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Database: UniProt
Entry: G9MPD9_HYPVG
LinkDB: G9MPD9_HYPVG
Original site: G9MPD9_HYPVG 
ID   G9MPD9_HYPVG            Unreviewed;       272 AA.
AC   G9MPD9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=TRIVIDRAFT_147251 {ECO:0000313|EMBL:EHK23740.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK23740.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK23740.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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:EHK23740.1}.
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DR   EMBL; ABDF02000005; EHK23740.1; -; Genomic_DNA.
DR   RefSeq; XP_013957946.1; XM_014102471.1.
DR   AlphaFoldDB; G9MPD9; -.
DR   STRING; 413071.G9MPD9; -.
DR   EnsemblFungi; EHK23740; EHK23740; TRIVIDRAFT_147251.
DR   GeneID; 25787986; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_147251; -.
DR   eggNOG; KOG1270; Eukaryota.
DR   HOGENOM; CLU_042432_3_1_1; -.
DR   InParanoid; G9MPD9; -.
DR   OMA; LASRWWD; -.
DR   OrthoDB; 1459at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
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:0061543; F:3-demethylubiquinol-6 3-O-methyltransferase activity; IEA:EnsemblFungi.
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; 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   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:UP000007115};
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   DOMAIN          86..188
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT   BINDING         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
SQ   SEQUENCE   272 AA;  29575 MW;  4FE68930C1A80157 CRC64;
     MQVVSAAVSA AVSVPVPGTA ATAPSRWHSS SSSVNPNEVS HFNALAAEWW EPHGSSRMLH
     LMNPLRHDFI RACRESSDDP NSVTYLDIGC GGGIFAESAA RLPSTKHVTA IDPTPSVLSV
     AKAHARKDPA LAGKLSYRLS SVEQLDVPAE GQGYDIVTLF EVIEHIDDPG AFLERVRPLV
     KPGGWLIMST IARTWVSWFT TNLVAEDILR IVPPGTHDWN KYINEGELRG YLAGKGWDSA
     RVMGVVYVPG LGWKEVKGSE KVGNYFFAVR KA
//
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