ID   A0A926M514_9PROT        Unreviewed;       240 AA.
AC   A0A926M514;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   29-MAY-2024, entry version 7.
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   ECO:0000313|EMBL:MBD1142655.1};
GN   ORFNames=IDH22_01575 {ECO:0000313|EMBL:MBD1142655.1};
OS   Pelagibacterales bacterium SAG-MED35.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales.
OX   NCBI_TaxID=2760037 {ECO:0000313|EMBL:MBD1142655.1, ECO:0000313|Proteomes:UP000611396};
RN   [1] {ECO:0000313|EMBL:MBD1142655.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAG-MED35 {ECO:0000313|EMBL:MBD1142655.1};
RX   PubMed=31840364;
RA   Haro-Moreno J.M., Rodriguez-Valera F., Rosselli R., Martinez-Hernandez F.,
RA   Roda-Garcia J.J., Gomez M.L., Fornas O., Martinez-Garcia M.,
RA   Lopez-Perez M.;
RT   "Ecogenomics of the SAR11 clade.";
RL   Environ. Microbiol. 22:1748-1763(2020).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBD1142655.1}.
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DR   EMBL; JACWEF010000006; MBD1142655.1; -; Genomic_DNA.
DR   Proteomes; UP000611396; Unassembled WGS sequence.
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   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|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00472}; Reference proteome {ECO:0000313|Proteomes:UP000611396};
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};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_00472}.
FT   DOMAIN          63..156
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
FT   BINDING         36
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
SQ   SEQUENCE   240 AA;  27659 MW;  81B4713B710567D5 CRC64;
     MSSVNKIEIE KFSNMADEWW DPHGKFKPLH KFNPIRIKYI KENIIRQFKI KNKNKPLSGI
     SILDIGCGGG LLSEPMCRLG ADVTGIDASI KNIKISKLHA KKDNLKINYI CSSPEKLKIS
     EKFDVILNME IVEHVEDISF FLKSCSKLLN KNGLMFVATI NKTLKSYVFA IVGAEYVLRW
     LPIGTHDWEK FVKPEELKEI LSKNNLFLKK LDGMHFNIIK DEWNITNDLS INYIAKFLKN
//