COQ3_CANAX
ID COQ3_CANAX Reviewed; 327 AA.
AC O93995;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE Short=DHHB methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
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};
DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_03190};
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};
DE EC=2.1.1.114 {ECO:0000255|HAMAP-Rule:MF_03190};
GN Name=COQ3 {ECO:0000255|HAMAP-Rule:MF_03190}; ORFNames=Ca20C1.07;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_03190};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_03190}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03190}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03190}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_03190}.
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DR EMBL; AL033391; CAA21929.1; -; Genomic_DNA.
DR AlphaFoldDB; O93995; -.
DR SMR; O93995; -.
DR VEuPathDB; FungiDB:C6_01840C_A; -.
DR VEuPathDB; FungiDB:CAWG_05184; -.
DR UniPathway; UPA00232; -.
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:UniProtKB-UniRule.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..327
FT /note="Ubiquinone biosynthesis O-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000035930"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
SQ SEQUENCE 327 AA; 37561 MW; 285108D0A32F179F CRC64;
MMVFLVSFIS VEMKSMHCAP LFRQLVFSRS LHYSKTIFHN GRGLTSTSES EMSHFNALAS
SWWDVNGPQR ILHKMNLLRM DFIHDTIRKN LKLNENTDDE VYIPPFSVDL LPQGIKNKID
EDQEMRRDEI LNDSSLTVLD VGCGGGILSE SMARLSFVSS VKGIDLSADV LEAAKLHKQK
DPMLKDKLSY TLNAIEDIPE TERFDIVTMF EVLEHVDYPS RVLLEGLKRL ESGGWLFLST
INRDFVSWFT TIFMGEHVLR IVPVGTHTLE KYINQSEIKD WLQEDSNRKS EFRVADTKGC
VYLPAYGWKF TSCPDVGNYF MAIQRVK
