ID I1W6R0_ADADE Unreviewed; 323 AA. AC I1W6R0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 18-SEP-2019, entry version 29. 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; OC Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga; OC Cucujiformia; 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 RT (Coleoptera: Cocinellidae) and origin of ancient mitochondrial RT haplotypes in the gene 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- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC 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}; KW 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, KW 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, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 24 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 225 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 262 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 322 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 323 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFI61887.1}. FT NON_TER 323 323 {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 //