COQ6_XENTR
ID COQ6_XENTR Reviewed; 464 AA.
AC Q6DF46;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 AltName: Full=Coenzyme Q10 monooxygenase 6 {ECO:0000255|HAMAP-Rule:MF_03193};
DE Flags: Precursor;
GN Name=coq6 {ECO:0000255|HAMAP-Rule:MF_03193}; ORFNames=TEgg013o11.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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, composed of
CC at least coq3, coq4, coq5, coq6, coq7 and coq9. Interacts with coq8b
CC and coq7. {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}. Golgi
CC apparatus {ECO:0000255|HAMAP-Rule:MF_03193}. Cell projection
CC {ECO:0000255|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and
CC Golgi apparatus in podocytes. {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; CR761032; CAJ83665.1; -; mRNA.
DR EMBL; AAMC01082860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076897; AAH76897.1; -; mRNA.
DR RefSeq; NP_001006829.1; NM_001006828.2.
DR AlphaFoldDB; Q6DF46; -.
DR SMR; Q6DF46; -.
DR PaxDb; Q6DF46; -.
DR GeneID; 448564; -.
DR KEGG; xtr:448564; -.
DR CTD; 51004; -.
DR Xenbase; XB-GENE-945926; coq6.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; Q6DF46; -.
DR OMA; AHGFNFG; -.
DR OrthoDB; 655400at2759; -.
DR PhylomeDB; Q6DF46; -.
DR TreeFam; TF105772; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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 Cell projection; FAD; Flavoprotein; Golgi apparatus; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03193"
FT CHAIN 25..464
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000418623"
SQ SEQUENCE 464 AA; 50743 MW; F7AC71268E7FDF16 CRC64;
MRCLGGSSLS RLLRMLSQSQ GRALSSTGPA VYDVVISGGG MVGTAMACAL GSDPHLQHKK
VLLLEAGNRK PFDHLPENFS NRVSSITPGS ATLLASFGAW DHILAMRLKP YKRMQVWDAC
SDALITFDKD ALEDMGYIVE NDIIIEALTK QLELMSDHVE VMYRSRALSY SWPPPYNNGK
ATPWVEIELA DGQRLHTKLL IGADGHNSMV RSAAGMQSVQ WNYNHAAVVA TLHLSEATDN
NVAWQRFLPT GPIALLPLSD TCSSLVWSTS PEHASELVSM DEESFVDTVN SAFWSNENHS
EFITSAGSLL HSALSFFMPT GSSPRQLPPS VSRVEQNSRA SFPLGLKHAT EYIRHRVALI
GDAAHRVHPL AGQGVNMGFG DVACLAHHLS QAAFNGSDLG STKHLLEYET ERQRHNLPLM
AAVDLLKRLY NTKQPPIVLL RTLGLQATNA LTPVKEQIMA FASK
