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Database: UniProt
Entry: R7YKG4_CONA1
LinkDB: R7YKG4_CONA1
Original site: R7YKG4_CONA1 
ID   R7YKG4_CONA1            Unreviewed;       495 AA.
AC   R7YKG4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03193};
DE            EC=1.14.13.- {ECO:0000256|HAMAP-Rule:MF_03193};
GN   Name=COQ6 {ECO:0000256|HAMAP-Rule:MF_03193};
GN   ORFNames=W97_01305 {ECO:0000313|EMBL:EON62086.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON62086.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) 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-
CC       polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the
CC       hydroxylation reaction may be funneled indirectly from NADPH via a
CC       ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03193};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_03193};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|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. {ECO:0000256|HAMAP-
CC       Rule:MF_03193}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03193}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03193}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03193}.
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC       {ECO:0000256|ARBA:ARBA00005349, ECO:0000256|HAMAP-Rule:MF_03193}.
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DR   EMBL; JH767557; EON62086.1; -; Genomic_DNA.
DR   RefSeq; XP_007777403.1; XM_007779213.1.
DR   AlphaFoldDB; R7YKG4; -.
DR   STRING; 1168221.R7YKG4; -.
DR   GeneID; 19898616; -.
DR   eggNOG; KOG3855; Eukaryota.
DR   HOGENOM; CLU_009665_8_0_1; -.
DR   OMA; VKQMQVW; -.
DR   OrthoDB; 5473786at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000016924; Unassembled WGS sequence.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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: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; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   NCBIfam; TIGR01988; Ubi-OHases; 1.
DR   PANTHER; PTHR43876; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43876:SF7; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS01304; UBIH; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03193};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_03193}; Membrane {ECO:0000256|HAMAP-Rule:MF_03193};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03193};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|HAMAP-Rule:MF_03193};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW   Rule:MF_03193};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03193}; Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_03193}.
FT   DOMAIN          43..330
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          337..448
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   495 AA;  53441 MW;  244B12DB7C8799D7 CRC64;
     MPSRVLYSIR SCSRISLLRS HIPARSWYST AAASSTPGQP ELYDVVCVGG GPAGLSLVAG
     LRSSKITSNL KIALVEGQDL QKNVLKDASP TIYSNRCSSL TPASVKYLRE IGAWDHIDTS
     RVQPYQEMQV WDGVSDSRIS FDWASASGLA LKQPVDRTTI AYMIENLNLT TALLSRLSEL
     DSKLSISSPT RVSSVELGQE TEALDLRSWP TVTLDNGRQL AARLLVGADG ANSPVRTFAG
     IPSRGWDYGR HGVVASLRLE GPGWGGEEHK IAYQRFLPTG PVAMLPLPGN MATLVWSTVP
     ERAARLKALK EEDFVAMVNA AFRLSPVDLE YLHTIPEGQK EEVEWREQHT PVDEQKIPMR
     AVGAQAGSVA NFPLKMRHAD TYTGERVALV GDAAHTVHPL AGQGLNQGQA DAAALVRVIE
     TAVSQGSDIG SQLALEAYTG ERWQANNALL GAVDKLHKLY SFGSGPIVPV RSWGLSAVNA
     IGPLKGWFMR QAAGT
//
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