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Database: UniProt
Entry: A5CC53_ORITB
LinkDB: A5CC53_ORITB
Original site: A5CC53_ORITB 
ID   A5CC53_ORITB            Unreviewed;       387 AA.
AC   A5CC53;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=2-polyprenyl-6-methoxyphenol 4-hydroxylase {ECO:0000313|EMBL:CAM79218.1};
DE            EC=1.14.13.- {ECO:0000313|EMBL:CAM79218.1};
GN   Name=ubiH {ECO:0000313|EMBL:CAM79218.1};
GN   OrderedLocusNames=OTBS_0152 {ECO:0000313|EMBL:CAM79218.1};
OS   Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM79218.1, ECO:0000313|Proteomes:UP000001565};
RN   [1] {ECO:0000313|EMBL:CAM79218.1, ECO:0000313|Proteomes:UP000001565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boryong {ECO:0000313|EMBL:CAM79218.1,
RC   ECO:0000313|Proteomes:UP000001565};
RX   PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA   Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA   Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA   Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT   "The Orientia tsutsugamushi genome reveals massive proliferation of
RT   conjugative type IV secretion system and host-cell interaction genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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; AM494475; CAM79218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5CC53; -.
DR   KEGG; ots:OTBS_0152; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_8_1_5; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001565; 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:CAM79218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001565}.
FT   DOMAIN          1..297
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   387 AA;  43977 MW;  F16FEDBAD11F745F CRC64;
     MITALGLASY NIKSTIIEKK NLSNTNYLDT RTTALTQRSK SIFKNFNIWK DIEPYISNIN
     EVYVVDNKST MMVHLNASKS EFDSIGYMIE NSNLYVKLIE LVQNNPLINV IDNTSYVSID
     SHQHSTAIDI NTSSKIHCDL LIVCDGCNSI ARKQYFEYLI DKEYHQSAIV FNVRHQKQHF
     GTAVEHFLPN GPFAALPLAD QQVSSIVWVE KSNLATLYAQ MDKKSLTNYV QDKFGCSLGK
     IEIITTPVLY PLKAKIAKQY YHNNVVLVGD TAHMIHPLAG QGLNQSIKDI NSLTDILYSR
     KSLGLEMTSS EFKLYQRDRF LDNYTMYLLT DNLNRLFSNN LPLLATVRKI SLGLLDKSVI
     LKRMIMKYGM GSYSVGSKII NIANYIF
//
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