ID B7TIY3_9COLE Unreviewed; 219 AA. AC B7TIY3; B8Y1F8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 2. DT 27-MAR-2024, entry version 62. 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:ACL79630.2}; OS Hatchiana sp. THK-2008. OG Mitochondrion {ECO:0000313|EMBL:ACJ54125.2}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea; OC Cantharidae; Cantharinae; Hatchiana. OX NCBI_TaxID=568066 {ECO:0000313|EMBL:ACJ54125.2}; RN [1] {ECO:0000313|EMBL:ACN41867.1} RP NUCLEOTIDE SEQUENCE. RA Kang T.H., Kim J.I., Kim M.A., Park H.C.; RT "Taxonomic review of the genus Hatchiana Fender, 1966 (Coleoptera: RT Cantharidae) in Korea based on morphological data and DNA barcodes."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACJ54125.2} RP NUCLEOTIDE SEQUENCE. RA Kang T.H., Park H.C., Kim J.I.; RT "A review of the genus Hatchiana Fender, 1966 (Coleoptera: Cantharidae) RT from Korea using morphological and molecular data."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ACL79630.2} RP NUCLEOTIDE SEQUENCE. RA Kang T.H., Park H.C., Kim J.I., Kim M.A.; RT "Taxonomic review of the genus Hatchiana fender, 1966 (Coleoptera: RT Cantharidae) in Korea based on morphological data and DNA barcode."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ADC36182.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HASPAA {ECO:0000313|EMBL:ADC36182.1}, HASPAB RC {ECO:0000313|EMBL:ADC36183.1}, and HASPAC RC {ECO:0000313|EMBL:ADC36184.1}; RA Kang T.H., Park H.C., Han T.M., Kim M.A., Lee Y.B.; RT "Taxonomic Review of the Genus Hatchiana Fender 1966 (Coleoptera: RT Cantharidae) in Korea Based on Morphological Data and DNA Barcodes."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. 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: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, CC 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; FJ232990; ACJ54125.2; -; Genomic_DNA. DR EMBL; FJ462775; ACL79630.2; -; Genomic_DNA. DR EMBL; FJ646621; ACN41867.1; -; Genomic_DNA. DR EMBL; GU323939; ADC36182.1; -; Genomic_DNA. DR EMBL; GU323940; ADC36183.1; -; Genomic_DNA. DR EMBL; GU323941; ADC36184.1; -; Genomic_DNA. DR AlphaFoldDB; B7TIY3; -. 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 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. 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:ACJ54125.2}; KW Mitochondrion inner membrane {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 46..67 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 88..110 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 130..155 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..219 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACJ54125.2" FT NON_TER 219 FT /evidence="ECO:0000313|EMBL:ACJ54125.2" SQ SEQUENCE 219 AA; 23718 MW; 10D9D2D3CB4D4482 CRC64; TLYFIFGAWS GSLGLALSLL IRAELGTPGT LIGNDQLYNV IVTAHAFIMI FFMVMPIMIG GFGNWLVPLM LGAPDMAFPR MNNMSFWFLP PSLMFLLMSS MVESGAGTGW TVYPPLSANI AHSGPSVDLA IFSLHMAGIS SILGAVNFIS TIMNMKPPSM KFDQMPLFVW SVGITALLLL LSLPVLAGAI TMLLSDRNLN TSFFDPMGGG DPILYQHLF //