ID C5DYW1_ZYGRC Unreviewed; 478 AA.
AC C5DYW1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=ZYRO0F16192g {ECO:0000313|EMBL:CAR28972.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28972.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928178; CAR28972.1; -; Genomic_DNA.
DR RefSeq; XP_002497905.1; XM_002497860.1.
DR AlphaFoldDB; C5DYW1; -.
DR STRING; 559307.C5DYW1; -.
DR GeneID; 8205677; -.
DR KEGG; zro:ZYRO0F16192g; -.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; C5DYW1; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000008536; Chromosome F.
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; TIGR01989; COQ6; 1.
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; 1.
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:UP000008536};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03193}.
FT DOMAIN 351..403
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 478 AA; 53023 MW; E8AF6B6278ED2628 CRC64;
MLARSAIVRK YALRKLASTA TATPKLTDVL IVGGGPAGLT LAAALKSTPR LQHLKTTLVD
ASDLMGKVAP FYDSPPENFT NRVVSLTPPS KSFIETKAGA RMLEDRIQPY DGMYVTDGLT
NATLNMEKDS MAYMVEILNI QSSLLKRLEE LNLPSESLQL MDNTKVASIE YSDPEDTTSW
PIVTLDNGEV FKTRLLVGAD GFNSPVRKFS DIQSRGWFYN RFGVVATMKL EYPPYKLRGW
QRFLPTGPIA HLALPDDNAT LVWSTTEPLS RLLREITPEQ FTGLVNAAFV LEDSDLKYFY
RQLEKGTISN EKLLEDINFR TEQVYDSLEN DDLIDEIYPP RVKSILGPSR ARFPLKMFHA
DTYCKDRIAL VGDAAHATHP LAGQGLNMGQ GDVEALIKAL EKASMRGHDI GSLLSLQPFW
AERYPINNML LGMTDKLHKI YGTDFAPIVA LRSLGVSIMN KVGPLKNLIS GTLSDSGK
//
