COQ3_YEAST
ID COQ3_YEAST Reviewed; 312 AA.
AC P27680; D6W1X2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000305};
DE AltName: Full=3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000303|PubMed:1885593};
DE Short=DHHB methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000303|PubMed:1885593};
DE Short=DHHB-MT {ECO:0000255|HAMAP-Rule:MF_03190};
DE Short=DHHB-MTase {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000305|PubMed:10419476};
DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000269|PubMed:10419476};
DE AltName: Full=3-demethylubiquinone-6 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=Hexaprenyldihydroxybenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000305|PubMed:10419476};
DE EC=2.1.1.114 {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000269|PubMed:10419476};
DE Flags: Precursor;
GN Name=COQ3 {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000303|PubMed:1885593};
GN OrderedLocusNames=YOL096C {ECO:0000312|SGD:S000005456}; ORFNames=HRF316;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=D273-10B/A1;
RX PubMed=1885593; DOI=10.1016/s0021-9258(18)55349-7;
RA Clarke C.F., Williams W., Teruya J.H.;
RT "Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and
RT sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
RT gene.";
RL J. Biol. Chem. 266:16636-16644(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=10419476; DOI=10.1074/jbc.274.31.21665;
RA Poon W.W., Barkovich R.J., Hsu A.Y., Frankel A., Lee P.T., Shepherd J.N.,
RA Myles D.C., Clarke C.F.;
RT "Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-
RT methyltransferase steps in coenzyme Q biosynthesis.";
RL J. Biol. Chem. 274:21665-21672(1999).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [10]
RP INTERACTION WITH COQ4, AND SUBUNIT.
RX PubMed=15792955; DOI=10.1074/jbc.m501315200;
RA Marbois B.N., Gin P., Faull K.F., Poon W.W., Lee P.T., Strahan J.,
RA Shepherd J.N., Clarke C.F.;
RT "Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the
RT biosynthesis of coenzyme Q.";
RL J. Biol. Chem. 280:20231-20238(2005).
RN [11]
RP SUBUNIT.
RX PubMed=24406904; DOI=10.1016/j.bbalip.2013.12.017;
RA He C.H., Xie L.X., Allan C.M., Tran U.C., Clarke C.F.;
RT "Coenzyme Q supplementation or over-expression of the yeast Coq8 putative
RT kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null
RT mutants.";
RL Biochim. Biophys. Acta 1841:630-644(2014).
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. Catalyzes the methylation of
CC 3,4-dihydroxy-5-hexaprenylbenzoate (DHHB) to 3-methoxy-4-hydroxy-5-
CC hexaprenylbenzoate (HMHB) and the methylation of 2-hexaprenyl-3-methyl-
CC 5-hydroxy-6-methoxy-1,4-benzoquinol (3-demethylubiquinol-6) to
CC ubiquinol-6. {ECO:0000269|PubMed:10419476}.
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:0000255|HAMAP-
CC Rule:MF_03190, ECO:0000269|PubMed:10419476};
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:0000255|HAMAP-
CC Rule:MF_03190, ECO:0000269|PubMed:10419476};
CC -!- ACTIVITY REGULATION: Regulated in response to catabolite repression.
CC {ECO:0000269|PubMed:1885593}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000305|PubMed:10419476}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 (PubMed:15792955,
CC PubMed:24406904). Interacts directly with COQ4 (PubMed:15792955).
CC {ECO:0000269|PubMed:15792955, ECO:0000269|PubMed:24406904}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03190, ECO:0000269|PubMed:10419476,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03190,
CC ECO:0000269|PubMed:10419476}; Matrix side {ECO:0000255|HAMAP-
CC Rule:MF_03190, ECO:0000269|PubMed:10419476}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_03190,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63972.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA88165.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA99108.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA99109.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M73270; AAB63972.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z48149; CAA88165.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74838; CAA99109.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74837; CAA99108.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10688.1; -; Genomic_DNA.
DR PIR; A41171; A41171.
DR RefSeq; NP_014545.2; NM_001183350.1.
DR AlphaFoldDB; P27680; -.
DR SMR; P27680; -.
DR BioGRID; 34306; 67.
DR ComplexPortal; CPX-1155; CoQ biosynthetic complex.
DR DIP; DIP-7399N; -.
DR IntAct; P27680; 5.
DR STRING; 4932.YOL096C; -.
DR MaxQB; P27680; -.
DR PaxDb; P27680; -.
DR PRIDE; P27680; -.
DR EnsemblFungi; YOL096C_mRNA; YOL096C; YOL096C.
DR GeneID; 854057; -.
DR KEGG; sce:YOL096C; -.
DR SGD; S000005456; COQ3.
DR VEuPathDB; FungiDB:YOL096C; -.
DR eggNOG; KOG1270; Eukaryota.
DR GeneTree; ENSGT00390000007284; -.
DR HOGENOM; CLU_042432_3_0_1; -.
DR InParanoid; P27680; -.
DR OMA; RGTHDWE; -.
DR BioCyc; MetaCyc:YOL096C-MON; -.
DR BioCyc; YEAST:YOL096C-MON; -.
DR BRENDA; 2.1.1.114; 984.
DR BRENDA; 2.1.1.222; 984.
DR BRENDA; 2.1.1.64; 984.
DR Reactome; R-SCE-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:P27680; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P27680; protein.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:WormBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
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; IMP:SGD.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IMP:SGD.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00472; UbiG; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010233; UbiG_MeTrfase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01983; UbiG; 1.
PE 1: Evidence at protein level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT CHAIN 33..312
FT /note="Ubiquinone biosynthesis O-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000035932"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
SQ SEQUENCE 312 AA; 36331 MW; F0D973ADE4C2D6FD CRC64;
MLLRSRFLKV IHVRKQLSAC SRFAIQTQTR CKSTDASEDE VKHFQELAPT WWDTDGSQRI
LHKMNLTRLD FVQRTVRNQV KIQNPEIFVP GFNYKEFLPE YVCDNIQREM QESIETNLDK
RPEVSVLDVG CGGGILSESL ARLKWVKNVQ GIDLTRDCIM VAKEHAKKDP MLEGKINYEC
KALEDVTGQF DIITCMEMLE HVDMPSEILR HCWSRLNPEK GILFLSTINR DLISWFTTIF
MGENVLKIVP KGTHHLSKYI NSKEILAWFN DNYSGQFRLL DLKGTMYLPY QGWVEHDCSD
VGNYFMAIQR LN
