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Database: UniProt
Entry: A0A0Q7AW59_9BURK
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ID   A0A0Q7AW59_9BURK        Unreviewed;       414 AA.
AC   A0A0Q7AW59;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=2-octaprenyl-6-methoxyphenyl hydroxylase {ECO:0000313|EMBL:KQW38878.1};
GN   ORFNames=ASC76_13015 {ECO:0000313|EMBL:KQW38878.1};
OS   Rhizobacter sp. Root404.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW38878.1, ECO:0000313|Proteomes:UP000051611};
RN   [1] {ECO:0000313|EMBL:KQW38878.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW38878.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW38878.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW38878.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQW38878.1}.
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DR   EMBL; LMDS01000004; KQW38878.1; -; Genomic_DNA.
DR   RefSeq; WP_056466285.1; NZ_LMDS01000004.1.
DR   AlphaFoldDB; A0A0Q7AW59; -.
DR   STRING; 1736528.ASC76_13015; -.
DR   OrthoDB; 9769565at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000051611; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of 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; IPR018168; Ubi_Hdrlase_CS.
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.
DR   PROSITE; PS01304; UBIH; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT   DOMAIN          216..344
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   414 AA;  44221 MW;  FFC8C06E71B06511 CRC64;
     MPETPPVTAL HIAVIGAGPV GLALALQAAR ALPDSQVTLF DARPVDKDVS GDPRTLALSL
     GSVQLLERLG AWRAELAQPI LEVHVSQQPP SMLPLPGRLA DLLGEPELRI RAVDEAVPLL
     GAVLSYGSIV APLQQAWLAA EAAAPKRLHS RFGQPVAALK NLEHGVEVDA GIAERFDLAI
     VAEGGVFTTD PSRQLVRATE RPSIRHDYRQ TAWVGQVTFE DDATRAKGVA FERFTRHGPA
     ALLPLKAGGA GLVWCVPTDD DPVRELDAAQ RVTVLNSIFH PAAGRIASVT PLKDFALGLS
     AERTLTEGRT VRIGNAAQTL HPVAGQGLNL GLRDAFELVH ALARNPDVDA VLRRLEWQRG
     PDRWAMIAAT DFLARSFTWK LPGAGAARGL GLAALQLLGP AKSALARQMM FGRR
//
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