ID I1W6R0_ADADE Unreviewed; 323 AA. AC I1W6R0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 11-DEC-2019, entry version 30. 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: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; Holometabola; Coleoptera; Polyphaga; Cucujiformia; Coccinellidae; OC 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: 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; JQ757052; AFI61886.1; -; Genomic_DNA. DR EMBL; JQ757053; AFI61887.1; -; 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 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}; 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:AFI61887.1}; 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 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="COX1" 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 //