ID K0P313_HASOS Unreviewed; 240 AA. AC K0P313; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 05-DEC-2018, entry version 24. 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:CCM44533.1}; OS Haslea ostrearia (Marine diatom). OG Mitochondrion {ECO:0000313|EMBL:CCM44533.1}. OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Naviculaceae; Haslea. OX NCBI_TaxID=67476 {ECO:0000313|EMBL:CCM44533.1}; RN [1] {ECO:0000313|EMBL:CCM44533.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCC 392 {ECO:0000313|EMBL:CCM44533.1}; RX PubMed=23474208; DOI=10.1016/j.protis.2013.01.001; RA Gastineau R., Leignel V., Jacquette B., Hardivillier Y., Wulff A., RA Gaudin P., Bendahmane D., Davidovich N.A., Kaczmarska I., Mouget J.L.; RT "Inheritance of mitochondrial DNA in the Pennate diatom Haslea RT ostrearia (Naviculaceae) during auxosporulation suggests a uniparental RT transmission."; RL Protist 164:340-351(2013). 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: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399; 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; HE995427; CCM44533.1; -; 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: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|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:CCM44533.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; 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 SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 240 Cytochrome c oxidase subunit 1. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003838164. FT TRANSMEM 58 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 167 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 179 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 240 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:CCM44533.1}. FT NON_TER 240 240 {ECO:0000313|EMBL:CCM44533.1}. SQ SEQUENCE 240 AA; 26162 MW; 3477E5EC61C3874C CRC64; GAPDMAFPRM NNISFWLLPP SLLLLVESIL CEAGVGTGWT VYPPLSGITA HSGGSVDLAI FSLHLSGAAS ILGAISFICT IVNMRTKNLA FHRLPLFVWS IFITAILLLL SLPVLAGAIT MLLTDRNFNT TFFDPAGGGD PVLYQHLFWF FGHPEVYILI LPGFGIISHI VVSASRKPIF GYLGMVYAML SIGILGFIVW AHHMYTVGLD IDTRAYFTAA TMIIAIPTGI KVFSWLATLW //