ID A0A411KAD1_ANDDA Unreviewed; 516 AA. AC A0A411KAD1; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-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:QBC75164.1}; OS Andrias davidianus (Chinese giant salamander) (Sieboldia davidiana). OG Mitochondrion {ECO:0000313|EMBL:QBC75164.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Caudata; Cryptobranchoidea; Cryptobranchidae; OC Andrias. OX NCBI_TaxID=141262 {ECO:0000313|EMBL:QBC75164.1}; RN [1] {ECO:0000313|EMBL:QBC75164.1} RP NUCLEOTIDE SEQUENCE. RA Turvey S.T., Melissa M.M., Ian B., Selina B., Benjamin T., RA Robert M.W., Andrew C.A.; RT "Historical museum collections determine the evolutionary history of RT cryptic species radiation in the world's largest amphibians."; RL Submitted (NOV-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 -!- 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; MK177469; QBC75164.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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; 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. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887236}; 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:QBC75164.1}; 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 16 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 251 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 272 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 412 432 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 452 473 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 512 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 516 AA; 56595 MW; F6488EF39A66AADB CRC64; MMITRWLFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGTLLGD DQIYNVIVTA XXXXXXXXXV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGIEA GAGTGWTVYP PLASNLAHAG ASVDLTIFSL HXXXXSSILG AINFITTSIN MKPPAMTQYQ TPLFVWSVLI TAILLLLSLP VLAAGITMLL TDRNLNTTFF DPSGGXXXXX XXXXXXXXXX XXVYILILPG FGMIXXXXXX XXXXXXXXXX XGMVWAMMSI GLLGFIVWAH HMFTVDLNVD TRAYFTSATM IIAIPTGVKV FSWLATMHGG SIKWDAAMLW XXXXXXXFTV GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF SGYTLHATWS KIHFGVMFLG VNLTFFPQHF LGXXXXXXXX XXXXXXXXXX NTASSIGSLI SMIAVVMIMF IIWEAFSAKR EISTTDLSST NVEWLHGCPP PHHTYEEPSY VQTRVN //