ID A0A068F6G0_9NEOP Unreviewed; 262 AA. AC A0A068F6G0; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 22-APR-2020, entry version 15. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375}; GN Name=COX3 {ECO:0000313|EMBL:AID61642.1}; OS Grapholita dimorpha. OG Mitochondrion {ECO:0000313|EMBL:AID61642.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; Tortricoidea; OC Tortricidae; Olethreutinae; Grapholitini; Grapholita. OX NCBI_TaxID=934274 {ECO:0000313|EMBL:AID61642.1}; RN [1] {ECO:0000313|EMBL:AID61642.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24841435; RA Niu F.F., Fan X.L., Wei S.J.; RT "Complete mitochondrial genome of the Grapholita dimorpha Komai RT (Lepidoptera: Tortricidae)."; RL Mitochondrial DNA 0:0-0(2014). 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 -!- 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|SAAS:SAAS01246601}; CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|RuleBase:RU003375, ECO:0000256|SAAS:SAAS00709834}. 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; KJ671625; AID61642.1; -; Genomic_DNA. DR RefSeq; YP_009048931.1; NC_024582.1. DR GeneID; 19909119; -. DR CTD; 4514; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.20.120.80; -; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR033945; Cyt_c_oxase_su3_dom. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR PANTHER; PTHR11403; PTHR11403; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; SSF81452; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAAS:SAAS00709742, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:AID61642.1}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS01246713}; KW Transmembrane {ECO:0000256|RuleBase:RU003375, KW ECO:0000256|SAAS:SAAS00709762, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00709799, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 80..103 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 128..152 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 164..183 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 203..221 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 241..261 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 5..262 FT /note="COX3" FT /evidence="ECO:0000259|PROSITE:PS50253" SQ SEQUENCE 262 AA; 30641 MW; 43B58048BF197D48 CRC64; MTTHHNHPYH LVDYSPWPLT GAIGVLTLVT GMVKWFHNFN MNLLILGYII TLLTMYQWWR DICREGTMQG KHTILVSKGL RWGMILFIIS EVFFFLSFFW AFFHSSLSPN IEIGMMWPPV SIIPFNPFQI PLLNTIILIT SGITVTWAHH ALMENNFTQT TQGLFITVML GIYFTILQAY EYIEAPFTIA DSIYGSTFFM ATGFHGLHVM IGTIFLFICL LRHMNNHFSS NHHFGFEAAA WYWHFVDVVW LFLYISIYWW GN //