UBIG_BORBR
ID UBIG_BORBR Reviewed; 241 AA.
AC Q7WGT9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=BB3475;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE33967.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX640447; CAE33967.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_033451944.1; NC_002927.3.
DR AlphaFoldDB; Q7WGT9; -.
DR SMR; Q7WGT9; -.
DR STRING; 257310.BB3475; -.
DR EnsemblBacteria; CAE33967; CAE33967; BB3475.
DR KEGG; bbr:BB3475; -.
DR eggNOG; COG2227; Bacteria.
DR HOGENOM; CLU_042432_5_0_4; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001027; Chromosome.
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; S-adenosyl-L-methionine; Transferase;
KW Ubiquinone biosynthesis.
FT CHAIN 1..241
FT /note="Ubiquinone biosynthesis O-methyltransferase"
FT /id="PRO_0000193368"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
SQ SEQUENCE 241 AA; 25960 MW; 96B5EEFB7D2F1A07 CRC64;
MTTATQSSAP GVNVDQAEVE KFSALAARWW DPESEFKPLH AINPLRLGWI QETAGSLSGK
RVLDVGCGGG ILSESMAVAG AQVTGIDLAE KSLKIARLHG LESGVKVDYR AVPVEELATE
QPGQYDVVTC MEMLEHVPDP ASVVRACAAL AKPGGWVFFS TLNRNPKSFL FAIVGAEYVL
RLLPRGTHSY DSFIKPSELA ASARQAGLEP TGMRGMEYNP ITQVYSLSAN TSVNYLMSTR
K
