UBIG_PARXL
ID UBIG_PARXL Reviewed; 232 AA.
AC Q13VB4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000255|HAMAP-Rule:MF_00472};
DE EC=2.1.1.222 {ECO:0000255|HAMAP-Rule:MF_00472};
DE AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_00472};
GN Name=ubiG {ECO:0000255|HAMAP-Rule:MF_00472}; OrderedLocusNames=Bxeno_A3437;
GN ORFNames=Bxe_A0972;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-
CC Rule:MF_00472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-
CC COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-
CC methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:31411, Rhea:RHEA-COMP:9550,
CC Rhea:RHEA-COMP:9551, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:62729, ChEBI:CHEBI:62731;
CC EC=2.1.1.222; Evidence={ECO:0000255|HAMAP-Rule:MF_00472};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00472}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. UbiG/COQ3
CC family. {ECO:0000255|HAMAP-Rule:MF_00472}.
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DR EMBL; CP000270; ABE31975.1; -; Genomic_DNA.
DR RefSeq; WP_011489489.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13VB4; -.
DR SMR; Q13VB4; -.
DR STRING; 266265.Bxe_A0972; -.
DR EnsemblBacteria; ABE31975; ABE31975; Bxe_A0972.
DR KEGG; bxb:DR64_3133; -.
DR KEGG; bxe:Bxe_A0972; -.
DR PATRIC; fig|266265.5.peg.3610; -.
DR eggNOG; COG2227; Bacteria.
DR OMA; RGTHDWE; -.
DR OrthoDB; 1515497at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001817; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0102208; F:2-polyprenyl-6-hydroxyphenol methylase activity; IEA:RHEA.
DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00472; UbiG; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010233; UbiG_MeTrfase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01983; UbiG; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..232
FT /note="Ubiquinone biosynthesis O-methyltransferase"
FT /id="PRO_1000013897"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
SQ SEQUENCE 232 AA; 25451 MW; C6D636066CA0F847 CRC64;
MTNADPHELQ KFSDLAHRWW DPNAEFKPLH ELNPIRLSWI DAHAHLTGKT VLDIGCGGGI
LSESMASLGA HVKGIDLSTQ ALGVADLHSL ESGVTVDYEE IAAEALAARE PGTYDVVTCM
EMLEHVPQPA AIVEACRTLV KPGGWVFFST LNRNVKSYLF AVIGAEYIAQ MLPKGTHDYA
RFIRPSELAS FARATNLRTA DIKGIVYNPL SKHFTLSADT SVNYMLACRR DA
