ID   UBIL_RHORT              Reviewed;         429 AA.
AC   Q2RMZ4;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ubiquinone hydroxylase UbiL {ECO:0000305};
DE            Short=UQ hydroxylase {ECO:0000303|PubMed:30686758};
DE   AltName: Full=2-polyprenyl-6-methoxyphenol hydroxylase {ECO:0000305};
DE            EC=1.14.13.- {ECO:0000305|PubMed:30686758};
DE   AltName: Full=2-polyprenylphenol hydroxylase {ECO:0000305};
DE            EC=1.14.13.240 {ECO:0000305|PubMed:30686758};
GN   Name=ubiL {ECO:0000303|PubMed:30686758};
GN   OrderedLocusNames=Rru_A3707 {ECO:0000312|EMBL:ABC24501.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=30686758; DOI=10.1016/j.chembiol.2018.12.001;
RA   Hajj Chehade M., Pelosi L., Fyfe C.D., Loiseau L., Rascalou B.,
RA   Brugiere S., Kazemzadeh K., Vo C.D., Ciccone L., Aussel L., Coute Y.,
RA   Fontecave M., Barras F., Lombard M., Pierrel F.;
RT   "A soluble metabolon synthesizes the isoprenoid lipid ubiquinone.";
RL   Cell Chem. Biol. 26:482-492(2019).
CC   -!- FUNCTION: Catalyzes the hydroxylation of two positions of the aromatic
CC       ring during ubiquinone biosynthesis. {ECO:0000269|PubMed:30686758}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-all-trans-polyprenylphenol + H(+) + NADPH + O2 = a 3-(all-
CC         trans-polyprenyl)benzene-1,2-diol + H2O + NADP(+);
CC         Xref=Rhea:RHEA:55892, Rhea:RHEA-COMP:9516, Rhea:RHEA-COMP:9550,
CC         ChEBI:CHEBI:1269, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62729; EC=1.14.13.240;
CC         Evidence={ECO:0000305|PubMed:30686758};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P25535};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000269|PubMed:30686758}.
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000305}.
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DR   EMBL; CP000230; ABC24501.1; -; Genomic_DNA.
DR   RefSeq; WP_011391454.1; NC_007643.1.
DR   RefSeq; YP_428788.1; NC_007643.1.
DR   AlphaFoldDB; Q2RMZ4; -.
DR   SMR; Q2RMZ4; -.
DR   STRING; 269796.Rru_A3707; -.
DR   EnsemblBacteria; ABC24501; ABC24501; Rru_A3707.
DR   KEGG; rru:Rru_A3707; -.
DR   PATRIC; fig|269796.9.peg.3832; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_8_1_5; -.
DR   OMA; SDVACII; -.
DR   OrthoDB; 867226at2; -.
DR   PhylomeDB; Q2RMZ4; -.
DR   BioCyc; MetaCyc:MON-20130; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001929; Chromosome.
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-UniPathway.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018168; Ubi_Hdrlase_CS.
DR   InterPro; IPR010971; UbiH/COQ6.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR   PROSITE; PS01304; UBIH; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..429
FT                   /note="Ubiquinone hydroxylase UbiL"
FT                   /id="PRO_0000447677"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  45618 MW;  858868E52C859390 CRC64;
     MSEPLLRGLA AGDPPSATGP VTGSADKVAD VLIVGGGLVG GTLACALAEK GVSVVVIDGE
     DPEALLAAGY DGRCSAIALA CQRLLDTIGL WDLLGGESQP ILDIRVVDGG SPLFLHYAQA
     EAQGPMGYMV ENRLLRQAIL TRLGRLPAAT LLAPARMTAL RRDLDGVSAT LSDGQTVRAR
     LVVGADGRRS QVRESAGIGI RTLGYGQTAI VLTVEHERSH RGCAVEHFLP AGPFAILPMP
     GNRSSLVWTE RSDLVPGLLA LPAEHFQAEL ERRFGDHLGW VRPVGPRFSY RLTLQAANRY
     VDHRLALVGD AAHGMHPVAG QGMNYGLRDV AVLAERLVAA QRLGLDPGAP ALLAEYEALR
     RPDNLLMLAI TDALVRLFSN DIAPVALARR LGIGAVERMG PLKRLFMRHA MGTLKLGPEP
     PRLMRGVPL