ID COX1_TINMA Reviewed; 337 AA. AC O03554; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-DEC-2019, entry version 94. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE AltName: Full=Cytochrome c oxidase polypeptide I; DE Flags: Fragment; GN Name=MT-CO1; Synonyms=COI, COXI, MTCO1; OS Tinamus major (Great tinamou) (Tetrao major). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=30468; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lee K., Feinstein J., Cracraft J.; RT "Phylogenetic relationships of the ratite birds: resolving conflicts RT between molecular and morphological data sets."; RL (In) Mindell D.P. (eds.); RL Avian molecular evolution and systematics, pp.1-1, Academic Press, New York RL (1997). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000305}. 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; U76063; AAB61331.1; -; Genomic_DNA. DR SMR; O03554; -. 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; ISS:UniProtKB. 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 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 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; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Respiratory chain; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..>337 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183426" FT TRANSMEM 18..38 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 64..84 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 103..123 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 146..166 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 269..289 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 311..331 FT /note="Helical" FT /evidence="ECO:0000255" FT METAL 62 FT /note="Iron (heme A axial ligand)" FT /evidence="ECO:0000305" FT METAL 241 FT /note="Copper B" FT /evidence="ECO:0000305" FT METAL 245 FT /note="Copper B" FT /evidence="ECO:0000305" FT METAL 291 FT /note="Copper B" FT /evidence="ECO:0000305" FT METAL 292 FT /note="Copper B" FT /evidence="ECO:0000305" FT CROSSLNK 241..245 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250" FT NON_TER 337 SQ SEQUENCE 337 AA; 36806 MW; 637DBE38B678F319 CRC64; MTFITRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVVVT AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE TGVGTGWTVY PPLASNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALTQY QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPI LYQHLFWFFG HPEVYILILP GFGIISHVVA YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDP //