ID A0A3S6J279_9EUCA Unreviewed; 511 AA. AC A0A3S6J279; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-JUL-2019, entry version 3. 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:ASS30702.1}; OS Birgus latro. OG Mitochondrion {ECO:0000313|EMBL:ASS30702.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; OC Anomura; Paguroidea; Coenobitidae; Birgus. OX NCBI_TaxID=177283 {ECO:0000313|EMBL:ASS30702.1}; RN [1] {ECO:0000313|EMBL:ASS30702.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL39 {ECO:0000313|EMBL:ASS30702.1}; RA Gan H.M., Tan M.H., Lee Y.P., Austin C.M.; RT "Complete mitochondrial genome of Birgus latro isolate BL39."; RL Submitted (DEC-2016) 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; KY352241; ASS30702.1; -; 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, 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:ASS30702.1}; 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 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 357 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 377 398 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 410 428 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 471 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 510 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 511 AA; 56356 MW; 6CFFACC5B70EEA7A CRC64; MQRWFFSTNH KDIGTLYFIL GAWAGMVGTS LSLVIRAELG QPGSLIGDDQ IYNVVVTAHA FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPSLTLL LTSGMVESGV GTGWTVYPPL SAAIAHAGAS VDLGIFSLHL AGVSSILGAI NFMTTVINMR PRGMTMDRMP LFVWSVFITA ILLLISLPVL AGAITMLLTD RNLNTSFFDP AGGGDPVLYQ HLFWFFGHPE VYILILPAFG MISHIVSQES GKKEAFGSLG MIYAMLAIGI LGFVVWAHHM FTVGMDVDTR AYFTSATMII AVPTGIKVFS WLGTLHGTQI NYSPSMCWSL GFIFLFTVGG LTGVVLANSS IDIILHDTYY VVAHFHYVLS MGAVFGIFAG LAHWYPLFTG LALNPKWLKI HFCTMFLGVN ITFFPQHFLG LNGMPRRYSD YPDAYTAWNV LSSLGSMVSL VAVLGFIIII WESLVSYRVV VFSMYLPTSI EWEHSYPPAD HSYMEIPLVS N //