ID I1W6R0_ADADE Unreviewed; 323 AA. AC I1W6R0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 27-MAR-2024, entry version 45. 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:AFI61887.1}; OS Adalia decempunctata (Ten-spotted ladybird beetle). OG Mitochondrion {ECO:0000313|EMBL:AFI61887.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia; OC Coccinelloidea; Coccinellidae; Coccinellinae; Coccinellini; Adalia. OX NCBI_TaxID=115343 {ECO:0000313|EMBL:AFI61887.1}; RN [1] {ECO:0000313|EMBL:AFI61887.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1 {ECO:0000313|EMBL:AFI61886.1}, and 2 RC {ECO:0000313|EMBL:AFI61887.1}; RA Shaikevich E.V.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFI61887.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1 {ECO:0000313|EMBL:AFI61886.1}, and 2 RC {ECO:0000313|EMBL:AFI61887.1}; RA Zakharov I., Shaikevich E.; RT "Comparative study of mtDNA in species of the genus Adalia (Coleoptera: RT Cocinellidae) and origin of ancient mitochondrial haplotypes in the gene RT pool of Adalia bipunctata."; RL Eur. J. Entomol. 110:427-433(2013). 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, 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; JQ757052; AFI61886.1; -; Genomic_DNA. DR EMBL; JQ757053; AFI61887.1; -; Genomic_DNA. DR AlphaFoldDB; I1W6R0; -. DR UniPathway; UPA00705; -. 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; 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; IPR023615; Cyt_c_Oxase_su1_BS. 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. 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}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AFI61887.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 24..54 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 75..97 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 117..142 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 154..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 201..225 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 237..262 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 274..296 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 303..322 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..323 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFI61887.1" FT NON_TER 323 FT /evidence="ECO:0000313|EMBL:AFI61887.1" SQ SEQUENCE 323 AA; 35162 MW; 408EFE2E03871072 CRC64; GTSLSIIIRL ELGTTNSLIG NDQIYNVIVT AHAFIMIFFM VMPIMIGGFG NWLVPLMIGA PDMAFPRLNN MSFWLLPPAL TLLISSSIVE MGAGTGWTVY PPLSSNLAHN GPSVDLVIFS LHLAGISSIL GAVNFISTIM NMRPNGMNLD KTPLFVWSVL ITAILLLLSL PVLAGAITML LTDRNINTSF FDPTGGGDPV LYQHLFWFFG HPEVYILILP GFGMISHIIT QESGKKIAFG ALGMIYAMLA IGLLGFVVWA HHMFTVGMDV DTRAYFTSAT MIIAVPTGIK IFSWLATLHG VQFIFTPSLL WTLGFLFLFT IGG //