ID A0A0D9RJM1_CHLSB Unreviewed; 468 AA.
AC A0A0D9RJM1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
DE AltName: Full=Coenzyme Q10 monooxygenase 6 {ECO:0000256|HAMAP-Rule:MF_03193};
GN Name=COQ6 {ECO:0000256|HAMAP-Rule:MF_03193,
GN ECO:0000313|Ensembl:ENSCSAP00000008810.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000008810.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000008810.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000008810.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. Interacts with ADCK4
CC and COQ7. {ECO:0000256|HAMAP-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}. Golgi
CC apparatus {ECO:0000256|HAMAP-Rule:MF_03193}. Cell projection
CC {ECO:0000256|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and
CC Golgi apparatus in podocytes. {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; AQIB01053646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01053647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01053648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01053649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01053650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007985450.1; XM_007987259.1.
DR AlphaFoldDB; A0A0D9RJM1; -.
DR STRING; 60711.ENSCSAP00000008810; -.
DR Ensembl; ENSCSAT00000010721.1; ENSCSAP00000008810.1; ENSCSAG00000012631.1.
DR GeneID; 103229321; -.
DR CTD; 51004; -.
DR eggNOG; KOG3855; Eukaryota.
DR GeneTree; ENSGT00390000015152; -.
DR OMA; VKQMQVW; -.
DR OrthoDB; 5473786at2759; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 103229321; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 24.
DR Bgee; ENSCSAG00000012631; Expressed in adrenal cortex and 7 other cell types or tissues.
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:0110142; C:ubiquinone biosynthesis complex; IEA:Ensembl.
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 Cell projection {ECO:0000256|HAMAP-Rule:MF_03193};
KW FAD {ECO:0000256|HAMAP-Rule:MF_03193};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_03193};
KW Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_03193};
KW 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:UP000029965};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03193}.
FT DOMAIN 352..425
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 468 AA; 50684 MW; 64C380515668927E CRC64;
MAARLVSRCG AVGAAAYSSP LVSCRRWSGA STDTVYDVVV SGGGLVGAAM ACALGYDIHF
HDKKILLLEA GPKKVLEKLS ETYSNRVSSI SPGSATLLSS FGAWDHICNM RYRAFRRMQV
WDACSEALIM FDKDNLDDMG YIVENDVIMH ALTKQLEAVS DRVTVLYRSK AIRYTWPCPF
PMADSSPWVH ITLGDGSTFQ TKLLIGADGH NSGVRQAAGI QNVSWNYDQS AVVATLHLSE
ATENNVAWQR FLPSGPIALL PLSDTLSSLV WSTSHEHAAQ LVSMDEEKFV DAVNSAFWSD
ADHTDFIDTA GAMLHYAVGL LKPTKVSARQ LPPSVARVDA KSRVLFPLGL GHAAEYVRPR
VALIGDAAHR VHPLAGQGVN MGFGDISSLA HHLSTAAFNG KDLGSMSHLT GYETERQRHN
TALLAATDLL KRLYSTSAAP LVLLRTWGLQ ATNAVSPLKE QIMAFASK
//
