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Conserved domains on  [gi|313877250|gb|ADR82381|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Zeugodacus cucurbitae]

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 ...
 1-202 4.07e-146

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: 415.81  E-value: 4.07e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00153 310 IAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMG 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00153 390 GFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLTN 202
Cdd:MTH00153 470 IWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-202 4.07e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 415.81  E-value: 4.07e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00153 310 IAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMG 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00153 390 GFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLTN 202
Cdd:MTH00153 470 IWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-185 9.37e-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: 330.21  E-value: 9.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:cd01663  303 IAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFA 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:cd01663  383 GFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFI 462

                        170       180
                 ....*....|....*....|....*.
gi 313877250 161 IWESLVTQRQVIY-PMQLSSSIEWLQ 185
Cdd:cd01663  463 VWESFVSGRKVIFnVGEGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 1.39e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 225.78  E-value: 1.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:COG0843  313 IAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFL 158
Cdd:COG0843  393 GLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFL 472

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 313877250 159 FIIWESLVTQRQV-IYPMQlSSSIEWLQNTPPAEHSYSELPLLT 201
Cdd:COG0843  473 INLVVSLRKGPKAgGNPWG-ARTLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-194 2.34e-68

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: 216.71  E-value: 2.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250    1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:TIGR02891 304 IAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSSISLLGILFFL 158
Cdd:TIGR02891 384 AIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFL 463

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 313877250  159 FIIWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSY 194
Cdd:TIGR02891 464 WNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-149 1.49e-46

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: 158.51  E-value: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250    1 IAVPTGIKIFSWLATLHGTQLN-YSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIM 79
Cdd:pfam00115 279 IAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALF 358

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313877250   80 AGFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSSI 149
Cdd:pfam00115 359 GGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-202 4.07e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 415.81  E-value: 4.07e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00153 310 IAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMG 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00153 390 GFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLTN 202
Cdd:MTH00153 470 IWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-185 9.37e-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: 330.21  E-value: 9.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:cd01663  303 IAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFA 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:cd01663  383 GFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFI 462

                        170       180
                 ....*....|....*....|....*.
gi 313877250 161 IWESLVTQRQVIY-PMQLSSSIEWLQ 185
Cdd:cd01663  463 VWESFVSGRKVIFnVGEGSTSLEWTL 488
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-202 1.99e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 327.84  E-value: 1.99e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00142 310 IAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFA 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00142 390 GFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFI 469

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLTN 202
Cdd:MTH00142 470 VWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-200 5.45e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 326.63  E-value: 5.45e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00167 312 IAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00167 392 GFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFI 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLL 200
Cdd:MTH00167 472 IWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-198 7.42e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 326.16  E-value: 7.42e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00223 309 IAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFA 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00223 389 GFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFI 468

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELP 198
Cdd:MTH00223 469 VWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-202 1.34e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 325.89  E-value: 1.34e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00116 312 IAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00116 392 GFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFI 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLTN 202
Cdd:MTH00116 472 IWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-199 2.20e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 292.12  E-value: 2.20e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00037 312 IAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00037 392 GFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFL 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNT-PPAEHSYSELPL 199
Cdd:MTH00037 472 IWEAFASQREVISPEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-196 7.12e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 290.63  E-value: 7.12e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00103 312 IAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMG 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00103 392 GFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFM 471

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSE 196
Cdd:MTH00103 472 IWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-202 9.55e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 285.30  E-value: 9.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00077 312 IAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMG 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00077 392 GFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFI 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLTN 202
Cdd:MTH00077 472 IWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-196 4.07e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 281.04  E-value: 4.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00183 312 IAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00183 392 AFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFI 471

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSE 196
Cdd:MTH00183 472 LWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-201 4.43e-93

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 280.63  E-value: 4.43e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00007 309 IAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFA 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00007 389 AFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFI 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELPLLT 201
Cdd:MTH00007 469 LWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-200 2.73e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 248.20  E-value: 2.73e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00182 314 IAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFG 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00182 394 GFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYI 473

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 313877250 161 IWESLVTQRQVI----YPMQLSSSIEWLQNTPPAEHSYSELPLL 200
Cdd:MTH00182 474 IYDAYVREEKFIgwkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-196 3.00e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 244.98  E-value: 3.00e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00079 312 IAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFT 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00079 392 GISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYV 471

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 313877250 161 IWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSE 196
Cdd:MTH00079 472 LLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-200 8.69e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 238.96  E-value: 8.69e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:MTH00184 314 IAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFG 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:MTH00184 394 GFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYI 473

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313877250 161 IWESLVTQRQVIYPMQLS---SSIEWLQNTPPAEHSYSELPLL 200
Cdd:MTH00184 474 VYDAYVREIKFVGWVEDSghyPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-165 3.18e-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: 233.58  E-value: 3.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:cd00919  299 IAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFA 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFI 160
Cdd:cd00919  379 GLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGN 458


                 ....*
gi 313877250 161 IWESL 165
Cdd:cd00919  459 LFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-201 1.39e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 225.78  E-value: 1.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:COG0843  313 IAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFL 158
Cdd:COG0843  393 GLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFL 472

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 313877250 159 FIIWESLVTQRQV-IYPMQlSSSIEWLQNTPPAEHSYSELPLLT 201
Cdd:COG0843  473 INLVVSLRKGPKAgGNPWG-ARTLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-194 2.34e-68

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: 216.71  E-value: 2.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250    1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:TIGR02891 304 IAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSSISLLGILFFL 158
Cdd:TIGR02891 384 AIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFL 463

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 313877250  159 FIIWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSY 194
Cdd:TIGR02891 464 WNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-194 4.19e-62

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: 200.50  E-value: 4.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:cd01662  305 IAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFA 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFL 158
Cdd:cd01662  385 GFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFL 464

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 313877250 159 FIIWESLVTQRQVIY--PMQlSSSIEWLQNTPPAEHSY 194
Cdd:cd01662  465 INVIVSIRKGKRDATgdPWG-ARTLEWATSSPPPAYNF 501
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-200 1.52e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 192.15  E-value: 1.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLN--YSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAI 78
Cdd:MTH00026 313 IAVPTGIKIFSWLATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAI 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  79 MAGFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFL 158
Cdd:MTH00026 393 FGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFI 472

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 313877250 159 FIIWESL---------VTQRQVIYPMQLS----SSIEWLQNTPPAEHSYSELPLL 200
Cdd:MTH00026 473 VVIFDAYyreepfdinIMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-193 1.08e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 186.81  E-value: 1.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYS-PAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIM 79
Cdd:MTH00048 310 IGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVV 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  80 AGFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLF 159
Cdd:MTH00048 390 IMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVF 469

                        170       180       190
                 ....*....|....*....|....*....|....
gi 313877250 160 IIWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHS 193
Cdd:MTH00048 470 ILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-149 1.49e-46

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: 158.51  E-value: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250    1 IAVPTGIKIFSWLATLHGTQLN-YSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIM 79
Cdd:pfam00115 279 IAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALF 358

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313877250   80 AGFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSSI 149
Cdd:pfam00115 359 GGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-198 3.11e-41

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: 147.31  E-value: 3.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250    1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:TIGR02882 348 IAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLA 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSTIGSSISLLGILFFL 158
Cdd:TIGR02882 428 GLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLV 507

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 313877250  159 F-IIWESLVTQRQVIYPMQLSSSIEWLQNTPPAEHSYSELP 198
Cdd:TIGR02882 508 YnIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-198 6.58e-35

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 129.67  E-value: 6.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   1 IAVPTGIKIFSWLATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMA 80
Cdd:PRK15017 355 IAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFA 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  81 GFVHWYPLFTGLVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTTWNVVSTIGSSISLLGILFFLF 159
Cdd:PRK15017 435 GMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVI 514

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313877250 160 IIWESLVTQ---RQVIYPMQLSSSIEWLQNTPPAEHSYSELP 198
Cdd:PRK15017 515 QMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 6-166 4.11e-14

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 70.01  E-value: 4.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250   6 GIKIFSWLATLHGTQLNYSPAMLWALGFVFlftvGGLTGVVLANSSVDIILHDTYYVVAHFHyvLSMGAVFAIMA-GFVH 84
Cdd:cd01660  309 GKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAY 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313877250  85 WY-PLFTGLVLNPKWLKS-QFIIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----TTWNVVSTIGSSISLLGIL 155
Cdd:cd01660  383 WLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGA 462

                        170
                 ....*....|.
gi 313877250 156 FFLFIIWESLV 166
Cdd:cd01660  463 LFLYILFRTLL 473
 
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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