MMT1_ARATH
ID MMT1_ARATH Reviewed; 1071 AA.
AC Q9LTB2; Q9SWR2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Methionine S-methyltransferase;
DE EC=2.1.1.12;
DE AltName: Full=AdoMet:Met S-methyltransferase;
GN Name=MMT1; Synonyms=MMT; OrderedLocusNames=At5g49810; ORFNames=K21G20.2;
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 ENZYME ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10449582; DOI=10.2307/3870977;
RA Bourgis F., Roje S., Nuccio M.L., Fisher D.B., Tarczynski M.C., Li C.,
RA Herschbach C., Rennenberg H., Pimenta M.J., Shen T.-L., Gage D.A.,
RA Hanson A.D.;
RT "S-methylmethionine plays a major role in phloem sulfur transport and is
RT synthesized by a novel type of methyltransferase.";
RL Plant Cell 11:1485-1498(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION.
RX PubMed=12376649; DOI=10.1104/pp.001693;
RA Tagmount A., Berken A., Terry N.;
RT "An essential role of s-adenosyl-L-methionine:L-methionine s-
RT methyltransferase in selenium volatilization by plants. Methylation of
RT selenomethionine to selenium-methyl-L-selenium-methionine, the precursor of
RT volatile selenium.";
RL Plant Physiol. 130:847-856(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x;
RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., Hanson A.D.;
RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and
RT activity.";
RL Plant J. 25:575-584(2001).
RN [7]
RP PROBABLE FUNCTION OF SMM CYCLE.
RX PubMed=12692340; DOI=10.1104/pp.102.018846;
RA Kocsis M.G., Ranocha P., Gage D.A., Simon E.S., Rhodes D., Peel G.J.,
RA Mellema S., Saito K., Awazuhara M., Li C., Meeley R.B., Tarczynski M.C.,
RA Wagner C., Hanson A.D.;
RT "Insertional inactivation of the methionine s-methyltransferase gene
RT eliminates the s-methylmethionine cycle and increases the methylation
RT ratio.";
RL Plant Physiol. 131:1808-1815(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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Catalyzes the S-methylmethionine (SMM) biosynthesis from
CC adenosyl-L-homocysteine (AdoMet) and methionine. SMM biosynthesis (by
CC MMT1) and degradation (by HMT-1, HMT-2 and HMT-3) constitute the SMM
CC cycle in plants, which is probably required to achieve short term
CC control of AdoMet level. Also able to catalyze the selenium-
CC methylmethionine (SeMM) from AdoMet and selenium-methionine (SeMet).
CC May play a role in phoem sulfur transport; such function is however not
CC essential. {ECO:0000269|PubMed:10449582, ECO:0000269|PubMed:12376649}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine + S-adenosyl-L-methionine = S-adenosyl-L-
CC homocysteine + S-methyl-L-methionine; Xref=Rhea:RHEA:13761,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:58252,
CC ChEBI:CHEBI:59789; EC=2.1.1.12;
CC Evidence={ECO:0000269|PubMed:10449582};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves and cauline
CC leaves. Expressed at a lower level in developing seeds.
CC {ECO:0000269|PubMed:11309147}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; AF137380; AAD49574.1; -; mRNA.
DR EMBL; AB025612; BAA98148.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95858.1; -; Genomic_DNA.
DR EMBL; AY094459; AAM19829.1; -; mRNA.
DR EMBL; BT002664; AAO11580.1; -; mRNA.
DR PIR; T52306; T52306.
DR RefSeq; NP_199792.1; NM_124359.4.
DR AlphaFoldDB; Q9LTB2; -.
DR SMR; Q9LTB2; -.
DR STRING; 3702.AT5G49810.1; -.
DR iPTMnet; Q9LTB2; -.
DR PaxDb; Q9LTB2; -.
DR PRIDE; Q9LTB2; -.
DR ProteomicsDB; 237129; -.
DR EnsemblPlants; AT5G49810.1; AT5G49810.1; AT5G49810.
DR GeneID; 835044; -.
DR Gramene; AT5G49810.1; AT5G49810.1; AT5G49810.
DR KEGG; ath:AT5G49810; -.
DR Araport; AT5G49810; -.
DR TAIR; locus:2155466; AT5G49810.
DR eggNOG; ENOG502QS81; Eukaryota.
DR HOGENOM; CLU_005080_0_0_1; -.
DR InParanoid; Q9LTB2; -.
DR OMA; LGANGHY; -.
DR OrthoDB; 93776at2759; -.
DR PhylomeDB; Q9LTB2; -.
DR BioCyc; ARA:AT5G49810-MON; -.
DR PRO; PR:Q9LTB2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTB2; baseline and differential.
DR Genevisible; Q9LTB2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0030732; F:methionine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IMP:TAIR.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IMP:TAIR.
DR GO; GO:0001887; P:selenium compound metabolic process; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR025779; Met_S-MeTrfase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51555; SAM_MT12; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1071
FT /note="Methionine S-methyltransferase"
FT /id="PRO_0000204460"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 269
FT /note="I -> V (in Ref. 1; AAD49574)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="K -> R (in Ref. 1; AAD49574)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="M -> L (in Ref. 1; AAD49574)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="L -> F (in Ref. 1; AAD49574)"
FT /evidence="ECO:0000305"
FT CONFLICT 968
FT /note="R -> K (in Ref. 1; AAD49574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1071 AA; 118716 MW; 788D12B83CB47958 CRC64;
MADLSSVDEF LNQCKQSGDA AYGALRSVLE RLEDPNTRSK ARIFLSDIYK RVGSSETSLQ
TYHFHIQDIY LDQYEGFQSR KKLTMMVIPS IFIPEDWSFT FYEGLNRHPD TIFKDKTVSE
LGCGNGWISI AIAAKWLPSK VYGLDINPRA VKISWINLYL NALDDNGEPV YDEEKKTLLD
RVEFYESDLL GYCRDNKIQL ERIVGCIPQI LNPNPEAMSK LITENASEEF LHSLSNYCAL
QGFVEDQFGL GLIARAVEEG ISVIKPAGIM IFNMGGRPGQ GVCRRLFERR GVRVTQMWQT
KILQAADTDI SALVEIERSS PHRFEFFMGL SGDQPICART AWAYGKAGGR ISHALSVYSC
QIRQPNLVKI IFDFLKNGFQ EISNSLDLSF EDETVADEKI PFLAYLASVL KNSSYFPFEP
PAGSKRFCSL IAGFMRTYHR IPINQDNIVV FPSRAVAIES AFRLFSPRLA IVDEHLTRQL
PRSWLTSLAI EDTSMDKSDD QITVIESPHQ SDLMIELIKK LKPQVVVTGM APFEVITSSS
FLHLLEVTKE IGCRLFLDIS DHFELSSLPA SNGVLKYLAE NQLPSHAAII CGLVKNKVYS
DLEVAFVITE VDAIAKALSK TVEVLEGHTA IISQYYYGCL FHELLAFQLA DRHAPAERES
EKAKSEEIIG FSSSAVSILK DAELSVTEID ETSLIHMDVD QSFLQIPQSV KAAIFESFVR
QNISEAEVDI NPSIKQFVWS NYGFPTKSST GFVYADGSLA LFNKLVICCA QEGGTLCLPA
GTNGNYVAAA KFLKANVVNI PTESSDGFKL TEKTLTKALE SVKKPWVCIS GPTVSPTGLV
YSNEEMDILL STCAKFGAKV IIDTSFSGLE YSATSWDLKN ALSKMDSSLS VSLLGCLSLN
LLSGAIKLGF LVLDQSLIDA FHTLPGLSKP HSTVKYAAKK MLALKEEKAS DFLDAVSETI
KTLEGRSRRL KEVLQNSGWE VIQPSAGISM VAKPKAYLNK KVKLKAGDGQ EIVELTDSNM
RDVFLSHTGV CLNSGSWTGI PGYCRFSFAL EDSEFDKAIE SIAQFKSVLA N
