ID A0A151GDG5_9HYPO Unreviewed; 342 AA.
AC A0A151GDG5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03190};
DE AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
DE EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_03190};
DE AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
DE EC=2.1.1.114 {ECO:0000256|HAMAP-Rule:MF_03190};
GN Name=COQ3 {ECO:0000256|HAMAP-Rule:MF_03190};
GN ORFNames=DCS_07092 {ECO:0000313|EMBL:KYK55130.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK55130.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK55130.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK55130.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000256|HAMAP-
CC Rule:MF_03190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-
CC methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-
CC COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694,
CC ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03190};
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_03190};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03190}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000256|HAMAP-
CC Rule:MF_03190}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03190}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03190}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. UbiG/COQ3 family. {ECO:0000256|HAMAP-Rule:MF_03190}.
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:KYK55130.1}.
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DR EMBL; LAYC01000003; KYK55130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GDG5; -.
DR STRING; 98403.A0A151GDG5; -.
DR InParanoid; A0A151GDG5; -.
DR OrthoDB; 1459at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000076580; Chromosome 03.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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:0004395; F:hexaprenyldihydroxybenzoate 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 Membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03190}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03190};
KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03190};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03190}.
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
SQ SEQUENCE 342 AA; 38346 MW; 2635B9FFE781D4D8 CRC64;
MQLHGIVISR FHQLPSSIEL TLGRRADPQT RPSTDITVRL HPLMPAPSWT STTAARLARL
PTSLPRLQPP RTAPSHHGPK LSSRRRWSST FSSVNPDEVS HFNALAGEWW DPHGSSRLLH
LMNPLRHDFI QSCLRSEPPP ATPSVTAPPS LAYLDIGCGG GIFAESAARL PTTRSVTAVD
PTPSVLAVAK AHARKDPSLA GRLTYKQTAV EHLEVPQRDQ DRYDVVTLFE VIEHIDEPAA
LLDRLKPFVK PGGWLVMSTI ARTWLSWFTT NLVAEDLLRI VPRGTHDWNK YINEHELRRY
FAGKGWESPR VMGVVYVPGL GWKEVRGSEH VGNYFFAVRR EQ
//
