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Database: UniProt
Entry: A0A1R3VLZ0_9GAMM
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ID   A0A1R3VLZ0_9GAMM        Unreviewed;       236 AA.
AC   A0A1R3VLZ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05216526_0025 {ECO:0000313|EMBL:SIT65577.1};
OS   Ectothiorhodosinus mongolicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodosinus.
OX   NCBI_TaxID=233100 {ECO:0000313|EMBL:SIT65577.1, ECO:0000313|Proteomes:UP000223759};
RN   [1] {ECO:0000313|EMBL:SIT65577.1, ECO:0000313|Proteomes:UP000223759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M9 {ECO:0000313|EMBL:SIT65577.1,
RC   ECO:0000313|Proteomes:UP000223759};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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 methyltransferase superfamily. UbiG/COQ3
CC       family. {ECO:0000256|HAMAP-Rule:MF_00472}.
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DR   EMBL; FTPK01000001; SIT65577.1; -; Genomic_DNA.
DR   RefSeq; WP_076753886.1; NZ_FTPK01000001.1.
DR   AlphaFoldDB; A0A1R3VLZ0; -.
DR   STRING; 233100.SAMN05216526_0025; -.
DR   OrthoDB; 9801538at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000223759; Unassembled WGS sequence.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR013216; Methyltransf_11.
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; PF08241; Methyltransf_11; 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:SIT65577.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223759};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00472};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000313|EMBL:SIT65577.1};
KW   Ubiquinone {ECO:0000313|EMBL:SIT65577.1};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_00472}.
FT   DOMAIN          57..153
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
FT   BINDING         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         60
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
SQ   SEQUENCE   236 AA;  26195 MW;  91604A9490DCD4A2 CRC64;
     MAQTQANVDA GEIAKFDEMA HRWWDPQGEY RPLHEINPLR LDYIESRVGA LEGLQVLDVG
     CGGGLLSEGL ARRGAHVTGI DLGENALDVA RMHLFESGLE VDYQLRSAED MAVAKPGQFD
     VVTCMEMLEH VPDPGSVLTA CAQLLKPGGH LVVATLNRTP KAFALAIVGA EYVLRWLPRG
     THEYARFIRP SEMEAWMRAA DLRMRDLMGL HYDPLARRYH LGPGVDVNYL AHAVRD
//
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