ID A0A0D3Q333_SPIER Unreviewed; 521 AA. AC A0A0D3Q333; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 12-AUG-2020, entry version 17. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; GN Name=cox1 {ECO:0000313|EMBL:AJC01987.1}; OS Spirometra erinaceieuropaei (Tapeworm) (Spirometra erinacei). OG Mitochondrion {ECO:0000313|EMBL:AJC01987.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda; OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Spirometra. OX NCBI_TaxID=99802 {ECO:0000313|EMBL:AJC01987.1}; RN [1] {ECO:0000313|EMBL:AJC01987.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25793277; RA Zhang X., Cui J., Liu L.N., Jiang P., Wang H., Qi X., Wu X.Q., Wang Z.Q.; RT "Genetic Structure Analysis of Spirometra erinaceieuropaei Isolates from RT Central and Southern China."; RL PLoS ONE 10:E0119295-E0119295(2015). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane CC protein {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KM605298; AJC01987.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AJC01987.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 21..44 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 64..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 144..173 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 185..211 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 243..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 270..290 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 302..326 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 338..358 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 378..397 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 409..429 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 449..474 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 3..505 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 521 AA; 58527 MW; 45391D9573CBB4FD CRC64; MAKFSFFSWL FTLDHKRVGM IYTLIGIWSG FVGLSFSVMI RVNFVEPYFN VISSDCYNFL ITNHGIIMIF FFLMPGLMGG LGNYLIPLLP GLPNLNFPRL NPLNAGWLFP SILFLGRSMG WGAGNGGTFY PPLSPSLFSD SRGVNLLMFS LHLAGLSSLL GSINFICTLY SAFVDNFVSR SSILLWSYLF TSILLLLTIP VWAAAITMLL FDRNFGSAFF DPLGGGDPVL FQHMFWFFGH PEVYVLILPG FGMVSHVCSN LGCSYDTFGF YGLLFAMFSI VCLGSVVWGH HMFTVGLDVK TAVFFSSVTM IIGVPTGIKV FSWLYMILNS RVSLREPVFW WVLSFIVLFT MGGVTGIILS ACVLDNILHD TWFVVAHFHY VMSLGSYISV IIFFVWWWPV ITGVSLNKYL LQCHCIVSNV GFNLCFFPMH YFGICGLPRR VCVYESGYAW VNMLCSIGSF VSAFSGCFFI FILWESLANK NVVIGYYGSS STLLNLCWSP VPYHSNFFVR GLFVDYSVLA F //