ID Q136Y1_RHOPS Unreviewed; 398 AA.
AC Q136Y1;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000313|EMBL:ABE39858.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:ABE39858.1};
GN OrderedLocusNames=RPD_2629 {ECO:0000313|EMBL:ABE39858.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE39858.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE39858.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE39858.1,
RC ECO:0000313|Proteomes:UP000001818};
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
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; CP000283; ABE39858.1; -; Genomic_DNA.
DR AlphaFoldDB; Q136Y1; -.
DR STRING; 316057.RPD_2629; -.
DR KEGG; rpd:RPD_2629; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_1_5; -.
DR BioCyc; RPAL316057:RPD_RS13225-MONOMER; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001818; 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:ABE39858.1}.
FT DOMAIN 11..323
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 398 AA; 42668 MW; A008E34BA9EEE928 CRC64;
MTQSLLEPNS YDVIVVGGGP AGLAAAIAVA ETGAMTALIA RKVPYADNRT TALLGDSIDL
LEKLDVWRRC SSKAAALRTM RLVDDTGRLI RAPEVRFASD EIGMDAFGYN IENRNLMVAL
EERAAEIANL DRFDDEAESV APGDESTLVR TRKDQTLSAC LVVGADGRHS RCREAAGITV
SSRALNQSAL TFNVTTARSH QNVSTEFHTA EGPCVFVPLP GRRMSVVWVA APKEAQRLMA
LDDDALSVAA EKQSHSIFGR VTVEPGRNMF PLAIEKPSHY GRRRIVLVGE AAHVVPPIGA
QGLNMGLRDA GDIAEIVQDA MAGDQDVGSD AVIGRFGRAR GADVASRTFA IDIANRTLLS
DLLPAQAARA VGMQLISSVG PLRRLAMREG LSPFWRSL
//