Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:cd01665  172 ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243

Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:cd01665  172 ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:COG1845  121 PTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III 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]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226859329    4 SVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYV 71
Cdd:TIGR02897 119 GSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYL 186

Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:cd01665  172 ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVYWW 243

cytochrome c oxidase subunit III; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVY 70
Cdd:MTH00155 186 IADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255

cytochrome c oxidase subunit III; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:MTH00189 187 IADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 258

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:COG1845  121 PTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192

Cytochrome c oxidase subunit III;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329    1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:pfam00510 185 ISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWW 256

cytochrome c oxidase subunit III; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:MTH00130 188 IADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWW 259

cytochrome c oxidase subunit III; Validated

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:MTH00099 188 ISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259

cytochrome c oxidase subunit III; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:MTH00052 189 ISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWW 260

cytochrome c oxidase subunit III; Validated

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:MTH00009 186 IADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWW 257

cytochrome-c oxidase

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226859329   1 IADSVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVWFG 74
Cdd:PLN02194 191 ISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGG 264

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226859329   5 VYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:cd02865  117 PAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226859329   6 YGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFssQRHFGF---EACIWYWHFVDVVWVSLWFVVYVW 72
Cdd:cd02864  135 FGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKY--QRIGRYeivEIAGLYWHFVDLVWVFIFAFFYLW 202

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III 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]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226859329    4 SVYGSVFYLLTGFHGAHVVVGTIWLMVSLARLWRGEFSSQRHFGFEACIWYWHFVDVVWVSLWFVVYV 71
Cdd:TIGR02897 119 GSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYL 186