ID L2F7R4_9GAMM Unreviewed; 242 AA.
AC L2F7R4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=MOMA_01740 {ECO:0000313|EMBL:ELA09089.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA09089.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA09089.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA09089.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(2013).
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:ELA09089.1}.
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DR EMBL; ANIN01000001; ELA09089.1; -; Genomic_DNA.
DR RefSeq; WP_009766909.1; NZ_ANIN01000001.1.
DR AlphaFoldDB; L2F7R4; -.
DR STRING; 1230338.MOMA_01740; -.
DR PATRIC; fig|1230338.3.peg.384; -.
DR eggNOG; COG2227; Bacteria.
DR OrthoDB; 9801538at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000023795; 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; 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|HAMAP-Rule:MF_00472,
KW ECO:0000313|EMBL:ELA09089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023795};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00472};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000313|EMBL:ELA09089.1};
KW Ubiquinone {ECO:0000313|EMBL:ELA09089.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00472}.
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 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00472"
SQ SEQUENCE 242 AA; 27348 MW; 78B62266D4C49C8A CRC64;
MTQTHNNADF HEIGKFTALA NEWWDKNGAF ATLHDINPLR LNWVEEQTKL QHNSDLSAKK
VLDVGCGGGI LSHAMAERGA QVMGIDLGEE NIQAARFHAK KTHQVIDFQC TAVEDLAKTH
AAQFDVVTCM EMLEHVPNPK SIIDACFALL KPGGVLIMST INRNFKSYLF AIIGAEYVLR
LLDKGTHDFN KFITPAELDR FAERSGFKRQ DLIGLHYNPL TKRYWLAQNV DVNYMMAVYK
PK
//