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UBIG_YERPY
ID   UBIG_YERPY              Reviewed;         242 AA.
AC   B1JS96;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=YPK_2847;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA69123.1; -; Genomic_DNA.
DR   RefSeq; WP_002210820.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JS96; -.
DR   SMR; B1JS96; -.
DR   EnsemblBacteria; ACA69123; ACA69123; YPK_2847.
DR   GeneID; 66842311; -.
DR   KEGG; ypy:YPK_2847; -.
DR   PATRIC; fig|502800.11.peg.3562; -.
DR   OMA; RGTHDWE; -.
DR   UniPathway; UPA00232; -.
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..242
FT                   /note="Ubiquinone biosynthesis O-methyltransferase"
FT                   /id="PRO_1000199711"
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   242 AA;  27466 MW;  A397DB4825EEDA34 CRC64;
     MRAKTTSRHH NVDEQEIAKF EAVASRWWDL EGEFKPLHRI NPLRLNYILQ RSGGIFEKKV
     LDVGCGGGIL AESMAREGAQ VTGLDMGYEP LQVARLHALE TGVKLEYVQE TVENHAQQHP
     QHYDVVTCME MLEHVPDPAS VVRACAQLVK PGGHVFFSTI NRNTKSWLMA VVGAEYLLKM
     VPKGTHDAKK FIRPSELIGW VDQTPLLERH IIGLHYNPIT DHFKLGRNVD VNYMVHTQRD
     SE
 
 
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