ID   A0A1H6CYJ0_9GAMM        Unreviewed;       421 AA.
AC   A0A1H6CYJ0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=2-octaprenyl-6-methoxyphenol hydroxylase {ECO:0000313|EMBL:SEG77838.1};
GN   ORFNames=SAMN05444390_104304 {ECO:0000313|EMBL:SEG77838.1};
OS   Marinobacterium lutimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=568106 {ECO:0000313|EMBL:SEG77838.1, ECO:0000313|Proteomes:UP000236745};
RN   [1] {ECO:0000313|EMBL:SEG77838.1, ECO:0000313|Proteomes:UP000236745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22012 {ECO:0000313|EMBL:SEG77838.1,
RC   ECO:0000313|Proteomes:UP000236745};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNVQ01000004; SEG77838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6CYJ0; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000236745; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236745};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..340
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   421 AA;  45818 MW;  DA32BCEE6D9A3E51 CRC64;
     MRDDSDLADQ YDLVIVGGGM VGASLACALL PVASELKLRV AVVEAEQMPA PGEPVFQPSY
     DARSTALAYG VRAPFERMGI WQQLAQHLTP IEHIHVSDRG RFGVTRLDAQ RENVSALGYV
     VENHWLGQVL LSRLAQQGAP WIDFIAPAQV EDLDNRADGS QVRISTAEGE RTLNAGLVVI
     ADGGRSSLRE KLGIGYSQSS YEQHALVANV SLDRSHAGVA YERFTDSGPI ALLPGEDLDG
     QARCGLVWTL PEDDVDEVLA LDDAAFLRKL QERFGYRAGR FVRVGERFHY PLKLVLAEEQ
     VRAGLVVLGN AAHALHPIAG QGFNLAFRGV VALADMIIER RREGLPLGDL HALQAFETAR
     HSDQFRTIQF SDRTMKLFTS SQPGVGLLRD AGLVALELCP LGKTLLARAA MGLDQPAPKL
     H
//