COQ5_ARATH
ID COQ5_ARATH Reviewed; 288 AA.
AC Q9LVC8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03191};
DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_03191};
DE AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000255|HAMAP-Rule:MF_03191};
DE Flags: Precursor;
GN Name=COQ5 {ECO:0000255|HAMAP-Rule:MF_03191}; OrderedLocusNames=At5g57300;
GN ORFNames=MJB24.11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Methyltransferase required for the conversion of 2-
CC polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-
CC 6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC 1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03191};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_03191}.
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DR EMBL; AB019233; BAA96953.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96880.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96881.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96882.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70845.1; -; Genomic_DNA.
DR EMBL; AY050939; AAK93616.1; -; mRNA.
DR EMBL; AY091173; AAM14112.1; -; mRNA.
DR RefSeq; NP_001078760.1; NM_001085291.3.
DR RefSeq; NP_001190558.1; NM_001203629.1.
DR RefSeq; NP_001332423.1; NM_001345255.1.
DR RefSeq; NP_200540.1; NM_125112.5.
DR AlphaFoldDB; Q9LVC8; -.
DR SMR; Q9LVC8; -.
DR BioGRID; 21079; 2.
DR IntAct; Q9LVC8; 2.
DR STRING; 3702.AT5G57300.3; -.
DR PaxDb; Q9LVC8; -.
DR PRIDE; Q9LVC8; -.
DR ProteomicsDB; 241107; -.
DR EnsemblPlants; AT5G57300.1; AT5G57300.1; AT5G57300.
DR EnsemblPlants; AT5G57300.2; AT5G57300.2; AT5G57300.
DR EnsemblPlants; AT5G57300.3; AT5G57300.3; AT5G57300.
DR EnsemblPlants; AT5G57300.4; AT5G57300.4; AT5G57300.
DR GeneID; 835835; -.
DR Gramene; AT5G57300.1; AT5G57300.1; AT5G57300.
DR Gramene; AT5G57300.2; AT5G57300.2; AT5G57300.
DR Gramene; AT5G57300.3; AT5G57300.3; AT5G57300.
DR Gramene; AT5G57300.4; AT5G57300.4; AT5G57300.
DR KEGG; ath:AT5G57300; -.
DR Araport; AT5G57300; -.
DR TAIR; locus:2165630; AT5G57300.
DR eggNOG; KOG1540; Eukaryota.
DR HOGENOM; CLU_037990_0_1_1; -.
DR InParanoid; Q9LVC8; -.
DR OMA; VRNFENL; -.
DR OrthoDB; 1125002at2759; -.
DR PhylomeDB; Q9LVC8; -.
DR BioCyc; ARA:AT5G57300-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q9LVC8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVC8; baseline and differential.
DR Genevisible; Q9LVC8; AT.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0043429; F:2-nonaprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01183; UBIE_1; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT CHAIN 28..288
FT /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT mitochondrial"
FT /id="PRO_0000375863"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 160..161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
SQ SEQUENCE 288 AA; 32290 MW; EBC5D9ECDA542767 CRC64;
MALRSVSRRL GSRILNQRSF VASLHSHATS FGFQEVKEEE KSKLVGNVFT NVASSYDIMN
DVMSGGLHRL WKERLVGKLS PFAGMKHLDV AGGTGDVAFR IYDAVYSVKR RALQKVDEAS
LEETQIYVCD INPNMLNVGK QRAAERGLRD NKSLVWVEGD AEALSFDDNS MDGYTIAFGI
RNVTHIEKAL AEAYRVLKRG GRFLCLELSH VEIPVFKNLY DLYSFQVIPN LGELIAGDRE
SYQYLVESVR RFPPQERFAS MIADAGFEKV EYENLVGGVV AIHSAIKL
