ID B9V3I7_9CAEN Unreviewed; 216 AA. AC B9V3I7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 17-JUN-2020, entry version 42. 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=cox1 {ECO:0000313|EMBL:ACM48518.1}; OS Semisulcospira paludiformis. OG Mitochondrion {ECO:0000313|EMBL:ACM48518.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda; OC Caenogastropoda; Sorbeoconcha; Cerithioidea; Semisulcospiridae; OC Semisulcospira. OX NCBI_TaxID=576959 {ECO:0000313|EMBL:ACM48518.1}; RN [1] {ECO:0000313|EMBL:ACM48518.1} RP NUCLEOTIDE SEQUENCE. RA Du Y.Y., Wu X.P., Ouyang S.; RT "Phylogenetic relationships of Pleuroceridae Gastropoda (Mollusca) based on RT mitochondrial COI gene sequences."; RL Submitted (NOV-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|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; FJ437222; ACM48518.1; -; 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:ACM48518.1}; 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 34..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 80..102 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 122..147 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 159..186 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..216 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACM48518.1" FT NON_TER 216 FT /evidence="ECO:0000313|EMBL:ACM48518.1" SQ SEQUENCE 216 AA; 23375 MW; 83D1A482CDE741D3 CRC64; WSGLVGTALS LLIRAELGQP GALLGDDQLY NVIVTAHAFV MIFFLVMPMM IGGFGNWLVP LMLGAPDMAF PRLNNMSFWL LPPALLLLLS SAAVESGVGT GWTVYPPLSS NLAHAGGSVD LAIFSLHLAG ASSILGAVNF ITTIINMRWR GMQFERLPLF IWSVKITAIL LLLSLPVLAG AITMLLTDRN FNTAFFDPAG GGDPILYQHL FWFFGH //