ID A0A0M3LU51_XYLVI Unreviewed; 219 AA. AC A0A0M3LU51; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 20-JAN-2016, entry version 2. 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:AJD83365.1}; OS Xylocopa virginica (Carpenter bee). OG Mitochondrion {ECO:0000313|EMBL:AJD83365.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Apidae; Xylocopa; Xylocopoides. OX NCBI_TaxID=28638 {ECO:0000313|EMBL:AJD83365.1}; RN [1] {ECO:0000313|EMBL:AJD83365.1} RP NUCLEOTIDE SEQUENCE. RA Tripodi A.D.; RT "Population Genetics, Distributions and Phenology of Bombus Latreille, RT 1802 and Xylocopa Latreille, 1802 (Hymenoptera:Apidae)."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. 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: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {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; KM585679; AJD83365.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. 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}; 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:AJD83365.1}; 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 42 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 195 Helical. {ECO:0000256|SAM:Phobius}. FT NON_TER 1 1 {ECO:0000313|EMBL:AJD83365.1}. FT NON_TER 219 219 {ECO:0000313|EMBL:AJD83365.1}. SQ SEQUENCE 219 AA; 24664 MW; C3EA275865CAF34E CRC64; MLYIMLALWA GMIGTAMSFI IRMELSIPGN WINNDQIYNS LVTAHAFLMI FFMVMPFMIG GFGNWLIPLM LGLPDMAFPR MNNISFWLLP PSLILLLISN LFYPSPGTGW TIYPPLSSSL YHSSPSVDLM IFSLHISGIS SIMGAMNFMV TIMLMKNISM NYDKINLFSW SVFITTILLL LSLPVLAGAI TMLLFDRNFN TSFFDPMGGG DPILFQHLF //