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Conserved domains on  [gi|1770414070|gb|QFU20296|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Sitophilus oryzae]

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 ...
1-201 3.26e-135

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 388.07  E-value: 3.26e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00153   26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00153  106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00153  186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-201 3.26e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 388.07  E-value: 3.26e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00153   26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00153  106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00153  186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-201 1.92e-124

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: 359.87  E-value: 1.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:cd01663    19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:cd01663    99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:cd01663   179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 3.06e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.61  E-value: 3.06e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
1-196 3.55e-41

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: 144.25  E-value: 3.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSfieKGAGTGWTVYPPLssniahegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWA 160
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWA 161
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPA 196
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
7-201 2.79e-36

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 133.44  E-value: 2.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   7 SLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLL 86
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  87 MSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAI 166
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1770414070 167 LLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMP 265
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-201 3.26e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 388.07  E-value: 3.26e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00153   26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00153  106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00153  186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 226
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-201 1.92e-124

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: 359.87  E-value: 1.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:cd01663    19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:cd01663    99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:cd01663   179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 219
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-201 3.24e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 345.12  E-value: 3.24e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00167   28 MVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00167  108 SLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWS 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00167  188 ILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDP 228
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-201 4.15e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 339.65  E-value: 4.15e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00223   25 LVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00223  105 SLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWS 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00223  185 VKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 225
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-201 1.07e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 335.93  E-value: 1.07e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00142   26 MVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00142  106 ALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWS 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00142  186 VKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDP 226
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-201 1.18e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 335.91  E-value: 1.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00116   28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00116  108 SFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWS 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00116  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-201 2.20e-105

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 312.22  E-value: 2.20e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00007   25 LLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00007  105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWA 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00007  185 VVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP 225
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-201 1.00e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 305.69  E-value: 1.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00183   28 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00183  108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00183  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-201 3.19e-102

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 304.11  E-value: 3.19e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00103   28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00103  108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00103  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-201 9.74e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 303.02  E-value: 9.74e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00077   28 MVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00077  108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00077  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDP 228
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-201 6.05e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 295.97  E-value: 6.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00037   28 MVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00037  108 SFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWS 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00037  188 VFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDP 228
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-201 1.76e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 287.11  E-value: 1.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00184   30 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00184  110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00184  190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-201 2.55e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 286.72  E-value: 2.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00182   30 MIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00182  110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00182  190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 230
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-201 1.91e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 284.27  E-value: 1.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:MTH00079   29 MVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSnIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:MTH00079  109 SLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWT 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00079  188 VFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNP 228
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
2-201 6.71e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.03  E-value: 6.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   2 VGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPS 81
Cdd:MTH00026   30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  82 LTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAV 161
Cdd:MTH00026  110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1770414070 162 SITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00026  190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDP 229
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-201 7.77e-78

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: 240.13  E-value: 7.77e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:cd00919    17 LLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:cd00919    96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWS 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:cd00919   176 VLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDP 216
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 3.06e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.61  E-value: 3.06e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWA 160
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDP 230
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
2-201 1.37e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 207.22  E-value: 1.37e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   2 VGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPS 81
Cdd:MTH00048   30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  82 LTLLLMSSFIekGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGmLSERMTLFIWAV 161
Cdd:MTH00048  110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIILWSY 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1770414070 162 SITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:MTH00048  187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDP 226
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
3-201 1.77e-55

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: 183.17  E-value: 1.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   3 GTSLSLLIRAELGNP-GSLIGNDQiYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPS 81
Cdd:cd01662    25 GGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  82 LTLLLMSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAV 161
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1770414070 162 SITAILLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNP 222
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
1-196 3.55e-41

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: 144.25  E-value: 3.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   1 MVGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPP 80
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  81 SLTLLLMSSfieKGAGTGWTVYPPLssniahegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWA 160
Cdd:pfam00115  94 GAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWA 161
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1770414070 161 VSITAILLLFSLPVLAGAITMLLTDRNINTSFFDPA 196
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL 197
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
7-201 2.79e-36

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 133.44  E-value: 2.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070   7 SLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLL 86
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  87 MSSFIEKGAGTGWTVYPPLSSNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAI 166
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1770414070 167 LLLFSLPVLAGAITMLLTDRNINTSFFDPAGGGDP 201
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMP 265
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
27-200 3.09e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 130.83  E-value: 3.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070  27 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 106
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770414070 107 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 186
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
                         170
                  ....*....|....
gi 1770414070 187 NINTSFFDPAGGGD 200
Cdd:PRK15017  258 YLGTHFFTNDMGGN 271
 
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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