ID Q8HBS8_9SAUR Unreviewed; 170 AA. AC Q8HBS8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 25-NOV-2008, entry version 31. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE Flags: Fragment; GN Name=COI; OS Orthriophis taeniurus. OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Colubridae; Colubrinae; Orthriophis. OX NCBI_TaxID=74398; RN [1] RP NUCLEOTIDE SEQUENCE. RA Utiger U., Helfenberger N., Schaetti B., Schmidt C., Ruf M., RA Ziswiler V.; RT "Molecular systematics and phylogeny of Old and New World ratsnakes, RT Elaphe auct., and related genera (Reptilia, Squamata, Colubridae)."; RL Russ. J. Herpetol. 9:105-124(2002). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). 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; AY122723; AAM81041.1; -; Genomic_DNA. DR EMBL; AY122724; AAM81042.1; -; Genomic_DNA. DR EMBL; AY122725; AAM81043.1; -; Genomic_DNA. DR SMR; Q8HBS8; 1-170. DR HOVERGEN; Q8HBS8; -. DR GO; GO:0016021; C:integral to membrane; IEA:InterPro. DR GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR000883; Cyt_c_oxidase_su1. DR Gene3D; G3DSA:1.20.210.10; COX1; 1. DR PANTHER; PTHR10422; COX1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Heme; Membrane; Mitochondrion; KW Oxidoreductase; Respiratory chain; Transmembrane; Transport. FT NON_TER 1 1 FT NON_TER 170 170 SQ SEQUENCE 170 AA; 18510 MW; 6FA06BFE78C547B4 CRC64; AGTGWTVYPP LSGNLVHSGP SVDLAIFSLH LAGASSILGA INFITTCINM KPKSMPMFNI PLFVWSVLIT AIMLLLALPV LAAAITMLLT DRNLNTSFFD PCGGGDPVLF QHLFWFFGHP EVYILILPGF GIVSSIITFY TGKKNTFGYT SMIWAMMSIA ILGFVVWAHH //