ID A0A2U8XGT3_9BIVA Unreviewed; 182 AA. AC A0A2U8XGT3; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 03-AUG-2022, entry version 16. 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:AWN57548.1}; OS Ctenoides scaber. OG Mitochondrion {ECO:0000313|EMBL:AWN57548.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Pteriomorphia; 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: 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; 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: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 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 //