  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGIST---TISFTNLLITRRTLSMPGLRnrkflLPFITISTFLALRMLAI 219
Cdd:MTH00142  122 TGWTVYPPLSSNLAHSG-GSVDLAIFSLHLAGVSSilgAINFITTVINMRAGGMKFER-----VPLFVWSVKITAILLLL 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2095906925 220 ITPILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00142  196 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 235
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 143-259 2.14e-17

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 81.29  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITrrTLSMPGLRNRKFLLPFITISTFLALRMLAIITP 222
Cdd:MTH00116  124 TGWTVYPPLAGNLAHAG-ASVDLAIFSLHLAGVSSILGAINFITT--CINMKPPAMSQYQTPLFVWSVLITAVLLLLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00116  201 VLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 143-259 1.48e-16

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 78.81  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITP 222
Cdd:MTH00183  124 TGWTVYPPLAGNLAHAG-ASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAIS--QYQTPLFVWAVLITAVLLLLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00183  201 VLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 143-259 5.24e-16

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 76.90  E-value: 5.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITrrTLSMPGLRNRKFLLPFITISTFLALRMLAIITP 222
Cdd:MTH00077  124 TGWTVYPPLAGNLAHAG-ASVDLTIFSLHLAGVSSILGAINFITT--SINMKPPSMSQYQTPLFVWSVLITAVLLLLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00077  201 VLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWF 237
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 143-259 6.39e-16

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 76.84  E-value: 6.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITP 222
Cdd:MTH00103  124 TGWTVYPPLAGNLAHAG-ASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMS--QYQTPLFVWSVLITAVLLLLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00103  201 VLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 143-259 7.46e-16

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 76.41  E-value: 7.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIITP 222
Cdd:MTH00037  124 TGWTIYPPLSSNIAHAG-GSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDR--LPLFVWSVFITAFLLLLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00037  201 VLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 143-259 8.79e-16

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 76.40  E-value: 8.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIITP 222
Cdd:MTH00184  126 TGWTVYPPLSSIQAHSG-GSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDR--MPLFVWSILVTTFLLLLSLP 202

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00184  203 VLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 144-259 9.84e-16

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 76.25  E-value: 9.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 144 GWTFITPFSSNLKYTGIGSqDILILSVIFAGISTTISFTNLLITRRTLSMpglrNRKFLLPFITISTFLALRMLAIIT-P 222
Cdd:MTH00048  124 GWTFYPPLSSSLFSSSWGV-DFLMFSLHLAGVSSLFGSINFICTIYSAFM----TNVFSRTSIILWSYLFTSILLLLSlP 198

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00048  199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 143-259 1.96e-15

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: 75.31  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGIGSqDILILSVIFAGISTTISFTNLLITRRTLSMPGLRnrKFLLPFITISTFLALRMLAIITP 222
Cdd:cd01662   118 AGWFAYPPLSGLEYSPGVGV-DYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT--LMRMPIFTWTTLVTSILILFAFP 194

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:cd01662   195 VLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWI 231
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 143-259 2.53e-15

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 74.90  E-value: 2.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGIST---TISFTNLLITRRTLSMPGLRnrkflLPFITISTFLALRMLAI 219
Cdd:MTH00153  122 TGWTVYPPLSSNIAHSG-ASVDLAIFSLHLAGISSilgAINFITTIINMRSKGMTLDR-----MPLFVWSVLITAILLLL 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2095906925 220 ITPILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00153  196 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 143-259 4.02e-15

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 74.66  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIITP 222
Cdd:MTH00026  125 TGWTVYPPLASIQAHSG-GSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSR--IPLFVWSVFITAILLLLSLP 201

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00026  202 VLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 143-259 2.30e-14

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 72.16  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSNLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIITP 222
Cdd:MTH00182  126 TGWTVYPPLSSIQAHSG-GAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNR--LPLFVWSILITAFLLLLSLP 202

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00182  203 VLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWF 239
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 143-259 3.15e-13

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 68.94  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 143 SGWTFITPFSSnLKYTGiGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKflLPFITISTFLALRMLAIITP 222
Cdd:MTH00079  125 TSWTVYPPLST-LGHPG-SSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEH--MSLFVWTVFVTVFLLVLSLP 200

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2095906925 223 ILGASMIMIIFDRHWQTSFFEYAYGGDPILSQHLFWF 259
Cdd:MTH00079  201 VLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 142-259 8.56e-10

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: 58.35  E-value: 8.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095906925 142 TSGWTFitpfssnlkYTGIGSQDILILSVIFAGISTTISFTNLLITRRTLSMPGLRNRKFLLPFITISTFLalrMLAIIT 221
Cdd:pfam00115 106 TTGWTE---------YPPLVGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAI---LILLAF 173

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2095906925 222 PILGASMIMIIFDRHWQTSffeyayGGDPILSQHLFWF 259
Cdd:pfam00115 174 PVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWW 205
 
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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