ID A0A4D6Q1K8_9NEOB Unreviewed; 510 AA. AC A0A4D6Q1K8; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 29-SEP-2021, 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}; 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; Amphibia; OC Batrachia; Anura; Neobatrachia; Ranoidea; Dicroglossidae; Dicroglossinae; OC 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., Bao Y.-X., RA 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: 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 CC [Fe(III)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|RuleBase:RU000369}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; 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 -!- 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; MH087466; QCF40277.1; -; 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|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369}; KW 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|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU000369}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000369}; Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 16..36 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 56..82 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 103..125 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 145..170 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 182..209 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 242..260 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 267..290 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 302..325 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 337..358 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 378..401 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 413..435 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 455..475 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..510 FT /note="COX1" FT /evidence="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 //