NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|922668144|gb|ALA65611|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Eleutherozoa sp. COT033_L212]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-220 1.64e-147

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: 420.43  E-value: 1.64e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00153  69 MPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00153 149 HLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00153 229 YQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAH 288
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 1.64e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 420.43  E-value: 1.64e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00153  69 MPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00153 149 HLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00153 229 YQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAH 288
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-220 1.30e-143

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: 409.57  E-value: 1.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:cd01663   62 MPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:cd01663  142 HLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:cd01663  222 YQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAH 281
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 4-220 4.18e-90

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 273.33  E-value: 4.18e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144    4 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 83
Cdd:TIGR02891  67 ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   84 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 163
Cdd:TIGR02891 147 GISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH 226

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922668144  164 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAH 282
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-220 4.36e-89

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 272.00  E-value: 4.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   4 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 83
Cdd:COG0843   76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  84 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 163
Cdd:COG0843  156 GVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 922668144 164 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:COG0843  236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAH 291
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-220 9.32e-55

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: 180.46  E-value: 9.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144    4 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLA 83
Cdd:pfam00115  60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   84 GASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQH 163
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922668144  164 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAH 257
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-220 1.64e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 420.43  E-value: 1.64e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00153  69 MPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00153 149 HLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00153 229 YQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAH 288
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-220 1.30e-143

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: 409.57  E-value: 1.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:cd01663   62 MPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:cd01663  142 HLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:cd01663  222 YQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAH 281
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-220 9.86e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 393.04  E-value: 9.86e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00037  71 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00037 151 HLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPIL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00037 231 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAH 290
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-220 6.23e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 390.96  E-value: 6.23e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00167  71 MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00167 151 HLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPIL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00167 231 YQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAH 290
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-220 1.01e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 390.61  E-value: 1.01e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00116  71 MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00116 151 HLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00116 231 YQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAH 290
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-220 1.07e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 385.10  E-value: 1.07e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00223  68 MPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00223 148 HLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00223 228 YQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAH 287
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-220 2.33e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 381.76  E-value: 2.33e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00142  69 MPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00142 149 HLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPIL 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00142 229 YQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAH 288
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-220 6.57e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 347.68  E-value: 6.57e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00183  71 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00183 151 HLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00183 231 YQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAH 290
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-220 1.16e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 344.62  E-value: 1.16e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00077  71 MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00077 151 HLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00077 231 YQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAH 290
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-220 1.83e-117

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 343.79  E-value: 1.83e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00103  71 MPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00103 151 HLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00103 231 YQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAH 290
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-220 6.15e-116

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 339.96  E-value: 6.15e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00007  68 MPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00007 148 HLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIL 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00007 228 YQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAH 287
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-220 6.58e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 335.25  E-value: 6.58e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00182  73 MPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00182 153 HLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00182 233 FQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAH 292
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-220 5.03e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 330.25  E-value: 5.03e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00184  73 MPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00184 153 HLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00184 233 YQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAH 292
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-220 8.51e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 313.93  E-value: 8.51e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSgLAHAGGSVDLAIFSL 80
Cdd:MTH00079  72 MPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00079 151 HCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLL 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00079 231 YQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAH 290
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-220 7.28e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 296.92  E-value: 7.28e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00026  72 MPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00026 152 HLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPIL 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00026 232 YQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAH 291
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-220 2.03e-90

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: 273.25  E-value: 2.03e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPlMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:cd00919   60 MPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:cd00919  139 HLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVL 218

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:cd00919  219 YQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAH 277
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 4-220 4.18e-90

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 273.33  E-value: 4.18e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144    4 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 83
Cdd:TIGR02891  67 ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   84 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 163
Cdd:TIGR02891 147 GISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH 226

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922668144  164 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAH 282
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
4-220 4.36e-89

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 272.00  E-value: 4.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   4 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 83
Cdd:COG0843   76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  84 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 163
Cdd:COG0843  156 GVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 922668144 164 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:COG0843  236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAH 291
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-220 2.82e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 248.44  E-value: 2.82e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASagVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:MTH00048  72 MPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:MTH00048 150 HLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVL 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:MTH00048 229 FQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAH 288
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-220 2.54e-74

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: 232.86  E-value: 2.54e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:cd01662   66 MPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:cd01662  145 QFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPML 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:cd01662  225 WQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVH 283
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-220 9.32e-55

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: 180.46  E-value: 9.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144    4 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLA 83
Cdd:pfam00115  60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   84 GASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQH 163
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922668144  164 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAH 257
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-220 4.67e-46

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 161.64  E-value: 4.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   1 MPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:PRK15017 116 MPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:PRK15017 195 QLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMM 274

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144 161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSgKSEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:PRK15017 275 YINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLH 333
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-220 4.11e-44

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: 155.78  E-value: 4.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144    1 MPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSL 80
Cdd:TIGR02882 109 MPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIAL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144   81 HLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPIL 160
Cdd:TIGR02882 188 QISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPML 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668144  161 FQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWAH 220
Cdd:TIGR02882 268 WANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVH 326
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH