ID A0A4D6Q1K8_9NEOB Unreviewed; 510 AA. AC A0A4D6Q1K8; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 31-JUL-2019, 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}; GN Name=COX1 {ECO:0000313|EMBL:QCF40277.1}; OS Fejervarya kawamurai. OG Mitochondrion {ECO:0000313|EMBL:QCF40277.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Dicroglossidae; OC Dicroglossinae; Fejervarya. OX NCBI_TaxID=1772025 {ECO:0000313|EMBL:QCF40277.1}; RN [1] {ECO:0000313|EMBL:QCF40277.1} RP NUCLEOTIDE SEQUENCE. RA Cheng J.-X., Cai Y.-T., Zheng Y.-J., Zhang J.-Y., Storey K.B., RA Bao Y.-X., Yu D.-N.; RT "The complete mitochondrial genome of Fejervarya kawamurai (Anura: RT Dicroglossidae) and its phylogeny."; RL Mitochondrial DNA Part B Resour 3:551-553(2018). RN [2] {ECO:0000313|EMBL:QCF40277.1} RP NUCLEOTIDE SEQUENCE. RA Cheng J., Yu D., Bao Y.; RL Submitted (MAR-2018) 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, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369, CC ECO:0000256|SAAS:SAAS01116619}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887552}. 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; MH087466; QCF40277.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. 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, ECO:0000256|SAAS:SAAS00887236}; KW Electron transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711094}; KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161}; KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183}; KW Membrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711155}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:QCF40277.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711097}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711106}; 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}; KW Transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 16 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 82 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 145 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 209 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 242 260 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 267 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 302 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 401 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 413 435 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 455 475 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 510 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 510 AA; 56529 MW; 2AA3E439BDE2FB57 CRC64; MFSRWLFSTN HKDIGTMYLI FGAWAGMIGT ALSLLIRAEL SQPGTLLGDD PIYNVVVTAH AFVMIFFMVM PILIGGFGNW LIPLMIGAPD MAFPRMNNMS FWLLPPSFFL LLASSTVEAG AGTGWTVYPP LAGNLAHAGP SVDLAIFSLH LAGVSSILGA INFITTIINM KPPSTTQYQT PLFVWSVLIT AVLLLLSLPV LAAGITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP EVYILILPGF GIISHVVAYY STKKEPFGYM GMVWAMLSIG LLGFIVWAHH MFTTDLNVDT RAYFTSATMI IAIPTGVKVF SWLATMYGGI IKWEAPMLWA LGFIFLFTVG GLTGIVLANS SIDIVLHDTY YVVAHFHYVL SMGAVFAIMA GFVHWFPLFT GFTFHKTWAK AQFAVMFTGV NVTFFPQHFL GLAGMPRRYS DYPDAYTLWN TISSMGSLIS LVGVIMLMFI IWEAFSSKRL FSNPKLTTTN IEWLLGFPPQ HHTFEEASYS //