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COQ3_DICDI
ID   COQ3_DICDI              Reviewed;         321 AA.
AC   Q54XD0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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};
GN   Name=coq3 {ECO:0000255|HAMAP-Rule:MF_03190}; ORFNames=DDB_G0279037;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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.
CC       {ECO:0000255|HAMAP-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; AAFI02000026; EAL67940.1; -; Genomic_DNA.
DR   RefSeq; XP_641931.1; XM_636839.1.
DR   AlphaFoldDB; Q54XD0; -.
DR   SMR; Q54XD0; -.
DR   STRING; 44689.DDB0231592; -.
DR   PaxDb; Q54XD0; -.
DR   EnsemblProtists; EAL67940; EAL67940; DDB_G0279037.
DR   GeneID; 8621843; -.
DR   KEGG; ddi:DDB_G0279037; -.
DR   dictyBase; DDB_G0279037; coq3.
DR   eggNOG; KOG1270; Eukaryota.
DR   HOGENOM; CLU_042432_2_1_1; -.
DR   InParanoid; Q54XD0; -.
DR   OMA; RGTHDWE; -.
DR   PhylomeDB; Q54XD0; -.
DR   Reactome; R-DDI-2142789; Ubiquinol biosynthesis.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:Q54XD0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; ISS:dictyBase.
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; ISS:dictyBase.
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   Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..321
FT                   /note="Ubiquinone biosynthesis O-methyltransferase,
FT                   mitochondrial"
FT                   /id="PRO_0000328306"
FT   BINDING         102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT   BINDING         157
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   321 AA;  36538 MW;  5AF617DB3C0C767C CRC64;
     MIYHLISKSC QRLNKPNLIN NLIKSQKQSI IYSSSSSSGS SKFISNKYFT TTSNSNNNSN
     NTTTTTTTTL RQDEIDFFNQ QSSDWWNPEG TMKPLHRMNP FRVKYICDRL KIYNEKVSKN
     PIHLPLEGLN VIDVGCGVGL LTESLSRLGA SKVVGLDAAK NNILMAISHA SFDQKLNENI
     QNKSLNYLES TIENFYNIEN DQQFDAVCSL EVIEHVDNPK QFIDYLSKIV KPGGSIFIST
     INKTFLSYIS AILGAEYIFR MVPVGTHHWD QFIKPKDLES YFDSNNCQIT DLKGLVYNPL
     TCEWDFTNDL NVNYLLHAIK K
 
 
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