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Conserved domains on  [gi|134148668|gb|ABO64295|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Drosophila melanogaster]

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 ...
 1-184 4.15e-123

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: 356.49  E-value: 4.15e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00153  62 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00153 142 DLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPA 221

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00153 222 GGGDPILYQHLFWFFGHPEVYILI 245
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-184 4.15e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 356.49  E-value: 4.15e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00153  62 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00153 142 DLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPA 221

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00153 222 GGGDPILYQHLFWFFGHPEVYILI 245
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-184 1.54e-111

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: 326.36  E-value: 1.54e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:cd01663   55 IMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:cd01663  135 DLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPA 214

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:cd01663  215 GGGDPILYQHLFWFFGHPEVYILI 238
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-184 2.56e-71

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: 223.64  E-value: 2.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668    1 IMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:TIGR02891  58 IMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:TIGR02891 137 DLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPA 216

                         170       180
                  ....*....|....*....|....
gi 134148668  161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:TIGR02891 217 RGGDPLLWQHLFWFFGHPEVYIIF 240
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-184 6.66e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 223.47  E-value: 6.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:COG0843   67 IMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:COG0843  146 DLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPA 225

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:COG0843  226 GGGDPLLWQHLFWFFGHPEVYILI 249
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-184 1.07e-39

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: 139.63  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668    1 IMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMvenGAGTGWTVYPPLSAgiahggasV 80
Cdd:pfam00115  51 LMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------V 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNtsffdpA 160
Cdd:pfam00115 119 DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------A 191

                         170       180
                  ....*....|....*....|....
gi 134148668  161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILI 215
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-184 4.15e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 356.49  E-value: 4.15e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00153  62 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00153 142 DLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPA 221

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00153 222 GGGDPILYQHLFWFFGHPEVYILI 245
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-184 1.54e-111

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: 326.36  E-value: 1.54e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:cd01663   55 IMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:cd01663  135 DLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPA 214

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:cd01663  215 GGGDPILYQHLFWFFGHPEVYILI 238
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-184 5.10e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 310.46  E-value: 5.10e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00167  64 VMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00167 144 DLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPA 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00167 224 GGGDPILYQHLFWFFGHPEVYILI 247
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-184 4.29e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 308.06  E-value: 4.29e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00223  61 VMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00223 141 DLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPA 220

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00223 221 GGGDPILYQHLFWFFGHPEVYILI 244
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-184 8.27e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 307.40  E-value: 8.27e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00116  64 VMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00116 144 DLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPA 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00116 224 GGGDPILYQHLFWFFGHPEVYILI 247
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-184 1.23e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 302.03  E-value: 1.23e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00142  62 VMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00142 142 DLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPA 221

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00142 222 GGGDPILYQHLFWFFGHPEVYILI 245
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-184 6.88e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 282.18  E-value: 6.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00007  61 LMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00007 141 DLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 220

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00007 221 GGGDPILYQHLFWFFGHPEVYILI 244
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-184 5.29e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 279.79  E-value: 5.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00037  64 VMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00037 144 DLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPA 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00037 224 GGGDPILFQHLFWFFGHPEVYILI 247
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-184 7.60e-91

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 274.45  E-value: 7.60e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00103  64 VMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00103 144 DLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPA 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00103 224 GGGDPILYQHLFWFFGHPEVYILI 247
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-184 1.40e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 273.72  E-value: 1.40e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00183  64 VMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00183 144 DLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPA 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00183 224 GGGDPILYQHLFWFFGHPEVYILI 247
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-184 4.36e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 272.58  E-value: 4.36e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00077  64 VMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00077 144 DLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPA 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00077 224 GGGDPVLYQHLFWFFGHPEVYILI 247
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-184 1.66e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 268.09  E-value: 1.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAgIAHGGASV 80
Cdd:MTH00079  65 LMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00079 144 DLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPS 223

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00079 224 TGGNPLLYQHLFWFFGHPEVYILI 247
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-184 7.61e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 267.07  E-value: 7.61e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00182  66 IMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00182 146 DMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPA 225

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00182 226 GGGDPILFQHLFWFFGHPEVYILI 249
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-184 1.28e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 266.31  E-value: 1.28e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00184  66 VMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00184 146 DMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPA 225

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00184 226 GGGDPILYQHLFWFFGHPEVYILI 249
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-184 2.09e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 245.69  E-value: 2.09e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00026  65 VMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSV 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00026 145 DMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPA 224

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00026 225 GGGDPILYQHLFWFFGHPEVYILI 248
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-184 1.21e-71

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: 223.56  E-value: 1.21e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:cd00919   53 IMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:cd00919  132 DLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPA 211

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:cd00919  212 GGGDPVLYQHLFWFFGHPEVYILI 235
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-184 2.56e-71

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: 223.64  E-value: 2.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668    1 IMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:TIGR02891  58 IMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:TIGR02891 137 DLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPA 216

                         170       180
                  ....*....|....*....|....
gi 134148668  161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:TIGR02891 217 RGGDPLLWQHLFWFFGHPEVYIIF 240
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-184 6.66e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 223.47  E-value: 6.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:COG0843   67 IMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:COG0843  146 DLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPA 225

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:COG0843  226 GGGDPLLWQHLFWFFGHPEVYILI 249
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-184 8.36e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 199.13  E-value: 8.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVenGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:MTH00048  65 IMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:MTH00048 143 DFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPL 221

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:MTH00048 222 GGGDPVLFQHMFWFFGHPEVYVLI 245
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-184 1.40e-60

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: 195.88  E-value: 1.40e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:cd01662   59 IMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:cd01662  138 DYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNA 217

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:cd01662  218 LGGNPMLWQHLFWIFGHPEVYILI 241
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-184 1.07e-39

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: 139.63  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668    1 IMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMvenGAGTGWTVYPPLSAgiahggasV 80
Cdd:pfam00115  51 LMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------V 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNtsffdpA 160
Cdd:pfam00115 119 DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------A 191

                         170       180
                  ....*....|....*....|....
gi 134148668  161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILI 215
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-184 3.78e-38

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 138.14  E-value: 3.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   1 IMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:PRK15017 109 IMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGV 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668  81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:PRK15017 188 DYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTND 267

                        170       180
                 ....*....|....*....|....
gi 134148668 161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:PRK15017 268 MGGNMMMYINLIWAWGHPEVYILI 291
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-184 5.60e-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: 131.90  E-value: 5.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668    1 IMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASV 80
Cdd:TIGR02882 102 IMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGV 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134148668   81 DLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPA 160
Cdd:TIGR02882 181 NYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVA 260

                         170       180
                  ....*....|....*....|....
gi 134148668  161 GGGDPILYQHLFWFFGHPEVYILI 184
Cdd:TIGR02882 261 HGGMPMLWANLFWIWGHPEVYIVI 284
 
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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