ID D3TSY8_9CRUS Unreviewed; 149 AA. AC D3TSY8; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 02-DEC-2020, entry version 44. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {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: 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; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|ARBA:ARBA00009578, 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:InterPro. 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 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 //