ID A0A0D3Q333_SPIER Unreviewed; 521 AA. AC A0A0D3Q333; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-NOV-2016, entry version 8. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {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; Platyhelminthes; Cestoda; Eucestoda; OC 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., RA Wang Z.Q.; RT "Genetic Structure Analysis of Spirometra erinaceieuropaei Isolates RT from Central and Southern China."; RL PLoS ONE 10:E0119295-E0119295(2015). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {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:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 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; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. 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|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AJC01987.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 21 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 173 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 185 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 263 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 270 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 302 326 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 397 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 409 429 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 449 474 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 3 505 COX1. {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 //