ID A0A097C6W9_9COLE Unreviewed; 219 AA. AC A0A097C6W9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 05-DEC-2018, entry version 19. 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:AIS77891.1}; OS Anisotoma humeralis. OG Mitochondrion {ECO:0000313|EMBL:AIS77891.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga; OC Staphyliniformia; Leiodidae; Leiodinae. OX NCBI_TaxID=355579 {ECO:0000313|EMBL:AIS77891.1}; RN [1] {ECO:0000313|EMBL:AIS77891.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25255319; RA Pentinsaari M., Hebert P.D., Mutanen M.; RT "Barcoding beetles: a regional survey of 1872 species reveals high RT identification success and unusually deep interspecific divergences."; RL PLoS ONE 9:E108651-E108651(2014). RN [2] {ECO:0000313|EMBL:AJA39373.1} RP NUCLEOTIDE SEQUENCE. RA Rougerie R.; RT "PASSIFOR: A reference library of DNA barcodes for French saproxylic RT beetles (Insecta, Coleoptera)."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AJB85687.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25469559; DOI=10.1111/1755-0998.12354; RA Hendrich L., Moriniere J., Haszprunar G., Hebert P.D., Hausmann A., RA Kohler F., Balke M.; RT "A comprehensive DNA barcode database for Central European beetles RT with a focus on Germany: adding more than 3500 identified species to RT BOLD."; RL Mol. Ecol. Resour. 15:795-818(2015). RN [4] {ECO:0000313|EMBL:ARB55382.1} RP NUCLEOTIDE SEQUENCE. RA Rulik B., Ahrens D.; RT "Using taxonomic consistency with semi-automatized data pre-processing RT for high quality Barcode data submissions - a case study on German RT beetles."; RL Submitted (MAR-2016) 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: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399; 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; KJ962141; AIS77057.1; -; Genomic_DNA. DR EMBL; KJ962690; AIS77606.1; -; Genomic_DNA. DR EMBL; KJ962975; AIS77891.1; -; Genomic_DNA. DR EMBL; KM286060; AJA39373.1; -; Genomic_DNA. DR EMBL; KM439972; AJB85687.1; -; Genomic_DNA. DR EMBL; KM443088; AJB88803.1; -; Genomic_DNA. DR EMBL; KM443591; AJB89306.1; -; Genomic_DNA. DR EMBL; KM451176; AJB96891.1; -; Genomic_DNA. DR EMBL; KM452262; AJB97977.1; -; Genomic_DNA. DR EMBL; KU908962; ARB55382.1; -; Genomic_DNA. DR EMBL; KU910541; ARB56961.1; -; Genomic_DNA. DR EMBL; KU911936; ARB58356.1; -; Genomic_DNA. DR EMBL; KU911943; ARB58363.1; -; Genomic_DNA. DR EMBL; KU915090; ARB61510.1; -; Genomic_DNA. DR EMBL; KU916466; ARB62886.1; -; Genomic_DNA. DR EMBL; KU918362; ARB64782.1; -; 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:respiratory chain; 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 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:AIS77891.1}; 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 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 194 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 219 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AIS77891.1}. FT NON_TER 219 219 {ECO:0000313|EMBL:AIS77891.1}. SQ SEQUENCE 219 AA; 23597 MW; F503CE3F85564173 CRC64; TLYFIFGAWS GMVGTSLSIL IRAELGTPGS LIGDDQIYNV IVTAHAFVMI FFMVMPIMIG GFGNWLVPLM LGAPDMAFPR MNNMSFWLLP PSLTLLLMSS MVENGAGTGW TVYPPLSANI SHSGSSVDLA IFSLHLAGIS SILGAVNFIT TVINMRSIGM TFDKMPLFVW SVVITALLLL LSLPVLAGAI TMLLTDRNLN TSFFDPAGGG DPILYQHLF //