ID Q101K9_9CHON Unreviewed; 185 AA. AC Q101K9; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 2. DT 22-APR-2020, entry version 64. 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=COI {ECO:0000313|EMBL:AAZ91995.2}; OS Bathyraja lindbergi (cmmander skate). OG Mitochondrion {ECO:0000313|EMBL:AAZ91995.2}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Batoidea; Rajiformes; Bathyraja. OX NCBI_TaxID=341245 {ECO:0000313|EMBL:AAZ91995.2}; RN [1] {ECO:0000313|EMBL:AAZ91995.2} RP NUCLEOTIDE SEQUENCE. RA Spies I.B., Gaichas S., Stevenson D.E., Orr J.W., Canino M.F.; RT "DNA-based identification of Alaska skates (Amblyraja, Bathyraja and Raja: RT Rajidae) using cytochrome c oxidase subunit I (coI) variation."; RL J. Fish Biol. 69:283-292(2006). RN [2] {ECO:0000313|EMBL:AAZ91995.2} RP NUCLEOTIDE SEQUENCE. RA Canino M.F., Spies I.B., Gaichas S., Orr J.W., Stevenson D.E.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}. 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; CC Evidence={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; DQ104909; AAZ91995.2; -; Genomic_DNA. 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:0070469; C:respirasome; 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: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 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}; 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, ECO:0000313|EMBL:AAZ91995.2}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 18..48 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 69..93 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 113..136 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 148..175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..185 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAZ91995.2" FT NON_TER 185 FT /evidence="ECO:0000313|EMBL:AAZ91995.2" SQ SEQUENCE 185 AA; 19922 MW; 22B08E17F0626B3A CRC64; LIRAELSQPG TLLGDDQIYN VIVTAHAFVM IFFMVMPIMI GGFGNWLVPL MIGSPDMAFP RMNNMSFWLL PPSFLLLLAS AGVEAGAGTG WTVYPPLAGN LAHAGASVDL TIFSLHLAGI SSILASINFI TTIINMKPPA ISQYQTPLFV WSVLVTTVLL LLALPILAAA ITMLLTDRNL NTTFF //