ID A0A0M3T221_9GAMM Unreviewed; 234 AA.
AC A0A0M3T221;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=W908_05565 {ECO:0000313|EMBL:ALE02061.1};
OS Candidatus Pseudothioglobus singularis PS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE02061.1, ECO:0000313|Proteomes:UP000068905};
RN [1] {ECO:0000313|EMBL:ALE02061.1, ECO:0000313|Proteomes:UP000068905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000313|EMBL:ALE02061.1,
RC ECO:0000313|Proteomes:UP000068905};
RX PubMed=26494659;
RA Marshall K.T., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01155-e01115(2015).
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; CP006911; ALE02061.1; -; Genomic_DNA.
DR RefSeq; WP_053820276.1; NZ_CP006911.1.
DR AlphaFoldDB; A0A0M3T221; -.
DR STRING; 1125411.W908_05565; -.
DR KEGG; tsn:W908_05565; -.
DR PATRIC; fig|1125411.7.peg.1097; -.
DR OrthoDB; 9801538at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000068905; 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: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; 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; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00472}; Reference proteome {ECO:0000313|Proteomes:UP000068905};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00472};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00472}; Ubiquinone {ECO:0000313|EMBL:ALE02061.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00472}.
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
SQ SEQUENCE 234 AA; 26148 MW; 056C0AD8B8D1FF56 CRC64;
MNSNVDHEEV NKFAALAARW WDRNSEFKPL HDINPLRLNY IKEQCGGTLE GKRILDVGCG
GGILSESLAL EGATVVGIDL AEAGLEVAKL HLLESGLDID YQSISAEDLT EKETESFDVI
ACLEMLEHVP DPSLVIEACS KLVKPQGQVF FSTINRNPKS YFFAIVGAEY VLNLLPKGTH
NYEKFIRPSE IDEWARSSEL SISSMIGMTY NPITKKYKLG DDVSVNYMVH YEKK
//
