(data stored in SCRATCH3701 zone)

SWISSPROT: UBIG_RICTY

ID   UBIG_RICTY              Reviewed;         246 AA.
AC   Q68WB5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 87.
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=RT0613;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU04077.1; -; Genomic_DNA.
DR   RefSeq; WP_011191057.1; NC_006142.1.
DR   SMR; Q68WB5; -.
DR   STRING; 257363.RT0613; -.
DR   PRIDE; Q68WB5; -.
DR   EnsemblBacteria; AAU04077; AAU04077; RT0613.
DR   KEGG; rty:RT0613; -.
DR   eggNOG; ENOG4108HWB; Bacteria.
DR   eggNOG; COG2227; LUCA.
DR   HOGENOM; HOG000278065; -.
DR   KO; K00568; -.
DR   OMA; IVPRGTH; -.
DR   OrthoDB; 1515497at2; -.
DR   BioCyc; RTYP257363:G1G0L-617-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000604; Chromosome.
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   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010233; UbiG_MeTrfase.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01983; UbiG; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68WB5.
DR   SWISS-2DPAGE; Q68WB5.
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..246
FT                   /note="Ubiquinone biosynthesis O-methyltransferase"
FT                   /id="PRO_0000193400"
FT   BINDING         36
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT   BINDING         60
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT   BINDING         81
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
FT   BINDING         123
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00472"
SQ   SEQUENCE   246 AA;  28235 MW;  04C2C703B8A38478 CRC64;
     MSSINKKELK KFEKISHNWW NKDGEFGILH RINHIRIEYI IEKIKLHYND ISKLQILDVG
     CGGGLIAAPL ASQGFNVTAI DALKSNIETA TIYAQKNDLK INYLQTTIEE LENDKLYDVV
     ICLEVIEHVE NVQQFILNLV QHIKPNGIAI ISTINRTKKA YLFGIIVAEY ILGWVPKNTH
     DYSKFLKPSE IYEILTDTNI EIKELKGLVF NLARNEWKLS NDIDVNYFMY LGKKINSLSN
     AINSIP
//

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