ID A0A0W0VF74_9GAMM Unreviewed; 390 AA.
AC A0A0W0VF74;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=2-polyprenyl-6-methoxyphenol hydroxylase {ECO:0000313|EMBL:KTD18751.1};
GN Name=ubiH_1 {ECO:0000313|EMBL:KTD18751.1};
GN ORFNames=Llan_2354 {ECO:0000313|EMBL:KTD18751.1};
OS Legionella lansingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD18751.1, ECO:0000313|Proteomes:UP000054869};
RN [1] {ECO:0000313|EMBL:KTD18751.1, ECO:0000313|Proteomes:UP000054869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD18751.1,
RC ECO:0000313|Proteomes:UP000054869};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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:KTD18751.1}.
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DR EMBL; LNYI01000057; KTD18751.1; -; Genomic_DNA.
DR RefSeq; WP_028372467.1; NZ_LT906451.1.
DR AlphaFoldDB; A0A0W0VF74; -.
DR STRING; 45067.Llan_2354; -.
DR PATRIC; fig|45067.4.peg.2473; -.
DR eggNOG; COG0654; Bacteria.
DR OrthoDB; 9769565at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000054869; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000054869}.
FT DOMAIN 6..341
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 390 AA; 42967 MW; 6634B01D8D825938 CRC64;
MTGHFDIMVA GGGIVGLTAA LAMASRGFKV AVLDGSPLTT DCKEFDPRVY AINLASQELL
EKLGVWQQLD KSRRSPYRHM HVWDAMNKAS IDFDARMIVA NALGHILEES ILKTALLKQV
EAQEKITVFA RTKVEKVEQK EENIAIESTS HTWTAQLLMI ADGANSFCRQ LLKVPLITWP
YHQEAIVALV NTEKPHQQTA YQVFNPDGPL AFLPLADDHL CSIVWSTTPA HAKRLMHAAE
HDFSEELTIA FAHRLGQVSV RSTRYCFPLT MRHAKNYSGK SWILLGDAAH TIHPLAGLGL
NVGLADVATW LGCLDNTANK ISNRALGSYQ RQRKSAVWQI IALMGGLKTL FSNPLSPVIA
LRGAGLRICN NINALKKFFI AQAAGKSVEP
//
