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Database: UniProt
Entry: G1MIV1_AILME
LinkDB: G1MIV1_AILME
Original site: G1MIV1_AILME 
ID   G1MIV1_AILME            Unreviewed;       538 AA.
AC   G1MIV1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 51.
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:ENSAMEP00000019286.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000019286.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000019286.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000019286.2}
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   AlphaFoldDB; G1MIV1; -.
DR   STRING; 9646.ENSAMEP00000019286; -.
DR   Ensembl; ENSAMET00000020052.2; ENSAMEP00000019286.2; ENSAMEG00000018242.2.
DR   eggNOG; KOG3855; Eukaryota.
DR   GeneTree; ENSGT00390000015152; -.
DR   HOGENOM; CLU_009665_8_0_1; -.
DR   TreeFam; TF105772; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
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: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:UP000008912};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_03193}.
FT   DOMAIN          422..495
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   538 AA;  57952 MW;  79BB925C878A9037 CRC64;
     MPEPVPLPRE PLILPAQVGR DRFLIGLLFA RSISGTEAGP TQLAIGELCS GSAAKGGSNG
     APSTLQVSTM AGRLAVSRWR AAPSAAGRGP LLSCRRWSGA KADTVYDVVV SGGGLVGAAM
     ACALGYDIHF HDKKILLLEA GPKKVWEKLP ETYSNRVSSI SPGSATLLSS FGAWDHICNM
     RYRAFRRMQV WDACSEALIM FDKDNLDDMG YIVENDVIMC ALTKQLEAVS DRVTVLYRSK
     AVSYTWPYPF TMADSSPWVH ITLGDGSTLQ TKLLIGADGH NSGVRQAAGI KNVSWNYDQS
     AVVATLHLSE ATENNVAWQR FLPSGPIALL PLSDTLSSLV WSTSHEHAAE LVGMDEEKFV
     DTINSAFWSD ANHTDFIDSA SSVLQSVVGF LRPTKVSARQ LPPSVARVDA RSRVLFPLGL
     GHAAEYVRPR LALIGDAAHR VHPLAGQGVN MGFGDVSSLV HHLSAAAFNG KDLGSMSHLT
     GYETDRQRHN TALLAATDLL KRFYSTSAAP LVLLRTWGLQ ATNAVSPLKE QIMAFASK
//
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