ID A0A2U8XGT3_9BIVA Unreviewed; 182 AA. AC A0A2U8XGT3; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 11-DEC-2019, entry version 6. 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:AWN57548.1}; OS Ctenoides scaber. OG Mitochondrion {ECO:0000313|EMBL:AWN57548.1}. OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia; OC Limoida; Limidae; Ctenoides. OX NCBI_TaxID=1411920 {ECO:0000313|EMBL:AWN57548.1}; RN [1] {ECO:0000313|EMBL:AWN57548.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Florida_2 {ECO:0000313|EMBL:AWN57546.1}, Florida_3 RC {ECO:0000313|EMBL:AWN57547.1}, Florida_7 RC {ECO:0000313|EMBL:AWN57548.1}, Florida_8 RC {ECO:0000313|EMBL:AWN57549.1}, Haiti_1 {ECO:0000313|EMBL:AWN57550.1}, RC Haiti_10 {ECO:0000313|EMBL:AWN57551.1}, Haiti_2 RC {ECO:0000313|EMBL:AWN57552.1}, Haiti_3 {ECO:0000313|EMBL:AWN57553.1}, RC Haiti_4 {ECO:0000313|EMBL:AWN57554.1}, Haiti_5 RC {ECO:0000313|EMBL:AWN57555.1}, Haiti_6 {ECO:0000313|EMBL:AWN57556.1}, RC Haiti_7 {ECO:0000313|EMBL:AWN57557.1}, Haiti_8 RC {ECO:0000313|EMBL:AWN57558.1}, Haiti_9 {ECO:0000313|EMBL:AWN57559.1}, RC and UFID_505125 {ECO:0000313|EMBL:AWN57561.1}; RA Dougherty L.F., Li J.; RT "Molecular Phylogeny and Morphological Distinctions of Two Popular RT Bivalves, Ctenoides scaber and Ctenoides mitis."; RL J Mar Biol 2017:1624014-1624014(2017). 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; MF540382; AWN57546.1; -; Genomic_DNA. DR EMBL; MF540383; AWN57547.1; -; Genomic_DNA. DR EMBL; MF540384; AWN57548.1; -; Genomic_DNA. DR EMBL; MF540385; AWN57549.1; -; Genomic_DNA. DR EMBL; MF540386; AWN57550.1; -; Genomic_DNA. DR EMBL; MF540387; AWN57551.1; -; Genomic_DNA. DR EMBL; MF540388; AWN57552.1; -; Genomic_DNA. DR EMBL; MF540389; AWN57553.1; -; Genomic_DNA. DR EMBL; MF540390; AWN57554.1; -; Genomic_DNA. DR EMBL; MF540391; AWN57555.1; -; Genomic_DNA. DR EMBL; MF540392; AWN57556.1; -; Genomic_DNA. DR EMBL; MF540393; AWN57557.1; -; Genomic_DNA. DR EMBL; MF540394; AWN57558.1; -; Genomic_DNA. DR EMBL; MF540395; AWN57559.1; -; Genomic_DNA. DR EMBL; MF540397; AWN57561.1; -; 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:AWN57548.1}; 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 21..50 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 70..97 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 118..139 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 151..178 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..182 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AWN57548.1" FT NON_TER 182 FT /evidence="ECO:0000313|EMBL:AWN57548.1" SQ SEQUENCE 182 AA; 19741 MW; 5221CE8852C87735 CRC64; FSLVIRMQLS RPGQWLGDSQ LYNVVVTSHA LLMIFFFVMP VLIGGFGNWL IPLMIGSPDM AFPRLNNLSF WLLVPALFLV LSSMRVGGGS GSGWTLYPPL SGLIGEHSSC VDYTIVSLHL AGLSSMTGAI NFLSTIYLSR PDAMVGERLP LYGWSISVTA VLLLVSIPVL AGALTMLLTD RH //