COQ3_RAT
ID COQ3_RAT Reviewed; 345 AA.
AC Q63159; A0JN24; Q642D7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {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=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE EC=2.1.1.114 {ECO:0000255|HAMAP-Rule:MF_03190};
DE Flags: Precursor;
GN Name=Coq3 {ECO:0000255|HAMAP-Rule:MF_03190};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-345.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8125303; DOI=10.1016/0378-1119(94)90810-9;
RA Marbois B.N., Hsu A., Pillai R., Colicelli J., Clarke C.F.;
RT "Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate
RT methyltransferase by functional complementation of a Saccharomyces
RT cerevisiae mutant deficient in ubiquinone biosynthesis.";
RL Gene 138:213-217(1994).
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 -!- 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; BC081811; AAH81811.1; -; mRNA.
DR EMBL; BC126094; AAI26095.1; -; mRNA.
DR EMBL; L20427; AAC37643.1; -; mRNA.
DR PIR; I53714; I53714.
DR RefSeq; NP_062060.1; NM_019187.1.
DR RefSeq; XP_017448690.1; XM_017593201.1.
DR AlphaFoldDB; Q63159; -.
DR SMR; Q63159; -.
DR BioGRID; 247973; 1.
DR STRING; 10116.ENSRNOP00000013384; -.
DR iPTMnet; Q63159; -.
DR PhosphoSitePlus; Q63159; -.
DR PaxDb; Q63159; -.
DR PRIDE; Q63159; -.
DR Ensembl; ENSRNOT00000013384; ENSRNOP00000013384; ENSRNOG00000009974.
DR GeneID; 29309; -.
DR KEGG; rno:29309; -.
DR UCSC; RGD:2380; rat.
DR CTD; 51805; -.
DR RGD; 2380; Coq3.
DR eggNOG; KOG1270; Eukaryota.
DR GeneTree; ENSGT00390000007284; -.
DR HOGENOM; CLU_042432_0_1_1; -.
DR InParanoid; Q63159; -.
DR OMA; RGTHDWE; -.
DR OrthoDB; 1542938at2759; -.
DR PhylomeDB; Q63159; -.
DR BioCyc; MetaCyc:MON-13874; -.
DR BRENDA; 2.1.1.114; 5301.
DR BRENDA; 2.1.1.222; 5301.
DR BRENDA; 2.1.1.64; 5301.
DR Reactome; R-RNO-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q63159; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009974; Expressed in heart and 20 other tissues.
DR Genevisible; Q63159; RN.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; ISO:RGD.
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:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IMP:RGD.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008171; F:O-methyltransferase activity; ISO:RGD.
DR GO; GO:0006071; P:glycerol metabolic process; ISO:RGD.
DR GO; GO:0032259; P:methylation; IDA:RGD.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IGI:RGD.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Membrane; Methyltransferase; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT CHAIN 87..345
FT /note="Ubiquinone biosynthesis O-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000035928"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS4"
FT MOD_RES 149
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS4"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS4"
SQ SEQUENCE 345 AA; 38708 MW; 68ABF28DF7E252AA CRC64;
MWRGGRLSSR GVRFLETLGF ACPSAVAEPP RVTSWTAFSG NQLTRNLQIK PWEFSGHRTM
WLRSYRITFS CLTRLKTYRS SWKKLYSTSQ TVDSKEVKTF QALAHSWWDE QGKFAPLHSM
NDLRVPFIRD NLLKTSTNHD PGKPLSGMKI LDVGCGGGLL TEPLGRLGAS VVGIDPVAEN
IKIAQHHKSF DPVLDKRIQY RVCSLEETLN ENAECFDAVV ASEVVEHVNN LEMFIQCCYQ
VLKPGGSLFI TTVNKTQLSY VLGIVFSEQI AGIVPKGTHT WEKFVSPEKL ESILEPNGLS
VETVAGMVYN PFSGYWHWTE NTSLNYAAHA VRARAQEHLE PAESA
