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UBIG_RHIME
ID   UBIG_RHIME              Reviewed;         248 AA.
AC   Q92MK1;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=R02615;
GN   ORFNames=SMc02440;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591688; CAC47194.1; -; Genomic_DNA.
DR   RefSeq; NP_386721.1; NC_003047.1.
DR   RefSeq; WP_010970076.1; NC_003047.1.
DR   AlphaFoldDB; Q92MK1; -.
DR   SMR; Q92MK1; -.
DR   STRING; 266834.SMc02440; -.
DR   EnsemblBacteria; CAC47194; CAC47194; SMc02440.
DR   GeneID; 61604077; -.
DR   KEGG; sme:SMc02440; -.
DR   PATRIC; fig|266834.11.peg.4113; -.
DR   eggNOG; COG2227; Bacteria.
DR   HOGENOM; CLU_042432_0_0_5; -.
DR   OMA; RGTHDWE; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001976; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Ubiquinone biosynthesis.
FT   CHAIN           1..248
FT                   /note="Ubiquinone biosynthesis O-methyltransferase"
FT                   /id="PRO_0000193396"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT   BINDING         72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT   BINDING         93
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
SQ   SEQUENCE   248 AA;  27438 MW;  0190692A5C18C593 CRC64;
     MSETARTTID QSEVDRFSAM AAEWWDPTGK FRPLHKFNPV RLTYIRDRVS EHFGRDAKSR
     QPLEGLRVLD IGCGGGLLSE PMARMGADVV GADASEKNIG IARTHAAGSG VSVDYRAVTA
     EALAEAGESF DVVLNMEVVE HVADVEFFMT TCAHMVRPGG LMFVATINRT LKAAALAIFA
     AENVLRWLPR GTHQYDKLVR PDELERPLEA SGMEIADRTG VFFNPLANQW NLSRDMDVNY
     MIVAKRPI
 
 
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