ID Q1LIG3_CUPMC Unreviewed; 474 AA.
AC Q1LIG3;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family {ECO:0000313|EMBL:ABF10063.1};
GN OrderedLocusNames=Rmet_3191 {ECO:0000313|EMBL:ABF10063.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF10063.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF10063.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1LIG3; -.
DR STRING; 266264.Rmet_3191; -.
DR KEGG; rme:Rmet_3191; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_3_4; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002429; Chromosome.
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:UP000002429};
KW Ubiquinone {ECO:0000313|EMBL:ABF10063.1}.
FT DOMAIN 63..423
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 50955 MW; CAF01D78BD9F78AF CRC64;
MPASGGRVRR PGGKRQNRSV CVSEPITRME PPSRRYNSGM SGPAASVSRT VTSSMSSNSS
SRFQVAVVGG GIVGKACALL LAQQGMQVAL AAPRPAAEGA RRGGDDWDAR IYAFSASSQA
LLERLRVWEA LDPARVQPVR DMRVFGDESA AETDPSLDGD LHFSAYAAAV PQLAWIVESG
HVERVLDTAL RFQHQVKWFD DTATGLERDV DGVTLTLASG AQVRANLLVG ADGSRSWVRQ
QCHIGTTQRR YRQLGVVANF QCELPHQETA WQWFLGAPEK LMADEEPANG EILAMLPLPG
NRVSMVWSAD EAHAHDLLAL SPEALAATVA QVASGAVGAR FGALRCITPA QGFPLVLQRA
EQFVQPHVAL VGDAAHVVHP LAGQGMNLGL RDVVELGRVM ADKESFRSEG DLRLLRRYER
ARATDLLSLT AATDGLHRLF SLPGTPARVV RNLGMRAVGS QGLIKRLLIG HALG
//
