ID A0A2R8B7A0_9RHOB Unreviewed; 398 AA.
AC A0A2R8B7A0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=2-octaprenyl-6-methoxyphenol hydroxylase {ECO:0000313|EMBL:SPH18498.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:SPH18498.1};
GN Name=ubiH {ECO:0000313|EMBL:SPH18498.1};
GN ORFNames=DEA8626_02037 {ECO:0000313|EMBL:SPH18498.1};
OS Defluviimonas aquaemixtae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Defluviimonas.
OX NCBI_TaxID=1542388 {ECO:0000313|EMBL:SPH18498.1, ECO:0000313|Proteomes:UP000244924};
RN [1] {ECO:0000313|EMBL:SPH18498.1, ECO:0000313|Proteomes:UP000244924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8626 {ECO:0000313|EMBL:SPH18498.1,
RC ECO:0000313|Proteomes:UP000244924};
RA Keele B.F.;
RL Submitted (MAR-2018) 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; OMOQ01000001; SPH18498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8B7A0; -.
DR OrthoDB; 9796623at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000244924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SPH18498.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..351
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 398 AA; 42557 MW; 92B1830A1837B85C CRC64;
MRETTDILIS GGGVAGLTAA AAFGAAGLAV ICIDPTHPVT EAEGEGADLR TTAFLQPART
VLDAAGLWSR LAPHGAALKI MRIVDAGGET PEPRIVKDFD AAEIGAEPFG WNFPNWMLRR
EMVARIAELP NVSFRPGIAT RSVLTREGAA LVTLSDGTQV SARLLVAADG RASPVREAVG
IGVKTTRYGQ KALAFAVTHP IPHRNVSTEI HRSGGPFTLV PLPDRDGLPS SAIVWMERGP
EVMRLAALPV EAFETEMLQR SAGLFGPLTL VTRRSVWPII SQIADRFDAE RTALLAEAAH
VVPPIGAQGL NMSLADLACL LELAKAAPDR LGDRAMLTTY HRRRWPEVKA RVAGIDLLNR
TSMLGAQSLR NLRAGALNAL YSFGPVRRTL MKAGLGMR
//
