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Database: UniProt
Entry: D0SAI1_ACIJO
LinkDB: D0SAI1_ACIJO
Original site: D0SAI1_ACIJO 
ID   D0SAI1_ACIJO            Unreviewed;       402 AA.
AC   D0SAI1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Putative 2-polyprenyl-6-methoxyphenol 4-hydroxylase {ECO:0000313|EMBL:EEY97418.1};
GN   ORFNames=HMPREF0016_00501 {ECO:0000313|EMBL:EEY97418.1};
OS   Acinetobacter johnsonii SH046.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY97418.1, ECO:0000313|Proteomes:UP000012047};
RN   [1] {ECO:0000313|Proteomes:UP000012047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH046 {ECO:0000313|Proteomes:UP000012047};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
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; GG704964; EEY97418.1; -; Genomic_DNA.
DR   RefSeq; WP_005399804.1; NZ_GG704964.1.
DR   AlphaFoldDB; D0SAI1; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_8_1_6; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000012047; 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   402 AA;  44325 MW;  CBB927EE2CA64728 CRC64;
     MQQEVIIVGG GMVGLSLALM LAKQNIVVKL LEAIKYPNYD DVNLAPYHSS FDARNSALSR
     RTVQIYQELG LWNALQEHAT PILEVNITEQ GSFGKARLKA EQEKVESFGQ VIENAWLGRV
     LLTEVQKQPL IELIDGVKVT QLIQDADMAY IEASRGEEQL SLQAKLVIAA DGRDSFCRKA
     LGIGASEHDY DQVAIVTTVQ TSKPHNHVGF ERFSSLGPLA LLPLPGEYHR SVVWPVKKGT
     EGEWLGDEND QHFLDALQET YGDRAGKFQK TGKRFSFPLS QVLAEKQAVG RVVLMGNAAH
     TIHPVAGQGF NLCMRDAHVL VRFLTEQIAQ NADLGDAAML QAYEASRLTD QQRVIKFCDS
     VVRGFSNSNP ILKFIRNTGL VAFDTIPGIK PLVANYAMGL KA
//
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