ID Q8HBV0_CHEDE Unreviewed; 44 AA. AC Q8HBV0; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 22-APR-2020, entry version 60. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375}; DE Flags: Fragment; GN Name=COIII {ECO:0000313|EMBL:AAN75553.1}; OS Cherax destructor albidus. OG Mitochondrion {ECO:0000313|EMBL:AAN75553.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea; OC Parastacoidea; Parastacidae; Cherax. OX NCBI_TaxID=72414 {ECO:0000313|EMBL:AAN75553.1}; RN [1] {ECO:0000313|EMBL:AAN75553.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CRA {ECO:0000313|EMBL:AAN75553.1}, and DWY RC {ECO:0000313|EMBL:AAN75555.1}; RA Nguyen T.T.T., Austin C.M.; RT "Data partitioning, incongruence and the utility of different mitochondrial RT gene regions for phylogenetic studies of the freshwater crayfish Cherax RT destructor Clark (Decapoda: Parastacidae)."; RL Submitted (SEP-2002) 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:RU003375}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|RuleBase:RU003375}. 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; AY153905; AAN75553.1; -; Genomic_DNA. DR EMBL; AY153907; AAN75555.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0015002; F:heme-copper terminal oxidase activity; IEA:InterPro. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; SSF81452; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:AAN75553.1}; KW Transmembrane {ECO:0000256|RuleBase:RU003375, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 17..36 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 5..44 FT /note="COX3" FT /evidence="ECO:0000259|PROSITE:PS50253" FT NON_TER 44 FT /evidence="ECO:0000313|EMBL:AAN75553.1" SQ SEQUENCE 44 AA; 4971 MW; 6D251399D4463419 CRC64; MSSHSHHAYH LVDMSPWPLT GSISAMLLTS GLIKWFHQLN PDLL //