ID N8QDX5_9GAMM Unreviewed; 403 AA.
AC N8QDX5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=2-polyprenyl-6-methoxyphenol 4-hydroxylase {ECO:0000313|EMBL:ENU36961.1};
GN ORFNames=F988_00854 {ECO:0000313|EMBL:ENU36961.1};
OS Acinetobacter parvus DSM 16617 = CIP 108168.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=981333 {ECO:0000313|EMBL:ENU36961.1, ECO:0000313|Proteomes:UP000023776};
RN [1] {ECO:0000313|EMBL:ENU36961.1, ECO:0000313|Proteomes:UP000023776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 108168 {ECO:0000313|EMBL:ENU36961.1,
RC ECO:0000313|Proteomes:UP000023776};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter parvus CIP 108168.";
RL Submitted (FEB-2013) 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}.
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:ENU36961.1}.
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DR EMBL; APOM01000027; ENU36961.1; -; Genomic_DNA.
DR RefSeq; WP_004681277.1; NZ_KB849211.1.
DR AlphaFoldDB; N8QDX5; -.
DR PATRIC; fig|981333.9.peg.871; -.
DR HOGENOM; CLU_009665_8_1_6; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000023776; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..357
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 403 AA; 44668 MW; 7371D0A86AFA8838 CRC64;
MQQQVIIVGG GMVGLSLALM LAKSNIAVKL LEAVKYPNYD DENVAPYHSS FDARNTALSR
RSVQIYQKLG LWEALQQHAT PILQVHITEQ GSFGKARLVA EQEKVESFGQ VIENAWLGRV
LLTQVRQQPL IELIDGVQVT SLTQDADEVH IEAMRNGEYI HSLKSKLVIA ADGRDSFCRQ
AIGVGVDEHD YDQVAIVTTV QTSKPHQQVG FERFSALGPL ALLPLPGEYR RSVVWPVKKG
TEAEWLGEEN DQHFLDALQE TYGDRAGKFE KTGKRFSYPL SQVLAHKQAV GRVVLMGNAA
HTIHPVAGQG FNLCLRDADV LVRYLLEQLA KSDDIGHPDN LLAYEQARLT DQQRVIKFCD
SVVRGFSNQN PILKLLRNTG LIAFDVIPGV KPLVANYAMG LKA
//
