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Conserved domains on  [gi|215789235|gb|ACJ69659|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Gorgoderina sp. FLUKE170-08]

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 ...
 1-154 1.28e-77

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 MTH00048:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 238.81  E-value: 1.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   1 FYNIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMIGGAGVGW 80
Cdd:MTH00048  46 YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGW 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215789235  81 TFYPPLSGAGYS-GWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00048 126 TFYPPLSSSLFSsSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVL 200
 
Name Accession Description Interval E-value
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-154 1.28e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 238.81  E-value: 1.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   1 FYNIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMIGGAGVGW 80
Cdd:MTH00048  46 YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGW 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215789235  81 TFYPPLSGAGYS-GWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00048 126 TFYPPLSSSLFSsSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVL 200
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 3-154 1.75e-60

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: 193.85  E-value: 1.75e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   3 NIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGW 80
Cdd:cd01663   38 QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALveGGAGTGW 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215789235  81 TFYPPLSGAGY-SGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:cd01663  118 TVYPPLSSILAhSGPSVDLAIFSLHLAGISSILGAINFITTIFNmRAPGMTLEKMPLFVWSVLITAFLLLLSLPVL 193
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-154 2.98e-38

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 136.03  E-value: 2.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   2 YNIVSPEVYNYVITSHGIAMIFFFLMPvLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVG 79
Cdd:COG0843   49 LGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFvgGAADVG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235  80 WTFYPPLSGAGYS-GWGVDFLMFSLHLAGISSVFGSLNFICTIVS------SLGscnvaRCSIIIWAYLFTSILLIFSLP 152
Cdd:COG0843  128 WTFYPPLSGLEASpGVGVDLWLLGLALFGVGSILGGVNFIVTILKmrapgmTLM-----RMPLFTWAALVTSILILLAFP 202


                 ..
gi 215789235 153 VL 154
Cdd:COG0843  203 VL 204
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-154 1.31e-27

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: 105.73  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235    3 NIVSPEVYNYVITSHGIAMIFFFLMPVlIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMiGGAGVGWTF 82
Cdd:pfam00115  34 NFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF-GGATTGWTE 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215789235   83 YPPLsgagysgWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:pfam00115 112 YPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAILILLAFPVL 176
 
Name Accession Description Interval E-value
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-154 1.28e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 238.81  E-value: 1.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   1 FYNIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMIGGAGVGW 80
Cdd:MTH00048  46 YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGW 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215789235  81 TFYPPLSGAGYS-GWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00048 126 TFYPPLSSSLFSsSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVL 200
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 3-154 1.75e-60

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: 193.85  E-value: 1.75e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   3 NIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGW 80
Cdd:cd01663   38 QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALveGGAGTGW 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215789235  81 TFYPPLSGAGY-SGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:cd01663  118 TVYPPLSSILAhSGPSVDLAIFSLHLAGISSILGAINFITTIFNmRAPGMTLEKMPLFVWSVLITAFLLLLSLPVL 193
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 6-154 2.72e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 157.06  E-value: 2.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   6 SPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGWTFY 83
Cdd:MTH00223  47 DDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAveSGVGTGWTVY 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215789235  84 PPLSGA-GYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00223 127 PPLSSNlAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINmRSPGMQLERLPLFVWSVKVTAFLLLLSLPVL 199
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 9-154 4.37e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 153.87  E-value: 4.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   9 VYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGWTFYPPL 86
Cdd:MTH00153  51 IYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMveSGAGTGWTVYPPL 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  87 SGA-GYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS--SLGsCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00153 131 SSNiAHSGASVDLAIFSLHLAGISSILGAINFITTIINmrSKG-MTLDRMPLFVWSVLITAILLLLSLPVL 200
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 8-154 1.04e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 147.52  E-value: 1.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGWTFYPP 85
Cdd:MTH00167  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGveAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSGA-GYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00167 132 LAGNlAHAGASVDLAIFSLHLAGVSSILGSINFITTIINmKPPGITQYQTPLFVWSILVTTILLLLSLPVL 202
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-154 8.94e-42

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 145.21  E-value: 8.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   3 NIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGW 80
Cdd:MTH00079  48 LLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFvdMGPGTSW 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215789235  81 TFYPPLSGAGYSGWGVDFLMFSLHLAGISSVFGSLNFICT-IVSSLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00079 128 TVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTtKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVL 202
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 8-154 4.70e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 140.63  E-value: 4.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICL--SLSMIGGAGVGWTFYPP 85
Cdd:MTH00142  50 QLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLlsSAAVESGAGTGWTVYPP 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSGAG-YSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00142 130 LSSNLaHSGGSVDLAIFSLHLAGVSSILGAINFITTVINmRAGGMKFERVPLFVWSVKITAILLLLSLPVL 200
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 8-154 5.09e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 140.61  E-value: 5.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPS-SICLSLSMIG-GAGVGWTFYPP 85
Cdd:MTH00116  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSfLLLLASSTVEaGAGTGWTVYPP 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00116 132 LAGnLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINmKPPAMSQYQTPLFVWSVLITAVLLLLSLPVL 202
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-154 2.98e-38

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 136.03  E-value: 2.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   2 YNIVSPEVYNYVITSHGIAMIFFFLMPvLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVG 79
Cdd:COG0843   49 LGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFvgGAADVG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235  80 WTFYPPLSGAGYS-GWGVDFLMFSLHLAGISSVFGSLNFICTIVS------SLGscnvaRCSIIIWAYLFTSILLIFSLP 152
Cdd:COG0843  128 WTFYPPLSGLEASpGVGVDLWLLGLALFGVGSILGGVNFIVTILKmrapgmTLM-----RMPLFTWAALVTSILILLAFP 202


                 ..
gi 215789235 153 VL 154
Cdd:COG0843  203 VL 204
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 6-154 4.51e-38

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 135.41  E-value: 4.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   6 SPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICL--SLSMIGGAGVGWTFY 83
Cdd:MTH00007  47 SDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLvsSAAVEKGVGTGWTVY 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215789235  84 PPLSG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGS-CNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00007 127 PPLASnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKgLRLERIPLFVWAVVITVVLLLLSLPVL 199
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 8-154 7.82e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 134.68  E-value: 7.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICL--SLSMIGGAGVGWTFYPP 85
Cdd:MTH00077  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLlaSSGVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00077 132 LAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINmKPPSMSQYQTPLFVWSVLITAVLLLLSLPVL 202
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 8-154 1.26e-37

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 134.28  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICL--SLSMIGGAGVGWTFYPP 85
Cdd:MTH00183  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLlaSSGVEAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00183 132 LAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINmKPPAISQYQTPLFVWAVLITAVLLLLSLPVL 202
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 8-154 7.54e-37

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 131.93  E-value: 7.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGWTFYPP 85
Cdd:MTH00103  52 QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMveAGAGTGWTVYPP 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00103 132 LAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINmKPPAMSQYQTPLFVWSVLITAVLLLLSLPVL 202
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 3-154 8.41e-37

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: 131.11  E-value: 8.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   3 NIVSPEVYNYVITSHGIAMIFFFLMPVLIGGFGNYlLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGW 80
Cdd:cd00919   36 LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNL-LPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLvgGGAGTGW 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215789235  81 TFYPPLSGAGY-SGWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGS-CNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:cd00919  115 TFYPPLSTLSYsSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPgMTLDKMPLFVWSVLVTAILLLLALPVL 190
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 8-154 3.98e-36

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 129.95  E-value: 3.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICL--SLSMIGGAGVGWTFYPP 85
Cdd:MTH00184  54 HLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLlgSAFVEQGAGTGWTVYPP 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGS-CNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00184 134 LSSiQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPgITMDRMPLFVWSILVTTFLLLLSLPVL 204
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 8-154 1.64e-35

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 128.41  E-value: 1.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   8 EVYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICL--SLSMIGGAGVGWTFYPP 85
Cdd:MTH00037  52 QIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLlaSAGVESGAGTGWTIYPP 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215789235  86 LSGA-GYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLG-SCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00037 132 LSSNiAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTpGMTFDRLPLFVWSVFITAFLLLLSLPVL 202
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 9-154 4.31e-34

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 124.55  E-value: 4.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   9 VYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGWTFYPPL 86
Cdd:MTH00182  55 LYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFveQGAGTGWTVYPPL 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235  87 SG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLG-SCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00182 135 SSiQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRApGVTFNRLPLFVWSILITAFLLLLSLPVL 204
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 5-154 8.10e-32

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: 118.07  E-value: 8.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   5 VSPEVYNYVITSHGIAMIFFFLMPVLIGgFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMIGGAG--VGWTF 82
Cdd:cd01662   44 LSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFpdAGWFA 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215789235  83 YPPLSGAGYS-GWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLG-SCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:cd01662  123 YPPLSGLEYSpGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRApGMTLMRMPIFTWTTLVTSILILFAFPVL 196
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 9-154 1.82e-31

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 117.42  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   9 VYNYVITSHGIAMIFFFLMPVLIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMI--GGAGVGWTFYPPL 86
Cdd:MTH00026  54 LYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLveQGAGTGWTVYPPL 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235  87 SG-AGYSGWGVDFLMFSLHLAGISSVFGSLNFICTIVS-SLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:MTH00026 134 ASiQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNmRTPGMTMSRIPLFVWSVFITAILLLLSLPVL 203
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-154 1.31e-27

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: 105.73  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235    3 NIVSPEVYNYVITSHGIAMIFFFLMPVlIGGFGNYLLPLLLGIADLNLPRLNALSAWLMLPSSICLSLSMiGGAGVGWTF 82
Cdd:pfam00115  34 NFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF-GGATTGWTE 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215789235   83 YPPLsgagysgWGVDFLMFSLHLAGISSVFGSLNFICTIVSSLGSCNVARCSIIIWAYLFTSILLIFSLPVL 154
Cdd:pfam00115 112 YPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAILILLAFPVL 176
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 4-88 6.23e-03

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: 35.72  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215789235   4 IVSPEVYNYVITSHGIAMIFFFLMpVLIGGFGNYLLPLLLGIADLNlPRLNALSAWLMLPSSICLSLSMIGG-AGVGWTF 82
Cdd:cd01660   38 PSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVPILLGqASVLYTF 115


                 ....*.
gi 215789235  83 YPPLSG 88
Cdd:cd01660  116 YPPLQA 121
 
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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