ID A0A0K0Q4W9_9COLE Unreviewed; 219 AA. AC A0A0K0Q4W9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 11-DEC-2019, entry version 15. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AKR06426.1}; OS Ptomaphaginus cf. latimanus BOLD:ACK0183. OG Mitochondrion {ECO:0000313|EMBL:AKR06426.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Coleoptera; Polyphaga; Staphyliniformia; Leiodidae; OC Cholevinae; Ptomaphaginus. OX NCBI_TaxID=1685025 {ECO:0000313|EMBL:AKR06426.1}; RN [1] {ECO:0000313|EMBL:AKR06426.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26266979; DOI=10.1038/nature14949; RA Merckx V.S., Hendriks K.P., Beentjes K.K., Mennes C.B., Becking L.E., RA Peijnenburg K.T., Afendy A., Arumugam N., de Boer H., Biun A., Buang M.M., RA Chen P.P., Chung A.Y., Dow R., Feijen F.A., Feijen H., Feijen-van Soest C., RA Geml J., Geurts R., Gravendeel B., Hovenkamp P., Imbun P., Ipor I., RA Janssens S.B., Jocque M., Kappes H., Khoo E., Koomen P., Lens F., RA Majapun R.J., Morgado L.N., Neupane S., Nieser N., Pereira J.T., Rahman H., RA Sabran S., Sawang A., Schwallier R.M., Shim P.S., Smit H., Sol N., RA Spait M., Stech M., Stokvis F., Sugau J.B., Suleiman M., Sumail S., RA Thomas D.C., van Tol J., Tuh F.Y., Yahya B.E., Nais J., Repin R., Lakim M., RA Schilthuizen M.; RT "Evolution of endemism on a young tropical mountain."; RL Nature 524:347-350(2015). RN [2] {ECO:0000313|EMBL:AKR06426.1} RP NUCLEOTIDE SEQUENCE. RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {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=1.9.3.1; CC Evidence={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; KP978416; AKR06426.1; -; 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:UniProtKB-EC. 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 PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 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}; 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, ECO:0000313|EMBL:AKR06426.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..25 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 37..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 133..155 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..219 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AKR06426.1" FT NON_TER 219 FT /evidence="ECO:0000313|EMBL:AKR06426.1" SQ SEQUENCE 219 AA; 23463 MW; 4F5E5EB2655BFD79 CRC64; TLYFIFGAWS GMLGTSLSLL IRAELGNPGS LIGDDQIYNV IVTAHAFIMI FFMVMPIVIG GFGNWLVPLM LGAPDMAFPR MNNMSFWLLP PSLTLLLMSS MVESGAGTGW TVYPPLSANI AHSGPSVDLA IFSLHLAGIS SILGAVNFIT TVINMRSPGM SLDKIPLFVW SVAITALLLL LSLPVLAGAI TMLLTDRNLN TSFFDPAGGG DPILYQHLF //