ID Q666R3_YERPS Unreviewed; 392 AA.
AC Q666R3;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=2-octaprenyl-6-methoxyphenol hydroxylase {ECO:0000313|EMBL:CAH22422.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:CAH22422.1};
DE Flags: Precursor;
GN Name=ubiH {ECO:0000313|EMBL:CAH22422.1};
GN OrderedLocusNames=YPTB3184 {ECO:0000313|EMBL:CAH22422.1};
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH22422.1, ECO:0000313|Proteomes:UP000001011};
RN [1] {ECO:0000313|EMBL:CAH22422.1, ECO:0000313|Proteomes:UP000001011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH22422.1; -; Genomic_DNA.
DR RefSeq; WP_011192963.1; NZ_CP009712.1.
DR AlphaFoldDB; Q666R3; -.
DR GeneID; 66844385; -.
DR KEGG; ypo:BZ17_3427; -.
DR KEGG; yps:YPTB3184; -.
DR PATRIC; fig|273123.14.peg.3596; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
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; IPR011295; UbiH.
DR InterPro; IPR010971; UbiH/COQ6.
DR NCBIfam; TIGR01988; Ubi-OHases; 1.
DR NCBIfam; TIGR01984; UbiH; 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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAH22422.1}.
FT DOMAIN 2..342
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 392 AA; 42496 MW; 93B0614BFEF2AA86 CRC64;
MSVIIVGGGM AGVTLALAIS SLTHGQVPVA LVEAQQPNDR QHPGFDARAI ALAQGTCQQL
ARIGAWSALA DCATAIDHVH VSDRGHSGFV NLRAEDYGVP ALGHVLELHD AGERLFALLM
KAPGVTLHCP AKVVDVVRTA ESARVTLDDG QQLAAKLLVA ADGSHSALAQ SCAIQWQRQD
YQQVAIIANI TTSELPNGRA FERFTRNGPL ALLPMSQGRS SLVWCHAKHD QQQIDSWDDA
RFLAELQQAF GWRLGKMLQA GKRHSYPLQL LTASRHISHR LALVGNAAQT LHPIAGQGFN
LGLRDVMSLA ETLAEAAAMG NDLGDYTVLS HYQQRRQQDQ QATIGVTDGL IRLFANRYGP
LVAGRNLALM AMEQMPTIRD TFARRTLGWV ER
//
