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Database: UniProt
Entry: G5QPA8_SALRU
LinkDB: G5QPA8_SALRU
Original site: G5QPA8_SALRU 
ID   G5QPA8_SALRU            Unreviewed;       387 AA.
AC   G5QPA8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000313|EMBL:EHC82169.1};
GN   ORFNames=LTSERUB_4851 {ECO:0000313|EMBL:EHC82169.1};
OS   Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913081 {ECO:0000313|EMBL:EHC82169.1, ECO:0000313|Proteomes:UP000004903};
RN   [1] {ECO:0000313|EMBL:EHC82169.1, ECO:0000313|Proteomes:UP000004903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-653 {ECO:0000313|EMBL:EHC82169.1,
RC   ECO:0000313|Proteomes:UP000004903};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC82169.1}.
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DR   EMBL; AFCT01001771; EHC82169.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5QPA8; -.
DR   PATRIC; fig|913081.3.peg.3749; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000004903; Unassembled WGS sequence.
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; PS01304; UBIH; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..332
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   387 AA;  42795 MW;  7675A4C4ABEB26E4 CRC64;
     MGLAVACGLQ GSGLRVAVLD HVVPQPLAND APPQLRVSAI NAASEKLLTR LGVWSNIVAR
     RASCYHGMEV WDKDSFGRIT FDDASMGYSH LGHIVENSVI HYALWQKAQQ AADITLMAPA
     ELQQVAWGEN DAFLTLKDGA MLTARLVIAA DGANSWLRNK ADIPLTFWDY RHHALVATIR
     TEEPHGAVAR QVFHGEGILA FLPLSDPHLC SIVWSLSPQD AERMQQSGDE AFNQALTIAF
     DNRLGLCRLE SERQVFPLTG RYARQFAAHR LALVGDAAHT IHPLAGQGVN LGFMDAAELV
     DDLRRLQRQG KDIGQHLYLR RYERSRKHSA AMMLAGMQGF RDLFAGENPA KKLLRDIGLK
     LADTLPGVKP QLLRQAMGLN DLPQWLR
//
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