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Conserved domains on  [gi|350285905|gb|AEQ28205|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Melanotis caerulescens]

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 ...
 1-292 0e+00

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 MTH00116:

Pssm-ID: 469701  Cd Length: 515  Bit Score: 585.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00116 224 GGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00116 304 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00116 384 GAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMT 463

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQVQE 292
Cdd:MTH00116 464 AVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQE 515
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-292 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 585.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00116 224 GGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00116 304 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00116 384 GAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMT 463

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQVQE 292
Cdd:MTH00116 464 AVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQE 515
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-273 0e+00

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: 535.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:cd01663  215 GGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRA 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:cd01663  295 YFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSM 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:cd01663  375 GAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFV 454

                        250       260       270
                 ....*....|....*....|....*....|....
gi 350285905 241 AVIMLVFIIWEAFASKRKA-FQPELTSTNVEWIH 273
Cdd:cd01663  455 SVLLFLFIVWESFVSGRKViFNVGEGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-285 7.20e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 366.76  E-value: 7.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:COG0843  226 GGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKA 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:COG0843  305 FFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIG 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DAYALWNTISSVGSLIS 238
Cdd:COG0843  385 GVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFIL 464

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 350285905 239 LTAVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEP 285
Cdd:COG0843  465 AVGFLLFLINLVVSLRKGPKAGGNPWGARTLEWATPSPPPLYNFASI 511
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-282 1.79e-122

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: 359.23  E-value: 1.79e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905    1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:TIGR02891 217 RGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:TIGR02891 296 FFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVG 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA--YALWNTISSVGSLIS 238
Cdd:TIGR02891 376 GSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFIL 455

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 350285905  239 LTAVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTF 282
Cdd:TIGR02891 456 AAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-237 1.33e-85

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: 262.89  E-value: 1.33e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905    1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQA 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKW-DPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLS 159
Cdd:pfam00115 271 LFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLF 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  160 MGAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDAYALWNTISSVGS 235
Cdd:pfam00115 351 GGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGG 430


                  ..
gi 350285905  236 LI 237
Cdd:pfam00115 431 VL 432
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-292 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 585.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00116 224 GGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00116 304 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00116 384 GAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMT 463

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQVQE 292
Cdd:MTH00116 464 AVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQE 515
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-284 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 560.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00153 222 GGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRA 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00153 302 YFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSM 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00153 382 GAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLI 461

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEE 284
Cdd:MTH00153 462 SILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSE 505
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-289 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 555.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00167 224 GGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00167 304 YFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00167 384 GAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLV 463

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQ 289
Cdd:MTH00167 464 AVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-273 0e+00

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: 535.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:cd01663  215 GGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRA 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:cd01663  295 YFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSM 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:cd01663  375 GAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFV 454

                        250       260       270
                 ....*....|....*....|....*....|....
gi 350285905 241 AVIMLVFIIWEAFASKRKA-FQPELTSTNVEWIH 273
Cdd:cd01663  455 SVLLFLFIVWESFVSGRKViFNVGEGSTSLEWTL 488
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-292 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 531.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00183 224 GGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00183 304 YFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00183 384 GAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLV 463

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQVQE 292
Cdd:MTH00183 464 AVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEEPAFVQVQS 515
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-291 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 523.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00077 224 GGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00077 304 YFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00077 384 GAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLV 463

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQVQ 291
Cdd:MTH00077 464 AVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQTR 514
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-290 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 523.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00103 224 GGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00103 304 YFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00103 384 GAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLT 463

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFVQV 290
Cdd:MTH00103 464 AVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-288 2.15e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 499.50  E-value: 2.15e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00223 221 GGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRA 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00223 301 YFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSM 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00223 381 GAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFV 460

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFV 288
Cdd:MTH00223 461 SVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-285 1.07e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 492.70  E-value: 1.07e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00142 222 GGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRA 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00142 302 YFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSM 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00142 382 GAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFI 461

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEP 285
Cdd:MTH00142 462 AVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDEL 506
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-288 1.31e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 459.68  E-value: 1.31e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00037 224 GGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00037 304 YFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSM 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00037 384 GAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLV 463

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGC-PPPFHTFEEPAFV 288
Cdd:MTH00037 464 ATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSfPPSHHTFDETPST 512
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-288 3.34e-153

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 438.18  E-value: 3.34e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00007 221 GGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRA 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00007 301 YFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSM 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00007 381 GAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFV 460

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEPAFV 288
Cdd:MTH00007 461 ALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGII 508
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-289 1.35e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 403.82  E-value: 1.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00182 226 GGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00182 306 YFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSM 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00182 386 GAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIV 465

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 350285905 241 AVIMLVFIIWEAFASKRK----AFQPELTSTNVEWIHGCPPPFHTFEEPAFVQ 289
Cdd:MTH00182 466 GVVWFIYIIYDAYVREEKfigwKEGTGESWASLEWVHSSPPLFHTYNELPFVY 518
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-284 1.02e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 395.97  E-value: 1.02e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00079 224 TGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRA 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00079 304 YFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSL 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00079 384 GAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVF 463

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 350285905 241 AVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEE 284
Cdd:MTH00079 464 ALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-288 1.34e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 388.42  E-value: 1.34e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00184 226 GGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:MTH00184 306 YFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSM 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:MTH00184 386 GAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIV 465

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 350285905 241 AVIMLVFIIWEAFASKRKAF---QPELTSTNVEWIHGCPPPFHTFEEPAFV 288
Cdd:MTH00184 466 GVVWFIYIVYDAYVREIKFVgwvEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-253 2.34e-127

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: 370.32  E-value: 2.34e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:cd00919  212 GGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRA 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:cd00919  291 YFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSG 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISLT 240
Cdd:cd00919  371 GVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGL 450

                        250
                 ....*....|...
gi 350285905 241 AVIMLVFIIWEAF 253
Cdd:cd00919  451 GLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-285 7.20e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 366.76  E-value: 7.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:COG0843  226 GGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKA 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:COG0843  305 FFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIG 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DAYALWNTISSVGSLIS 238
Cdd:COG0843  385 GVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFIL 464

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 350285905 239 LTAVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTFEEP 285
Cdd:COG0843  465 AVGFLLFLINLVVSLRKGPKAGGNPWGARTLEWATPSPPPLYNFASI 511
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-282 1.79e-122

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: 359.23  E-value: 1.79e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905    1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:TIGR02891 217 RGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:TIGR02891 296 FFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVG 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA--YALWNTISSVGSLIS 238
Cdd:TIGR02891 376 GSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFIL 455

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 350285905  239 LTAVIMLVFIIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTF 282
Cdd:TIGR02891 456 AAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-282 3.55e-111

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: 330.70  E-value: 3.55e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:cd01662  218 LGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNA 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:cd01662  297 FFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIG 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DAYALWNTISSVGSLIS 238
Cdd:cd01662  377 GVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLI 456

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 350285905 239 LTAVIMLVF-IIWEAFASKRKAFQPELTSTNVEWIHGCPPPFHTF 282
Cdd:cd01662  457 AAGVLLFLInVIVSIRKGKRDATGDPWGARTLEWATSSPPPAYNF 501
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-288 3.36e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 329.28  E-value: 3.36e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00026 225 GGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRA 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHGG--TIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVL 158
Cdd:MTH00026 305 YFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVL 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 159 SMGAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLIS 238
Cdd:MTH00026 385 SMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIIS 464

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350285905 239 LTAVIMLVFIIWEAFASKRK--------------AFQPELTSTnVEWIHGCPPPFHTFEEPAFV 288
Cdd:MTH00026 465 IIAVIWFIVVIFDAYYREEPfdinimakgplipfSCQPAHFDT-LEWSLTSPPEHHTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-258 1.85e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 323.94  E-value: 1.85e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:MTH00048 222 GGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAV 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  81 YFTSATMIIAIPTGIKVFSWLATLHG-GTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLS 159
Cdd:MTH00048 302 FFSSVTMIIGVPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLS 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 160 MGAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTISSVGSLISL 239
Cdd:MTH00048 382 LGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISA 461

                        250
                 ....*....|....*....
gi 350285905 240 TAVIMLVFIIWEAFASKRK 258
Cdd:MTH00048 462 FSGCFFVFILWESLVVKNE 480
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-237 1.33e-85

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: 262.89  E-value: 1.33e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905    1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQA 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKW-DPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLS 159
Cdd:pfam00115 271 LFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLF 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  160 MGAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDAYALWNTISSVGS 235
Cdd:pfam00115 351 GGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGG 430


                  ..
gi 350285905  236 LI 237
Cdd:pfam00115 431 VL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-289 6.79e-79

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 251.52  E-value: 6.79e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905    1 GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEpFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRA 80
Cdd:TIGR02843 267 AGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNA 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   81 YFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSM 160
Cdd:TIGR02843 346 FFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIG 425

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  161 GAVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPD-AYALWNTISSVGSLISL 239
Cdd:TIGR02843 426 GVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIA 505

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 350285905  240 TAVIMLVFIIWEAFASKRKafQPELT-----STNVEWIHGCPPPFHTFEEPAFVQ 289
Cdd:TIGR02843 506 CGILCQIIQIFVSIRDRDQ--NRDTTgdpwgGRTLEWSTSSPPPFYNFAVIPKVQ 558
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-282 3.27e-65

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 215.96  E-value: 3.27e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   2 GGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAY 81
Cdd:PRK15017 269 GGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAF 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  82 FTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMG 161
Cdd:PRK15017 348 FGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGG 427

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 162 AVFAILAGFTHWFPLFTGYTLHSTWAKAQFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDA-YALWNTISSVGSLISLT 240
Cdd:PRK15017 428 VVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIAL 507

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 350285905 241 AVIMLVFIIWEAFASK---RKAFQPELTSTNVEWIHGCPPPFHTF 282
Cdd:PRK15017 508 GILCQVIQMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNF 552
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 4-249 4.33e-20

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: 89.65  E-value: 4.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905   4 DPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKK---EPFGYMGMVWAMLsigfLGFIVWAHHMFT-VGMDVDTR 79
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLL----FSTPVGFHHQFAdPGIGPGWK 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905  80 AYFTSATMIIAIPTGIKVFSWLATL-HGGTIK-------------WDPPMLWALGF-IFLFTIGGLTGIVLANSSLDIAL 144
Cdd:cd01660  276 FIHMVLTFMVALPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVV 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285905 145 HDTYYVVAHFHyvLSMGAVFAILA-GFTHWF-PLFTGYTLHSTW-AKAQFGVMFVGVNLTFFPQHFLGLAGMPRR--YSD 219
Cdd:cd01660  356 HNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQ 433

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 350285905 220 YPDAY-----ALWNTISSVGSLISLTAVIMLVFII 249
Cdd:cd01660  434 YGGLPaagewAPYQQLMAIGGTILFVSGALFLYIL 468
 
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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