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Database: UniProt
Entry: A0A0E3Z3X2_9GAMM
LinkDB: A0A0E3Z3X2_9GAMM
Original site: A0A0E3Z3X2_9GAMM 
ID   A0A0E3Z3X2_9GAMM        Unreviewed;       391 AA.
AC   A0A0E3Z3X2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000313|EMBL:AKC88369.1};
GN   ORFNames=WQ53_11870 {ECO:0000313|EMBL:AKC88369.1};
OS   Pseudoxanthomonas suwonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC88369.1, ECO:0000313|Proteomes:UP000033067};
RN   [1] {ECO:0000313|EMBL:AKC88369.1, ECO:0000313|Proteomes:UP000033067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J1 {ECO:0000313|EMBL:AKC88369.1,
RC   ECO:0000313|Proteomes:UP000033067};
RX   PubMed=26067962;
RA   Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT   "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT   Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL   Genome Announc. 3:e00614-15(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC       {ECO:0000256|ARBA:ARBA00005349}.
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DR   EMBL; CP011144; AKC88369.1; -; Genomic_DNA.
DR   RefSeq; WP_052634061.1; NZ_CP011144.1.
DR   AlphaFoldDB; A0A0E3Z3X2; -.
DR   KEGG; psuw:WQ53_11870; -.
DR   PATRIC; fig|314722.6.peg.2574; -.
DR   OrthoDB; 9769565at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000033067; 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; FAD/NAD(P)-binding domain; 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   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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS01304; UBIH; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033067}.
FT   DOMAIN          6..316
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   391 AA;  41926 MW;  907F8698A6A1F182 CRC64;
     MSRARLDVAV AGGGVVGAAC ALALARAGLE VALVEPRPAP RWLAERPDLR VYALAPDNAG
     LLDRLGVWPQ VRAARAQPYR RMRVWDAAGG GELMFDAAAM ARAELGWIVE NDLLVDRLWA
     ALAAAGVRLH CPARVEALEQ DAAGARLRLD DGTRLDARIA IAADGAGSAV RRLAGLEVDA
     HDYHQRGVVA FIETGQPHED TAWQRFLPTG PLALLPFADG RSSIVWTLPD AEAARVLTLD
     DDAFAVELTD AAAARLGHAR PVSPRVAFPL RRQLVRQQAA GRVLVLGDAA HVVHPLAGQG
     VNLGLRDVAA LLQEIESARA HRADWTAPHR LQRWARTRRS DNTVSAYAFE GINRLFSNAN
     PAAVLARGPL LGLAGKLPPL QRALWRHAAG V
//
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