NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2465767215|dbj|BDS00531|]
View 

cytochrome c oxidase subunit 1, partial (mitochondrion) [Hydroptila sp. Hd]

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 ...
 1-134 9.90e-93

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: 276.75  E-value: 9.90e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-134 9.90e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 276.75  E-value: 9.90e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-134 2.02e-86

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: 259.72  E-value: 2.02e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:cd01663   101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:cd01663   181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-134 2.49e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 178.01  E-value: 2.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:COG0843   112 LLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:COG0843   192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-134 9.05e-54

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: 175.87  E-value: 9.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   2 LLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILI 81
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2465767215  82 TAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-134 4.16e-28

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: 106.50  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMinKGVGTGWTVYPPLAtniahsgaSVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFdQMPLFVWSIL 80
Cdd:pfam00115  95 AVLLLASF--GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEV 134
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-134 9.90e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 276.75  E-value: 9.90e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-134 2.02e-86

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: 259.72  E-value: 2.02e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:cd01663   101 LLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:cd01663   181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-134 2.52e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 244.97  E-value: 2.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00167  110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSIL 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00167  190 VTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-134 1.91e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 240.26  E-value: 1.91e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   2 LLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILI 81
Cdd:MTH00223  108 LLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKV 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2465767215  82 TAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00223  188 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-134 3.78e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 239.61  E-value: 3.78e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00116  110 LLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVL 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00116  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-134 1.88e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 235.00  E-value: 1.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00142  108 LLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVK 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00142  188 ITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-134 2.96e-69

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 216.29  E-value: 2.96e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00103  110 LLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVL 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00103  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-134 1.33e-68

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 214.77  E-value: 1.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00007  107 ILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVV 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00007  187 ITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-134 3.60e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 213.65  E-value: 3.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00077  110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVL 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00077  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-134 7.31e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 212.86  E-value: 7.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00183  110 LLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVL 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00183  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-134 6.93e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 207.76  E-value: 6.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00037  110 LLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVF 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00037  190 ITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-134 1.72e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 206.98  E-value: 1.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:MTH00182  112 ILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSIL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00182  192 ITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-134 5.22e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 205.45  E-value: 5.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   2 LLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILI 81
Cdd:MTH00184  113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2465767215  82 TAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00184  193 TTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-134 1.63e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 198.75  E-value: 1.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   2 LLIWSSMINKGVGTGWTVYPPLATnIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILI 81
Cdd:MTH00079  112 LILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFV 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2465767215  82 TAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00079  191 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-134 1.31e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 189.45  E-value: 1.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   2 LLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILI 81
Cdd:MTH00026  112 LLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFI 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2465767215  82 TAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00026  192 TAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-134 5.38e-58

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: 185.81  E-value: 5.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:cd00919    98 LLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVL 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:cd00919   178 VTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-134 2.49e-54

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 178.01  E-value: 2.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:COG0843   112 LLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:COG0843   192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-134 9.05e-54

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: 175.87  E-value: 9.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   2 LLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILI 81
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2465767215  82 TAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 12-134 1.56e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 162.15  E-value: 1.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215  12 GVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMkFDQMPLFVWSILITAILLLMSLP 91
Cdd:MTH00048  120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLP 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2465767215  92 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:MTH00048  199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-134 1.87e-43

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: 148.50  E-value: 1.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMINKGVGTGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSIL 80
Cdd:cd01662   104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:cd01662   184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-134 4.16e-28

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: 106.50  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215   1 MLLIWSSMinKGVGTGWTVYPPLAtniahsgaSVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFdQMPLFVWSIL 80
Cdd:pfam00115  95 AVLLLASF--GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAIL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2465767215  81 ITAILLLMSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEV 134
Cdd:pfam00115 164 ATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 12-134 1.03e-24

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 98.08  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465767215  12 GVG----TGWTVYPPLATNIAHSGASVDLAIFSLHLAGISSILGAINFISTIINMKPINMKFDQMPLFVWSILITAILLL 87
Cdd:PRK15017  161 GVGefaqTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2465767215  88 MSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV 134
Cdd:PRK15017  241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287
 
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