GTOMC_ARATH
ID GTOMC_ARATH Reviewed; 348 AA.
AC Q9ZSK1; Q9XIP9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Tocopherol O-methyltransferase, chloroplastic;
DE EC=2.1.1.95 {ECO:0000269|PubMed:9851934};
DE AltName: Full=Gamma-tocopherol methyltransferase;
DE AltName: Full=Vitamin E pathway gene 4 protein;
DE Short=AtVTE4;
DE Flags: Precursor;
GN Name=VTE4; Synonyms=G-TMT; OrderedLocusNames=At1g64970; ORFNames=F13O11.27;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9851934; DOI=10.1126/science.282.5396.2098;
RA Shintani D., DellaPenna D.;
RT "Elevating the vitamin E content of plants through metabolic engineering.";
RL Science 282:2098-2100(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14682617; DOI=10.1023/b:plan.0000004307.62398.91;
RA Bergmueller E., Porfirova S., Doermann P.;
RT "Characterization of an Arabidopsis mutant deficient in gamma-tocopherol
RT methyltransferase.";
RL Plant Mol. Biol. 52:1181-1190(2003).
RN [7]
RP FUNCTION.
RX PubMed=12586887; DOI=10.1104/pp.015222;
RA Collakova E., DellaPenna D.;
RT "Homogentisate phytyltransferase activity is limiting for tocopherol
RT biosynthesis in Arabidopsis.";
RL Plant Physiol. 131:632-642(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-52, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the synthesis of tocopherol (vitamin E).
CC Methylates gamma- and delta-tocopherol to form beta- and alpha-
CC tocopherol, respectively. {ECO:0000269|PubMed:12586887,
CC ECO:0000269|PubMed:14682617, ECO:0000269|PubMed:9851934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-tocopherol + S-adenosyl-L-methionine = (+)-alpha-
CC tocopherol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:24012,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18145, ChEBI:CHEBI:18185,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.95;
CC Evidence={ECO:0000269|PubMed:9851934};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delta-tocotrienol + S-adenosyl-L-methionine = beta-tocotrienol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38091,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33275, ChEBI:CHEBI:33276,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.95;
CC Evidence={ECO:0000269|PubMed:9851934};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-tocotrienol + S-adenosyl-L-methionine = alpha-
CC tocotrienol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38095,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33270, ChEBI:CHEBI:33277,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.95;
CC Evidence={ECO:0000269|PubMed:9851934};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delta-tocopherol + S-adenosyl-L-methionine = beta-tocopherol +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:37991,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47771, ChEBI:CHEBI:47772,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.95;
CC Evidence={ECO:0000269|PubMed:9851934};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction of fresh weight in mature
CC plants. Leaves with high levels of gamma-tocopherol and absence of
CC alpha-tocopherol. {ECO:0000269|PubMed:14682617}.
CC -!- MISCELLANEOUS: Seeds overexpressing VTE4 show increased levels of
CC alpha-tocopherol.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. gTMT family. {ECO:0000255|PROSITE-ProRule:PRU00914}.
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DR EMBL; AF104220; AAD02882.1; -; mRNA.
DR EMBL; AC006193; AAD38271.2; -; Genomic_DNA.
DR EMBL; CP002684; AEE34310.1; -; Genomic_DNA.
DR EMBL; AY049258; AAK83600.1; -; mRNA.
DR EMBL; AY090280; AAL90941.1; -; mRNA.
DR EMBL; AY087138; AAM64696.1; -; mRNA.
DR PIR; C96673; C96673.
DR RefSeq; NP_176677.1; NM_105171.3.
DR AlphaFoldDB; Q9ZSK1; -.
DR SMR; Q9ZSK1; -.
DR STRING; 3702.AT1G64970.1; -.
DR SwissLipids; SLP:000001490; -.
DR iPTMnet; Q9ZSK1; -.
DR PaxDb; Q9ZSK1; -.
DR PRIDE; Q9ZSK1; -.
DR ProteomicsDB; 248499; -.
DR EnsemblPlants; AT1G64970.1; AT1G64970.1; AT1G64970.
DR GeneID; 842805; -.
DR Gramene; AT1G64970.1; AT1G64970.1; AT1G64970.
DR KEGG; ath:AT1G64970; -.
DR Araport; AT1G64970; -.
DR TAIR; locus:2010921; AT1G64970.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_039068_0_0_1; -.
DR InParanoid; Q9ZSK1; -.
DR OMA; YCLPYVI; -.
DR OrthoDB; 785883at2759; -.
DR PhylomeDB; Q9ZSK1; -.
DR BioCyc; ARA:AT1G64970-MON; -.
DR BRENDA; 2.1.1.95; 399.
DR UniPathway; UPA00160; -.
DR PRO; PR:Q9ZSK1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZSK1; baseline and differential.
DR Genevisible; Q9ZSK1; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0050342; F:tocopherol O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR025774; MTs_g-TMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51581; SAM_GTMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Methyltransferase; Plastid; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 52..348
FT /note="Tocopherol O-methyltransferase, chloroplastic"
FT /id="PRO_0000018677"
FT REGION 130..139
FT /note="SAM motif I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00914"
FT REGION 193..201
FT /note="SAM motif II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00914"
FT REGION 220..229
FT /note="SAM motif III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00914"
FT MOD_RES 52
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 175
FT /note="A -> S (in Ref. 1; AAD02882 and 5; AAM64696)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="Q -> K (in Ref. 5; AAM64696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38075 MW; E9290758C2E83B73 CRC64;
MKATLAAPSS LTSLPYRTNS SFGSKSSLLF RSPSSSSSVS MTTTRGNVAV AAAATSTEAL
RKGIAEFYNE TSGLWEEIWG DHMHHGFYDP DSSVQLSDSG HKEAQIRMIE ESLRFAGVTD
EEEEKKIKKV VDVGCGIGGS SRYLASKFGA ECIGITLSPV QAKRANDLAA AQSLAHKASF
QVADALDQPF EDGKFDLVWS MESGEHMPDK AKFVKELVRV AAPGGRIIIV TWCHRNLSAG
EEALQPWEQN ILDKICKTFY LPAWCSTDDY VNLLQSHSLQ DIKCADWSEN VAPFWPAVIR
TALTWKGLVS LLRSGMKSIK GALTMPLMIE GYKKGVIKFG IITCQKPL
