UBIG_ECOUT
ID UBIG_ECOUT Reviewed; 240 AA.
AC Q1R9I4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE AltName: Full=2-octaprenyl-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-8 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=UTI89_C2513;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE07980.1; -; Genomic_DNA.
DR RefSeq; WP_000990768.1; NC_007946.1.
DR AlphaFoldDB; Q1R9I4; -.
DR SMR; Q1R9I4; -.
DR PRIDE; Q1R9I4; -.
DR EnsemblBacteria; ABE07980; ABE07980; UTI89_C2513.
DR KEGG; eci:UTI89_C2513; -.
DR HOGENOM; CLU_042432_5_0_6; -.
DR OMA; RGTHDWE; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001952; 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..240
FT /note="Ubiquinone biosynthesis O-methyltransferase"
FT /id="PRO_1000013900"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
SQ SEQUENCE 240 AA; 26559 MW; D4EB4207F06B1657 CRC64;
MNAEKSPVNH NVDHEEIAKF EAVASRWWDL EGEFKPLHRI NPLRLGYIAE RAGGLFGKKV
LDVGCGGGIL AESMAREGAT VTGLDMGFEP LQVAKLHALE SGIQVDYVQE TVEEHAAKHA
GQYDVVTCME MLEHVPDPQS VVRACAQLVK PGGDVFFSTL NRNGKSWLMA VVGAEYILRM
VPKGTHDVKK FIKPAELLGW VDQTSLKERH MTGLHYNPIT NSFKLGPGVD VNYMLHTQNK
