ID M1EY13_AGRDO Unreviewed; 417 AA. AC M1EY13; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 22-FEB-2023, entry version 40. 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:AEZ68375.1}; OS Agriosphodrus dohrni (Japanese assassin-bug). OG Mitochondrion {ECO:0000313|EMBL:AEZ68375.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; OC Cimicomorpha; Reduviidae; Harpactorinae; Harpactorini; Agriosphodrus. OX NCBI_TaxID=184613 {ECO:0000313|EMBL:AEZ68375.1}; RN [1] {ECO:0000313|EMBL:AEZ68375.1} RP NUCLEOTIDE SEQUENCE. RA Liu H., Li H., Ishikawa T., Su H.Z., Cai Z.W., Kamitani S.; RT "Invasion of the assassin bug Agriosphodrus dohrni (Hemiptera: Reduviidae) RT to Japan: Source estimation inferred from mitochondrial and nuclear gene RT sequences."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; 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 -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000256|ARBA:ARBA00011164}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, 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; JN089467; AEZ68375.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro. 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 CDD; cd01663; Cyt_c_Oxidase_I; 1. 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 InterPro; IPR033944; Cyt_c_oxase_su1_dom. 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; 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:AEZ68375.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1..39 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 40..417 FT /note="Cytochrome c oxidase subunit 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004014510" FT TRANSMEM 62..87 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 99..126 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 146..171 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 183..207 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 219..242 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 254..275 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 295..316 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 328..346 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 366..389 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..417 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AEZ68375.1" FT NON_TER 417 FT /evidence="ECO:0000313|EMBL:AEZ68375.1" SQ SEQUENCE 417 AA; 46006 MW; 40438448051B50EB CRC64; LMIGAPDMAF PRMNNMSFWL LPPSLTLLLI SSIAEGGAGT GWTVYPPLSS NIAHSGASVD LAIFSLHLAG VSSILGAVNF ISTIINMRPA GMTPERIPLF VWSVGITALL LLLSLPVLAG AITMLLTDRN FNTSFFDPSG GGDPILYQHL FWFFGHPXXX XXXXXXXXLI SHIISMETGK NEAFGSLGMI YAMMTIGLLG FIVWAHHMFT VGMDVDTRAY FTSATMIIAV PTGIKIFSWL ATLHGSKQLS TPSLLWALGF IFLFTIGGLT GVVLANSSID ITLHDTYYVV AHFHYVLSMG AVFAIMGSFI QWYPLFSGLT MNPKWLKIQF FTMFVGVNLT FFPQHFLGLS GMPRRYSDYP DSYTCWNIIS SLGSTISLIS IMLFIFIIWE SMVTKRQVLV AKQTSSNIEW MQKYPPA //