BQMT_ARATH
ID BQMT_ARATH Reviewed; 338 AA.
AC Q9LY74; Q1EC48; Q8LDQ3; Q94IE2;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-methyl-6-phytyl-1,4-hydroquinone methyltransferase, chloroplastic;
DE EC=2.1.1.295;
DE AltName: Full=37 kDa inner envelope membrane protein;
DE Short=E37;
DE AltName: Full=MPBQ/MSBQ methyltransferase;
DE AltName: Full=Protein ALBINO OR PALE GREEN MUTANT 1;
DE AltName: Full=Protein INNER ENVELOPE PROTEIN 37;
DE AltName: Full=Protein VITAMIN E DEFECTIVE 3;
DE Flags: Precursor;
GN Name=VTE3; Synonyms=APG1, IE37; OrderedLocusNames=At3g63410;
GN ORFNames=MAA21.40;
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. Columbia;
RX PubMed=12787252; DOI=10.1046/j.1365-313x.2003.01763.x;
RA Motohashi R., Ito T., Kobayashi M., Taji T., Nagata N., Asami T.,
RA Yoshida S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Functional analysis of the 37 kDa inner envelope membrane polypeptide in
RT chloroplast biogenesis using a Ds-tagged Arabidopsis pale-green mutant.";
RL Plant J. 34:719-731(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-94, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14508009; DOI=10.1105/tpc.013656;
RA Cheng Z., Sattler S., Maeda H., Sakuragi Y., Bryant D.A., DellaPenna D.;
RT "Highly divergent methyltransferases catalyze a conserved reaction in
RT tocopherol and plastoquinone synthesis in cyanobacteria and photosynthetic
RT eukaryotes.";
RL Plant Cell 15:2343-2356(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=20194502; DOI=10.1074/jbc.m110.109744;
RA Viana A.A., Li M., Schnell D.J.;
RT "Determinants for stop-transfer and post-import pathways for protein
RT targeting to the chloroplast inner envelope membrane.";
RL J. Biol. Chem. 285:12948-12960(2010).
CC -!- FUNCTION: Involved in a key methylation step in both tocopherols
CC (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-
CC methyl-6-phytyl-1,4-hydroquinone (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-
CC hydroquinone (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-
CC 6-solanyl-1,4-benzoquinone (MSBQ) to plastoquinone.
CC {ECO:0000269|PubMed:14508009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-6-phytyl-1,4-benzene-1,4-diol + S-adenosyl-L-
CC methionine = 2,3-dimethyl-6-phytylbenzene-1,4-diol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:37979, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:75920,
CC ChEBI:CHEBI:75921; EC=2.1.1.295;
CC Evidence={ECO:0000269|PubMed:14508009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + S-adenosyl-
CC L-methionine = H(+) + plastoquinol-9 + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:37999, ChEBI:CHEBI:15378, ChEBI:CHEBI:28026,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:75402;
CC EC=2.1.1.295; Evidence={ECO:0000269|PubMed:14508009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-geranylgeranyl-2-methylbenzene-1,4-diol + S-adenosyl-L-
CC methionine = 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38007, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:75411,
CC ChEBI:CHEBI:75412; EC=2.1.1.295;
CC Evidence={ECO:0000269|PubMed:14508009};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:20194502}; Single-pass membrane protein
CC {ECO:0000269|PubMed:20194502}. Note=The transmembrane domain is
CC sufficient to direct stop-transfer insertion and topology in the inner
CC envelope membrane. {ECO:0000269|PubMed:20194502}.
CC -!- DISRUPTION PHENOTYPE: Pale green seedlings that are lethal when grown
CC on normal conditions. {ECO:0000269|PubMed:14508009}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MPBQ/MBSQ MT family. {ECO:0000255|PROSITE-
CC ProRule:PRU01069}.
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DR EMBL; AB054257; BAB62076.1; -; mRNA.
DR EMBL; AL163818; CAB87794.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80478.1; -; Genomic_DNA.
DR EMBL; AK316671; BAH19400.1; -; mRNA.
DR EMBL; BT025886; ABF85788.1; -; mRNA.
DR EMBL; AY085864; AAM63077.1; -; mRNA.
DR PIR; T49182; T49182.
DR RefSeq; NP_191900.1; NM_116206.3.
DR AlphaFoldDB; Q9LY74; -.
DR BioGRID; 10830; 3.
DR STRING; 3702.AT3G63410.1; -.
DR SwissLipids; SLP:000001493; -.
DR iPTMnet; Q9LY74; -.
DR PaxDb; Q9LY74; -.
DR PRIDE; Q9LY74; -.
DR ProteomicsDB; 240675; -.
DR EnsemblPlants; AT3G63410.1; AT3G63410.1; AT3G63410.
DR GeneID; 825516; -.
DR Gramene; AT3G63410.1; AT3G63410.1; AT3G63410.
DR KEGG; ath:AT3G63410; -.
DR Araport; AT3G63410; -.
DR TAIR; locus:2087393; AT3G63410.
DR eggNOG; KOG1540; Eukaryota.
DR HOGENOM; CLU_051421_0_0_1; -.
DR InParanoid; Q9LY74; -.
DR OMA; MAATYFV; -.
DR OrthoDB; 1178802at2759; -.
DR PhylomeDB; Q9LY74; -.
DR BRENDA; 2.1.1.295; 399.
DR UniPathway; UPA00160; -.
DR PRO; PR:Q9LY74; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY74; baseline and differential.
DR Genevisible; Q9LY74; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0102550; F:2-methyl-6-geranylgeranyl-1,4-benzoquinol methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051741; F:2-methyl-6-phytyl-1,4-benzoquinone methyltransferase activity; IDA:TAIR.
DR GO; GO:0051742; F:2-methyl-6-solanyl-1,4-benzoquinone methyltransferase activity; IEA:RHEA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0010236; P:plastoquinone biosynthetic process; IMP:TAIR.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR044649; MPBQ/MSBQ_MT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR031164; SAM_MPBQ_MSBQ_MT.
DR PANTHER; PTHR44516; PTHR44516; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51734; SAM_MPBQ_MSBQ_MT; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Methyltransferase; Plastid; Plastid inner membrane;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..338
FT /note="2-methyl-6-phytyl-1,4-hydroquinone
FT methyltransferase, chloroplastic"
FT /id="PRO_0000422876"
FT TOPO_DOM 52..307
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..338
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 114..123
FT /note="SAM motif I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01069"
FT REGION 159..172
FT /note="SAM motif II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01069"
FT REGION 200..213
FT /note="SAM motif III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01069"
FT MUTAGEN 94
FT /note="T->I: In vte3-1; Slight reduction in plant growth."
FT /evidence="ECO:0000269|PubMed:14508009"
FT CONFLICT 20
FT /note="G -> V (in Ref. 5; ABF85788)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="R -> K (in Ref. 1; BAB62076)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="R -> K (in Ref. 1; BAB62076)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="C -> Y (in Ref. 6; AAM63077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37927 MW; F00258037464FC3D CRC64;
MASLMLNGAI TFPKGLGSPG SNLHARSIPR PTLLSVTRTS TPRLSVATRC SSSSVSSSRP
SAQPRFIQHK KEAYWFYRFL SIVYDHVINP GHWTEDMRDD ALEPADLSHP DMRVVDVGGG
TGFTTLGIVK TVKAKNVTIL DQSPHQLAKA KQKEPLKECK IVEGDAEDLP FPTDYADRYV
SAGSIEYWPD PQRGIREAYR VLKIGGKACL IGPVYPTFWL SRFFSDVWML FPKEEEYIEW
FKNAGFKDVQ LKRIGPKWYR GVRRHGLIMG CSVTGVKPAS GDSPLQLGPK EEDVEKPVNN
PFSFLGRFLL GTLAAAWFVL IPIYMWIKDQ IVPKDQPI
