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-JUL-1998 (Rel. 36, 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; Archosauria; Aves; OC Palaeognathae; Tinamiformes; Tinamidae; Tinamus. 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) = 2 H(2)O + CC 4 FERRICYTOCHROME C. CC -!- PATHWAY: TERMINAL STEP IN THE RESPIRATORY CHAIN. 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; P98002; 1AR1. DR PFAM; PF00115; COX1; 1. 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; BD0340D0 CRC32; 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 //