ID Q12R20_SHEDO Unreviewed; 411 AA.
AC Q12R20;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000313|EMBL:ABE54106.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:ABE54106.1};
GN OrderedLocusNames=Sden_0817 {ECO:0000313|EMBL:ABE54106.1};
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE54106.1, ECO:0000313|Proteomes:UP000001982};
RN [1] {ECO:0000313|EMBL:ABE54106.1, ECO:0000313|Proteomes:UP000001982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC {ECO:0000313|Proteomes:UP000001982};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000302; ABE54106.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12R20; -.
DR STRING; 318161.Sden_0817; -.
DR KEGG; sdn:Sden_0817; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_3_6; -.
DR OrthoDB; 9769565at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001982; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular 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; 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.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABE54106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001982}.
FT DOMAIN 24..359
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 411 AA; 45517 MW; 04F92196E122CF96 CRC64;
MQDGRGQDGQ GQDEQGQALE RQVVDVIVIG GGMVGAATAL GLGQLGLKVA LVESRRPQAY
DPSQALDLRV SAINIASEQL LSRLGAMDQL KQWRHAPYLG LETWEMPDCI TRFHAKDINV
PHLGYFFENR LIQLSLWQQI AQLSQLSLHC PSKVKQISRS HDDSIYVSLD DGTELEAKLL
VGADGANSQV RQWAGIGVTG WDYAQAAMLI NIDTKAPQQD ITWQHFTPQG PRSLLPLPGN
HASLVWYDDA NRISQLMQLN HEQLAEQIRA HFPSRLAPEF SVSARGSFPL TRRHAQAYYQ
ANLVILGDAA HTINPLAGQG VNIGFKDVDA LLNTLASAIG EGEIWWQLDT LAKYQQVRRA
ENRLMMTAMD GFYSAFSNDL LPLKLLRNGL LKVANIDSPI KRRVLKHALG L
//
