ID COX1_TINMA STANDARD; PRT; 337 AA. AC O03554; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Cytochrome c oxidase polypeptide I (EC 1.9.3.1) (Fragment). GN MTCO1 OR COI. OS Tinamus major (Great tinamou). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=30468; RN [1] RP SEQUENCE FROM N.A. 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, RL New York (1997). 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. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O. CC -!- PATHWAY: Respiratory chain; terminal step. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE. CONTAINS 12 POTENTIAL TRANSMEMBRANE DOMAINS. CC -!- SIMILARITY: BELONGS TO THE HEME-COPPER RESPIRATORY OXIDASE FAMILY. 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; -. DR HSSP; P18401; 1FFT. DR InterPro; IPR000883; COX1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR PROSITE; PS00077; COX1; 1. KW Oxidoreductase; Heme; Copper; Mitochondrion; Transmembrane; KW Respiratory chain; Inner membrane. FT METAL 62 62 IRON (HEME A) (PROBABLE). FT METAL 241 241 COPPER B (PROBABLE). FT METAL 245 245 COPPER B (PROBABLE). FT METAL 291 291 COPPER B (PROBABLE). FT METAL 292 292 COPPER B (PROBABLE). FT NON_TER 337 337 SQ SEQUENCE 337 AA; 36805 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 //