ID D7H895_VIBCL Unreviewed; 245 AA.
AC D7H895;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=VCRC385_01968 {ECO:0000313|EMBL:EFH75276.1};
OS Vibrio cholerae RC385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH75276.1, ECO:0000313|Proteomes:UP000004696};
RN [1] {ECO:0000313|Proteomes:UP000004696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC385 {ECO:0000313|Proteomes:UP000004696};
RA Heidelberg J.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFH75276.1, ECO:0000313|Proteomes:UP000004696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC385 {ECO:0000313|EMBL:EFH75276.1,
RC ECO:0000313|Proteomes:UP000004696};
RG The Broad Institute Genome Sequencing Platform;
RA Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Walk T., White J., Yandava C., Borodovsky M.,
RA Heidelberg J., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Vibrio cholerae RC385.";
RL Submitted (OCT-2009) 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; GG774555; EFH75276.1; -; Genomic_DNA.
DR RefSeq; WP_000146463.1; NZ_GG774555.1.
DR AlphaFoldDB; D7H895; -.
DR SMR; D7H895; -.
DR GeneID; 69720061; -.
DR PATRIC; fig|345074.23.peg.3207; -.
DR HOGENOM; CLU_042432_5_0_6; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000004696; 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: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};
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:EFH75276.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00472}.
FT BINDING 49
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
SQ SEQUENCE 245 AA; 27238 MW; 3C050766DD23E54F CRC64;
MASIDLASTP LTATQNVDPN EIKKFEDMAS RWWDLEGEFK PLHQINPLRL NYVLEKANGL
FGKRVLDVGC GGGILAESMA REGAQVTGLD MGKEPLEVAR LHALETGTKL TYIQSTVEAH
AEANPHTYDV VTCMEMLEHV PDPLSVIQSC AKLVKPGGHV FFSTLNRNVK SYLFAIVGAE
KLLKIVPEGT HDHNKFIRPS ELLKMVDHTA LQEQGITGLH YNPFTDTYRL GSNVDVNYIV
HTRLF
//
