ID   UBIG_ECO24              Reviewed;         240 AA.
AC   A7ZP50;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 99.
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};
GN   OrderedLocusNames=EcE24377A_2527;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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         + S-adenosyl-L-homocysteine + H(+); 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 + S-adenosyl-
CC         L-homocysteine + H(+); 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; CP000800; ABV16577.1; -; Genomic_DNA.
DR   RefSeq; WP_000990765.1; NC_009801.1.
DR   AlphaFoldDB; A7ZP50; -.
DR   SMR; A7ZP50; -.
DR   GeneID; 75172359; -.
DR   GeneID; 75206477; -.
DR   KEGG; ecw:EcE24377A_2527; -.
DR   HOGENOM; CLU_042432_5_0_6; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0102208; F:2-polyprenyl-6-hydroxyphenol methylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061542; F:3-demethylubiquinol 3-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010420; F:polyprenyldihydroxybenzoate methyltransferase activity; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 3.40.50.150:FF:000028; Ubiquinone biosynthesis O-methyltransferase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010233; UbiG_MeTrfase.
DR   NCBIfam; TIGR01983; UbiG; 1.
DR   PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43464:SF19; UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Ubiquinone biosynthesis.
FT   CHAIN           1..240
FT                   /note="Ubiquinone biosynthesis O-methyltransferase"
FT                   /id="PRO_1000060385"
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;  26555 MW;  D4EB4707A06F5613 CRC64;
     MNAEKSPVNH NVDHEEIAKF EAVASRWWDL EGEFKPLHRI NPLRLGYIAE RAGGLFGKKV
     LDVGCGGGIL AESMAREGAT VTGLDMGFEP LQVAKLHALE SGIQVDYVQE TVEEHAAKHA
     GQYDVVTCME MLEHVPDPQS VVRACAQLVK PGGDVFFSTL NRNGKSWLMA VVGAEYILRM
     VPKGTHDVKK FIKPAELLGW VDQTSLKERH ITGLHYNPIT NTFKLGPGVD VNYMLHTQNK
//