ID A0A2R4LVL6_GRYBI Unreviewed; 494 AA. AC A0A2R4LVL6; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 19-JAN-2022, entry version 15. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; OS Gryllus bimaculatus (Two-spotted cricket). OG Mitochondrion {ECO:0000313|EMBL:AVW85736.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Polyneoptera; Orthoptera; Ensifera; Gryllidea; Grylloidea; OC Gryllidae; Gryllinae; Gryllus. OX NCBI_TaxID=6999 {ECO:0000313|EMBL:AVW85736.1}; RN [1] {ECO:0000313|EMBL:AVW85736.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H088 {ECO:0000313|EMBL:AVW85736.1}; RA He Z., Lu H.; RT "A taxonomic study on the species of genus Teleogryllus of East Asia RT (Insect, Orthoptera, Gryllidae)."; RL Submitted (MAY-2017) 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:ARBA00024637}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00024637}; 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane CC protein {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; MF046161; AVW85736.1; -; 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:0045277; C:respiratory chain complex IV; IEA:InterPro. 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 CDD; cd01663; Cyt_c_Oxidase_I; 1. 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 InterPro; IPR033944; 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. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AVW85736.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 7..28 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 48..70 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 91..109 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 129..153 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 174..201 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 221..246 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 258..282 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 294..317 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 329..350 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 370..391 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 403..421 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 441..464 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..494 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AVW85736.1" FT NON_TER 494 FT /evidence="ECO:0000313|EMBL:AVW85736.1" SQ SEQUENCE 494 AA; 54475 MW; CA145290F9F974F3 CRC64; TNHKDIGTLY FIFGAWAGMV GTSLSILIRT ELGQPGYLIG DDQTYNVIVT AHAFIMIFFM VMPIMIGGFG NWLVPLMLGA PDMAFPRMNN MSFWLLPPSL TLLLTSSMVE NGAGTGWTVY PPLSTGIAHA GASVDLAIFS LHLAGISSIL GAVNFITTMI NMRAPGMSLD QTPLFVWAVG ITALLLLLSL PVLAGAITML LTDRNLNTSF FDPAGGGDPI LYQHLFWFFG HPEVYILILP GFGMISHIIS QESGKKEAFG TLGMIYAMLA IGLLGFVVWA HHMFTVGMDV DTRAYFTSAT MIIAVPTGIK IFSWLATLHG SQLSYNPSLL WSLGFVFLFT IGGLTGIVLA NSSIDIILHD TYYVVAHFHY VLSMGAVFAI MAGFIHWYPL FSGLTMNPKW LKMQFMVMFI GVNLTFFPQH FLGLAGMPRR YSDYPDAYTS WNILSSLGST ISLIGIIMLI FILWESMISN RKLMFPMNLN SSLEWYQNLP PAEH //