ID A0A0U4ID79_BOVIN Unreviewed; 215 AA. AC A0A0U4ID79; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 08-JUN-2016, entry version 4. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COX1 {ECO:0000313|EMBL:ALY05414.1}; OS Bos taurus (Bovine). OG Mitochondrion {ECO:0000313|EMBL:ALY05414.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:ALY05414.1}; RN [1] {ECO:0000313|EMBL:ALY05414.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JFC00637 {ECO:0000313|EMBL:ALY05414.1}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) 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: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. 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; KT375464; ALY05414.1; -; Genomic_DNA. 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:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 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; IPR000883; COX1. DR InterPro; IPR023616; 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. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:ALY05414.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 116 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 158 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 170 197 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 215 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:ALY05414.1}. FT NON_TER 215 215 {ECO:0000313|EMBL:ALY05414.1}. SQ SEQUENCE 215 AA; 22834 MW; FD75B4CDE7684E86 CRC64; DIGTLYLLFG AWAGMVGTAL SLLIRAELGQ PGTLLGDDQI YNVVVTAHAF VMIFFMVMPI MIGGFGNWLV PLMIGAPDMA FPRMNNMSFW LLPPSFLLLL ASSMVEAGAG TGWTVYPPLA GNLAHAGASV DLTIFSLHLA GVSSILGAIN FITTIINMKP PAMSQYQTPL FVWSVMITAV LLLLSLPVLA AGITMLLTDR NLNTTFFDPA GGGDP //