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Database: UniProt
Entry: I7IAE1_9RICK
LinkDB: I7IAE1_9RICK
Original site: I7IAE1_9RICK 
ID   I7IAE1_9RICK            Unreviewed;       388 AA.
AC   I7IAE1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472};
DE   AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000256|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.222 {ECO:0000256|HAMAP-Rule:MF_00472};
DE   AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_00472};
GN   Name=ubiG {ECO:0000256|HAMAP-Rule:MF_00472};
GN   ORFNames=wOo_06110 {ECO:0000313|EMBL:CCF78234.1};
OS   Wolbachia endosymbiont of Onchocerca ochengi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=100901 {ECO:0000313|EMBL:CCF78234.1, ECO:0000313|Proteomes:UP000007516};
RN   [1] {ECO:0000313|EMBL:CCF78234.1, ECO:0000313|Proteomes:UP000007516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Adamawa_Cameroon {ECO:0000313|Proteomes:UP000007516};
RX   PubMed=22919073; DOI=10.1101/gr.138420.112;
RA   Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA   Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA   Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT   "Analysis of gene expression from the Wolbachia genome of a filarial
RT   nematode supports both metabolic and defensive roles within the
RT   symbiosis.";
RL   Genome Res. 22:2467-2477(2012).
CC   -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC       in the ubiquinone biosynthetic pathway. {ECO:0000256|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:0000256|HAMAP-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:0000256|HAMAP-
CC         Rule:MF_00472};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00472}.
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC       {ECO:0000256|ARBA:ARBA00008754}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. UbiG/COQ3
CC       family. {ECO:0000256|HAMAP-Rule:MF_00472}.
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DR   EMBL; HE660029; CCF78234.1; -; Genomic_DNA.
DR   RefSeq; WP_014869019.1; NC_018267.1.
DR   AlphaFoldDB; I7IAE1; -.
DR   STRING; 100901.wOo_06110; -.
DR   KEGG; woo:wOo_06110; -.
DR   PATRIC; fig|100901.6.peg.497; -.
DR   eggNOG; COG0698; Bacteria.
DR   eggNOG; COG2227; Bacteria.
DR   HOGENOM; CLU_042432_1_0_5; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000007516; Chromosome.
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:0061542; F:3-demethylubiquinol-n 3-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR004785; RpiB.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010233; UbiG_MeTrfase.
DR   NCBIfam; TIGR01120; rpiB; 1.
DR   NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR   NCBIfam; TIGR01983; UbiG; 1.
DR   PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR   PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR   Pfam; PF02502; LacAB_rpiB; 1.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000313|EMBL:CCF78234.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007516};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00472};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000313|EMBL:CCF78234.1};
KW   Ubiquinone {ECO:0000313|EMBL:CCF78234.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         234
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         276
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
SQ   SEQUENCE   388 AA;  43722 MW;  436F8050CBFDFDA3 CRC64;
     MSNIISIASD HAGYELKSEI KPYLKTLGYT VTDHGCTAEQ KSVDYPDYAI KVVKDIINRK
     ADYGILICGT GLGMSTVANR FEGIYAALCD SVEITKLARE HGNANVLCLG AGFTNNELAK
     DIVKQFLETE FSKESRHKKR LDKLSNISRK KNTQTYNEDE VSKFAKIASE WWNEDGKFKL
     LHMMNPVRGS YIIEKIKEFK KCDLNEISLL DVGCGGGILS ESMARIGINV VGIDICEENI
     KAAQSYTKKV GSNIEYIHTS IEELSNSKKY DVVLLMEVVE HVNNLEFFMK KAVELLKPEG
     LIFISTINRN IKSFCFAIIG AEYILNWLPK GTHNWNKFLK PSEIANHLRE NNVTLQSMTG
     MTYNVIKREW NLTQDVSINY ILCGLANG
//
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