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Conserved domains on  [gi|1934794723|gb|QPF49601|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Synergus mexicanus]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-201 1.22e-113

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: 333.37  E-value: 1.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00153   33 LLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00153  113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00153  193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-201 1.22e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 333.37  E-value: 1.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00153   33 LLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00153  113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00153  193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-201 2.27e-113

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: 331.75  E-value: 2.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:cd01663    26 LLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:cd01663   106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:cd01663   186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 4.69e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.23  E-value: 4.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELST-CPQLINNDQiYNSIVTAHAFIMIFFMVMPiMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLL 79
Cdd:COG0843    38 LLMRLQLAGpGLGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  80 SSMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTI 159
Cdd:COG0843   116 ISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSI 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1934794723 160 LLLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:COG0843   196 LILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-201 7.80e-40

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: 140.40  E-value: 7.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPiMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:pfam00115  22 LLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMfidQGAGTGWTIYPPLssnmshpgISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMdKISLFTWSIFLTTIL 160
Cdd:pfam00115 101 SF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAIL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTsffdpmGGGDPVLYQHLF 201
Cdd:pfam00115 169 ILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-201 1.33e-33

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: 126.12  E-value: 1.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGgFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:TIGR02882  73 LLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:TIGR02882 152 SFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLI 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:TIGR02882 232 IIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-201 1.22e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 333.37  E-value: 1.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00153   33 LLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00153  113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00153  193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-201 2.27e-113

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: 331.75  E-value: 2.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:cd01663    26 LLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:cd01663   106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:cd01663   186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-201 4.90e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 308.91  E-value: 4.90e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00167   35 LLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00167  115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTIL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00167  195 LLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-201 5.85e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 298.43  E-value: 5.85e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00223   32 LLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00223  112 SSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00223  192 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-201 1.55e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 294.69  E-value: 1.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00116   35 LLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00116  115 SSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00116  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-201 6.20e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 285.46  E-value: 6.20e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00142   33 LLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00142  113 SAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAIL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00142  193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-201 7.44e-88

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 267.52  E-value: 7.44e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00103   35 LLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00103  115 SSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00103  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-201 1.24e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 266.81  E-value: 1.24e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00077   35 LLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00077  115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00077  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-201 1.65e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 266.40  E-value: 1.65e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00183   35 LLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00183  115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00183  195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-201 7.28e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 262.46  E-value: 7.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   2 IIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLSS 81
Cdd:MTH00037   36 IIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLAS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  82 MFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTILL 161
Cdd:MTH00037  116 AGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLL 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934794723 162 LLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00037  196 LLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-201 1.58e-85

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 261.37  E-value: 1.58e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00007   32 LLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00007  112 SAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00007  192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-201 6.86e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 257.45  E-value: 6.86e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00184   37 MLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00184  117 SAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFL 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00184  197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-201 5.94e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 254.61  E-value: 5.94e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00079   36 LIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSnMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00079  116 SCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00079  195 LVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-201 1.94e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 253.59  E-value: 1.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00182   37 MLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00182  117 SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFL 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00182  197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-201 3.47e-75

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: 233.19  E-value: 3.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFsNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:cd00919    24 LLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGF-GNLLPPLIGARDLAFPRLNNLSFWLFPPGLLLLLS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:cd00919   103 SVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAIL 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:cd00919   183 LLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-201 4.39e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 232.60  E-value: 4.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:MTH00026   36 MLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:MTH00026  116 SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAIL 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00026  196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 4.69e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 219.23  E-value: 4.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELST-CPQLINNDQiYNSIVTAHAFIMIFFMVMPiMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLL 79
Cdd:COG0843    38 LLMRLQLAGpGLGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  80 SSMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTI 159
Cdd:COG0843   116 ISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSI 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1934794723 160 LLLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:COG0843   196 LILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 19-201 1.10e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 207.61  E-value: 1.10e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  19 IYNSIVTAHAFIMIFFMVMPIMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLSSMFIdqGAGTGWTIYPPL 98
Cdd:MTH00048   54 VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  99 SSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMdKISLFTWSIFLTTILLLLSLPVLAGGITMLLFD 178
Cdd:MTH00048  132 SSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFD 210

                         170       180
                  ....*....|....*....|...
gi 1934794723 179 RNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:MTH00048  211 RNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-201 3.27e-57

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: 187.79  E-value: 3.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCP-QLINNDQiYNSIVTAHAFIMIFFMVMPIMIGgFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLL 79
Cdd:cd01662    30 LLMRTQLALPGnDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  80 SSMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTI 159
Cdd:cd01662   108 ASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSI 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1934794723 160 LLLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:cd01662   188 LILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-201 7.80e-40

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: 140.40  E-value: 7.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPiMIGGFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:pfam00115  22 LLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMfidQGAGTGWTIYPPLssnmshpgISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMdKISLFTWSIFLTTIL 160
Cdd:pfam00115 101 SF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAIL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTsffdpmGGGDPVLYQHLF 201
Cdd:pfam00115 169 ILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 20-200 4.02e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 133.14  E-value: 4.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  20 YNSIVTAHAFIMIFFMVMPIMIGgFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLSSMFIDQGAGTGWTIYPPLS 99
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723 100 SNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTILLLLSLPVLAGGITMLLFDR 179
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180
                  ....*....|....*....|.
gi 1934794723 180 NLNTSFFDPMGGGDPVLYQHL 200
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINL 278
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-201 1.33e-33

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: 126.12  E-value: 1.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723   1 LIIRMELSTCPQLINNDQIYNSIVTAHAFIMIFFMVMPIMIGgFSNYLIPLMLGIPDMAFPRLNNMSFWLLIPSIMLLLS 80
Cdd:TIGR02882  73 LLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934794723  81 SMFIDQGAGTGWTIYPPLSSNMSHPGISTDLTIYSLHMSGISSILGSINFICTIWNMRPNKMTMDKISLFTWSIFLTTIL 160
Cdd:TIGR02882 152 SFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLI 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934794723 161 LLLSLPVLAGGITMLLFDRNLNTSFFDPMGGGDPVLYQHLF 201
Cdd:TIGR02882 232 IIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
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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