ID K4K2Z3_SALFO Unreviewed; 421 AA. AC K4K2Z3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 24-JUL-2024, entry version 53. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=CO1 {ECO:0000313|EMBL:AFU93385.1}; OS Salvelinus fontinalis (Brook trout) (Salmo fontinalis). OG Mitochondrion {ECO:0000313|EMBL:AFU93385.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Salvelinus. OX NCBI_TaxID=8038 {ECO:0000313|EMBL:AFU93385.1}; RN [1] {ECO:0000313|EMBL:AFU93385.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=#89 {ECO:0000313|EMBL:AFU93384.1}, and #90 RC {ECO:0000313|EMBL:AFU93385.1}; RX PubMed=23071608; DOI=10.1371/journal.pone.0046662; RA Crete-Lafreniere A., Weir L.K., Bernatchez L.; RT "Framing the salmonidae family phylogenetic portrait: a more complete RT picture from increased taxon sampling."; RL PLoS ONE 7:E46662-E46662(2012). 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 Fe(III)- CC [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|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; 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|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, 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; JX960958; AFU93384.1; -; Genomic_DNA. DR EMBL; JX960959; AFU93385.1; -; Genomic_DNA. DR AlphaFoldDB; K4K2Z3; -. DR UniPathway; UPA00705; -. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:TreeGrafter. 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:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 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}; 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|RuleBase:RU000369, ECO:0000313|EMBL:AFU93385.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..23 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 35..57 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 131..153 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 165..192 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 225..243 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 250..273 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 285..308 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 320..341 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 361..382 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 394..413 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..421 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFU93385.1" FT NON_TER 421 FT /evidence="ECO:0000313|EMBL:AFU93385.1" SQ SEQUENCE 421 AA; 46048 MW; DD407E029C55AAEE CRC64; YLVFGAWAGM VGTALSLLIR AELSQPGALL GDDQIYNVIV TAHAFVMIFF MVMPIMIGGF GNWLIPLMIG APDMAFPRMN NMSFWLLPPS FLLLLASSGV EAGAGTGWTV YPPLAGNLAH AGASVDLTIF SLHLAGISSI LGAINFITTI INMKPPAISQ YQTPLFVWAV LVTAVLLLLS LPVLAAGITM LLTDRNLNTT FFDPAGGGDP ILYQHLFWFF GHPEVYILIL PGFGMISHIV AYYSGKKEPF GYMGMVWAMM AIGLLGFIVW AHHMFTVGMD VDTRAYFTSA TMIIAIPTGV KVFSWLATLH GGSIKWETPL LWALGFIFLF TVGGLTGIVL ANSSLDIVLH DTYYVVAHFH YVLSMGAVFA IMGAFVHWFP LFTGYTLHST WTKIHFGIMF IGVNLTFFPQ HFLGLAGMPR R //