COQ3_ARATH
ID COQ3_ARATH Reviewed; 322 AA.
AC O49354; O80857; Q94AS6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 164.
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=EMBRYO DEFECTIVE 3002;
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}; Synonyms=EMB3002;
GN OrderedLocusNames=At2g30920; ORFNames=F7F1.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9628017; DOI=10.1046/j.1365-313x.1998.00109.x;
RA Avelange-Macherel M.H., Joyard J.;
RT "Cloning and functional expression of AtCOQ3, the Arabidopsis homologue of
RT the yeast COQ3 gene, encoding a methyltransferase from plant mitochondria
RT involved in ubiquinone biosynthesis.";
RL Plant J. 14:203-213(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-37.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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, ECO:0000305|PubMed:25732537}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side
CC {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; Y15055; CAA75340.1; -; mRNA.
DR EMBL; AC004669; AAC20726.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08458.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62865.1; -; Genomic_DNA.
DR EMBL; AY045828; AAK76502.1; -; mRNA.
DR EMBL; AY091366; AAM14305.1; -; mRNA.
DR PIR; C84714; C84714.
DR PIR; T52284; T52284.
DR RefSeq; NP_001324991.1; NM_001336307.1.
DR RefSeq; NP_180649.1; NM_128644.4.
DR AlphaFoldDB; O49354; -.
DR SMR; O49354; -.
DR BioGRID; 2991; 3.
DR IntAct; O49354; 3.
DR STRING; 3702.AT2G30920.1; -.
DR PaxDb; O49354; -.
DR PRIDE; O49354; -.
DR ProteomicsDB; 241178; -.
DR EnsemblPlants; AT2G30920.1; AT2G30920.1; AT2G30920.
DR EnsemblPlants; AT2G30920.2; AT2G30920.2; AT2G30920.
DR GeneID; 817642; -.
DR Gramene; AT2G30920.1; AT2G30920.1; AT2G30920.
DR Gramene; AT2G30920.2; AT2G30920.2; AT2G30920.
DR KEGG; ath:AT2G30920; -.
DR Araport; AT2G30920; -.
DR TAIR; locus:2052761; AT2G30920.
DR eggNOG; KOG1270; Eukaryota.
DR HOGENOM; CLU_042432_2_1_1; -.
DR InParanoid; O49354; -.
DR OMA; RGTHDWE; -.
DR OrthoDB; 1542938at2759; -.
DR PhylomeDB; O49354; -.
DR BRENDA; 2.1.1.114; 399.
DR BRENDA; 2.1.1.64; 399.
DR UniPathway; UPA00232; -.
DR PRO; PR:O49354; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O49354; baseline and differential.
DR Genevisible; O49354; AT.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
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:0010420; F:3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity; IGI:TAIR.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IGI:TAIR.
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; IGI:TAIR.
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..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 38..322
FT /note="Ubiquinone biosynthesis O-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000035929"
FT REGION 46..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT CONFLICT 311
FT /note="A -> T (in Ref. 1; CAA75340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35332 MW; 75743B58CAA86594 CRC64;
MLASVRVNQL QRLLLSARRL SSSPIIPPSR LLHQRLFSTS DTDASAASFS SSHPKIQTLE
GKASNKSRST SSTTSLNEDE LAKFSAIADT WWHSEGPFKP LHQMNPTRLA FIRSTLCRHF
SKDPSSAKPF EGLKFIDIGC GGGLLSEPLA RMGATVTGVD AVDKNVKIAR LHADMDPVTS
TIEYLCTTAE KLADEGRKFD AVLSLEVIEH VANPAEFCKS LSALTIPNGA TVLSTINRTM
RAYASTIVGA EYILRWLPKG THQWSSFVTP EEMSMILQRA SVDVKEIAGF VYNPITGRWL
LSDDISVNYI AYGTKRKDLG DI
