COQ6_DROME
ID COQ6_DROME Reviewed; 477 AA.
AC Q9VMQ5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03193};
DE EC=1.14.13.- {ECO:0000255|HAMAP-Rule:MF_03193};
DE Flags: Precursor;
GN Name=Coq6 {ECO:0000255|HAMAP-Rule:MF_03193}; ORFNames=CG7277;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: FAD-dependent monooxygenase required for the C5-ring
CC hydroxylation during ubiquinone biosynthesis. Catalyzes the
CC hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-
CC 4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation
CC reaction may be funneled indirectly from NADPH via a
CC ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2
CC reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-
CC hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:20361, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58373,
CC ChEBI:CHEBI:84492; Evidence={ECO:0000255|HAMAP-Rule:MF_03193};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03193};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03193}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03193}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03193}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
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DR EMBL; AE014134; AAF52257.1; -; Genomic_DNA.
DR EMBL; AY058443; AAL13672.1; -; mRNA.
DR RefSeq; NP_608934.1; NM_135090.4.
DR AlphaFoldDB; Q9VMQ5; -.
DR SMR; Q9VMQ5; -.
DR BioGRID; 59945; 20.
DR DIP; DIP-21077N; -.
DR STRING; 7227.FBpp0078759; -.
DR PaxDb; Q9VMQ5; -.
DR PRIDE; Q9VMQ5; -.
DR DNASU; 33777; -.
DR EnsemblMetazoa; FBtr0079128; FBpp0078759; FBgn0031713.
DR GeneID; 33777; -.
DR KEGG; dme:Dmel_CG7277; -.
DR UCSC; CG7277-RA; d. melanogaster.
DR CTD; 51004; -.
DR FlyBase; FBgn0031713; Coq6.
DR VEuPathDB; VectorBase:FBgn0031713; -.
DR eggNOG; KOG3855; Eukaryota.
DR GeneTree; ENSGT00390000015152; -.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; Q9VMQ5; -.
DR OMA; SDVACII; -.
DR OrthoDB; 655400at2759; -.
DR PhylomeDB; Q9VMQ5; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 33777; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33777; -.
DR PRO; PR:Q9VMQ5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031713; Expressed in second segment of antenna (Drosophila) and 26 other tissues.
DR Genevisible; Q9VMQ5; DM.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
DR GO; GO:0106364; F:4-hydroxy-3-all-trans-hexaprenylbenzoate oxygenase activity; IEA:RHEA.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_03193; COQ6_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018168; Ubi_Hdrlase_CS.
DR InterPro; IPR010971; UbiH/COQ6.
DR InterPro; IPR000689; UbQ_mOase_COQ6.
DR Pfam; PF01494; FAD_binding_3; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01989; COQ6; 1.
DR TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR PROSITE; PS01304; UBIH; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03193"
FT CHAIN 26..477
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000207586"
SQ SEQUENCE 477 AA; 51994 MW; FE3FFEE143DDD0D2 CRC64;
MLGVLRIQGA LASAGQARLL SVRLLASKST TDMTTNRGES TQSTSTEHFD IIIGGGGLVG
TTLAAALAKN STLADKKVLL LEGAPEFRGF NPTGPYQNRV SAINHNSIEL FKSIDAWKHI
ESARYKPVKQ MQVWESNTDA LIQFQHDNFA SDVACIIEND LILDAVYALA KESPNVEILN
KARIQCVRLP RDSNSNHSEL QLEDGRNFSC DLLIGADGAN SVVRKEMNVD VFSLNYDRMG
LVATLELGED ACDNSVAWQR FLPNGPVALL PLTDRLSSLV WSTTNEQAKM LQALPPTEFV
DALNEAFCRQ YPRVELADKA VQALNSLFGH NGSQHQVQYP PRVCGVLDKS RATFPLGFLH
ASSYVCNGAA LVGDAAHRVH PLAGQGVNLG FSDVRYLVES LAAGAYAGFK LGDKQHLIKY
ERKCLAKNVP IMLGVHGLHT LYATQFSPVV LLRSLGLQLT QNLPPVKNLF MRGAMGQ
