ID D3TSY8_9CRUS Unreviewed; 149 AA. AC D3TSY8; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 11-DEC-2019, entry version 40. 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:ACN37924.1}; OS Nebalia kensleyi. OG Mitochondrion {ECO:0000313|EMBL:ACN37924.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Phyllocarida; Leptostraca; Nebaliidae; Nebalia. OX NCBI_TaxID=586406 {ECO:0000313|EMBL:ACN37924.1}; RN [1] {ECO:0000313|EMBL:ACN37924.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TomalesBay73 {ECO:0000313|EMBL:ACN37924.1}, TomalesBay74 RC {ECO:0000313|EMBL:ACN37925.1}, TomalesBay76 RC {ECO:0000313|EMBL:ACN37926.1}, TomalesBay77 RC {ECO:0000313|EMBL:ACN37927.1}, TomalesBay78 RC {ECO:0000313|EMBL:ACN37928.1}, TomalesBay79 RC {ECO:0000313|EMBL:ACN37929.1}, TomalesBay82 RC {ECO:0000313|EMBL:ACN37930.1}, TomalesBay84 RC {ECO:0000313|EMBL:ACN37931.1}, TomalesBay86 RC {ECO:0000313|EMBL:ACN37932.1}, TomalesBay87 RC {ECO:0000313|EMBL:ACN37933.1}, TomalesBay88 RC {ECO:0000313|EMBL:ACN37934.1}, TomalesBay89 RC {ECO:0000313|EMBL:ACN37935.1}, and TomalesBay90 RC {ECO:0000313|EMBL:ACN37936.1}; RA Haney T.A., Jacobs D.K.; RT "Cryptic diversity and phylogeography of Nebalia (Crustacea: Leptostraca) RT along the western coast of North America."; RL Submitted (AUG-2008) 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 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {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; EC=1.9.3.1; 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; FJ170132; ACN37924.1; -; Genomic_DNA. DR EMBL; FJ170133; ACN37925.1; -; Genomic_DNA. DR EMBL; FJ170134; ACN37926.1; -; Genomic_DNA. DR EMBL; FJ170135; ACN37927.1; -; Genomic_DNA. DR EMBL; FJ170136; ACN37928.1; -; Genomic_DNA. DR EMBL; FJ170137; ACN37929.1; -; Genomic_DNA. DR EMBL; FJ170138; ACN37930.1; -; Genomic_DNA. DR EMBL; FJ170139; ACN37931.1; -; Genomic_DNA. DR EMBL; FJ170140; ACN37932.1; -; Genomic_DNA. DR EMBL; FJ170141; ACN37933.1; -; Genomic_DNA. DR EMBL; FJ170142; ACN37934.1; -; Genomic_DNA. DR EMBL; FJ170143; ACN37935.1; -; Genomic_DNA. DR EMBL; FJ170144; ACN37936.1; -; 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:ACN37924.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..27 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 47..70 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 90..113 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 125..148 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..149 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACN37924.1" FT NON_TER 149 FT /evidence="ECO:0000313|EMBL:ACN37924.1" SQ SEQUENCE 149 AA; 16355 MW; 789B398D63AF46D5 CRC64; IVTAHAFVMI FFMVMPVMIG GFGNWLVPLM IGSPDMSFPR MNNMSFWLLP FSLMFMLGSM FSDSGAGTGW TVYPPLSNYM FHSGVSVDMV IFSLHVAGVS SILGAINFIS TILNYRIMSM SHLPLFVWSV LITAFLLLVS LPVLAGALT //