ID A0A075M6W6_9COND Unreviewed; 219 AA. AC A0A075M6W6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 29-MAY-2024, entry version 34. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AIF76354.1}; OS Conus eximius. OG Mitochondrion {ECO:0000313|EMBL:AIF76354.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda; OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus. OX NCBI_TaxID=1519817 {ECO:0000313|EMBL:AIF76354.1}; RN [1] {ECO:0000313|EMBL:AIF76354.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24878223; RA Puillandre N., Bouchet P., Duda T.F.Jr., Kauferstein S., Kohn A.J., RA Olivera B.M., Watkins M., Meyer C.; RT "Molecular phylogeny and evolution of the cone snails (Gastropoda, RT Conoidea)."; RL Mol. Phylogenet. Evol. 78C:290-303(2014). 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] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, 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|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; KJ549907; AIF76354.1; -; Genomic_DNA. DR AlphaFoldDB; A0A075M6W6; -. DR SMR; A0A075M6W6; -. DR UniPathway; UPA00705; -. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:TreeGrafter. 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:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 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:AIF76354.1}; KW Mitochondrion inner membrane {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="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIF76354.1" FT NON_TER 219 FT /evidence="ECO:0000313|EMBL:AIF76354.1" SQ SEQUENCE 219 AA; 23597 MW; 40791E07F7F1F2A4 CRC64; TLYILFGMWS GLVGTALSLL IRAELGQPGA LLGDDQLYNV IVTAHAFVMI FFLVMPMMIG GFGNWLVPLM LGAPDMVFPR LNNMSFWLLP PALLLLLSSA AVESGVGTGW TVYPPLAGNL AHAGGSVDLA IFSLHLAGVS SILGAVNFIT TIINMRWQGM KFERLSLFVW SVKITAILLL LSLPVLAGAI TMLLTDRNFN TAFFDPAGGG DPILYQHLF //