ID A0A2R4LVL6_GRYBI Unreviewed; 494 AA. AC A0A2R4LVL6; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 05-DEC-2018, entry version 4. 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; OS Gryllus bimaculatus (Two-spotted cricket). OG Mitochondrion {ECO:0000313|EMBL:AVW85736.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Polyneoptera; Orthoptera; Ensifera; Gryllidea; OC Grylloidea; Gryllidae; Gryllinae; Gryllus. OX NCBI_TaxID=6999 {ECO:0000313|EMBL:AVW85736.1}; RN [1] {ECO:0000313|EMBL:AVW85736.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=088 {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: 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; 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:0009060; P:aerobic respiration; IEA:InterPro. 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 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, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AVW85736.1}; 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|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 201 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 246 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 282 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 317 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 329 350 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 370 391 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 403 421 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 441 464 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 494 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AVW85736.1}. FT NON_TER 494 494 {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 //