ID M1PD68_BARAA Unreviewed; 416 AA.
AC M1PD68;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=2-octaprenyl-6-methoxyphenyl hydroxylase {ECO:0000313|EMBL:AGF74531.1};
GN Name=ubiH {ECO:0000313|EMBL:AGF74531.1};
GN OrderedLocusNames=BAnh1_06520 {ECO:0000313|EMBL:AGF74531.1};
OS Bartonella australis (strain Aust/NH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF74531.1, ECO:0000313|Proteomes:UP000011729};
RN [1] {ECO:0000313|EMBL:AGF74531.1, ECO:0000313|Proteomes:UP000011729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF74531.1,
RC ECO:0000313|Proteomes:UP000011729};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
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; CP003123; AGF74531.1; -; Genomic_DNA.
DR AlphaFoldDB; M1PD68; -.
DR STRING; 1094489.BAnh1_06520; -.
DR KEGG; baus:BAnh1_06520; -.
DR PATRIC; fig|1094489.3.peg.798; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_1_5; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000011729; 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}.
FT DOMAIN 22..325
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 416 AA; 46034 MW; 9B12CE41B44E867D CRC64;
MIGYIGKVPA LVISEKNKHK NITVIGAGPI GMLAALNLAH KGYSVSLIGP AACENELRTT
ALMMPAVHML QRFDIWSTLE PYAAALSSIR IIDATSRLVR APTINFYSAE IGEKAFGYNI
PNLKLNNALV NSVAHTPSIT RFFSSAKSFH HQQNHTRITL SDGKIIQASL IVAADGRDSP
TRTAAGIGAQ IWHYRQTALV LNFSHSLPHH NTSNEFHTEH GPFTQVPLPG HNSSLVWVVT
PSRAEKLLNM RSEAVAKVVE DQMQSMLGKI MVKTPVQAWP LSGLIPHYFA ANRTILVGEA
AHVFPPIGAQ GFNLGFRDIQ TLIDIMPDKI SNFNFEKIIA YYNLYRKPDI FVRSGFIHAL
NCALLSDMLL VHIARSFGIE LLRNFSSLRN LFMQEGMHPG SGLRKITRIF TTKSPR
//
