MMT1_WEDBI
ID MMT1_WEDBI Reviewed; 1088 AA.
AC Q9SWR3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Methionine S-methyltransferase;
DE EC=2.1.1.12;
DE AltName: Full=AdoMet:Met S-methyltransferase;
GN Name=MMT1; Synonyms=MMT;
OS Wedelia biflora (Beach sunflower) (Wollastonia biflora).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Wollastonia.
OX NCBI_TaxID=101473;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-80; 162-196; 300-305;
RP 380-385; 421-445; 450-462; 531-555; 704-712; 804-821; 823-825 AND 932-948,
RP AND FUNCTION.
RC TISSUE=Leaf;
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 ENZYME ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7673218; DOI=10.1074/jbc.270.38.22344;
RA James F., Nolte K.D., Hanson A.D.;
RT "Purification and properties of S-adenosyl-L-methionine:L-methionine S-
RT methyltransferase from Wollastonia biflora leaves.";
RL J. Biol. Chem. 270:22344-22350(1995).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12226341; DOI=10.1104/pp.111.4.965;
RA Trossat C., Nolte K.D., Hanson A.D.;
RT "Evidence that the pathway of dimethylsulfoniopropionate biosynthesis
RT begins in the cytosol and ends in the chloroplast.";
RL Plant Physiol. 111:965-973(1996).
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}.
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:7673218};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:7673218};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7673218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226341}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF137023; AAD49573.1; -; mRNA.
DR AlphaFoldDB; Q9SWR3; -.
DR SMR; Q9SWR3; -.
DR BioCyc; MetaCyc:MON-14235; -.
DR SABIO-RK; Q9SWR3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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 InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53383; SSF53383; 2.
DR PROSITE; PS51555; SAM_MT12; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1088
FT /note="Methionine S-methyltransferase"
FT /id="PRO_0000204463"
SQ SEQUENCE 1088 AA; 121565 MW; 594CC75C1C4FB616 CRC64;
MAAVTGLYGS IDEFLNHCSQ SGDSAYSALR SLLERLEKPD TRTEARIFLA HLQKKLDNDG
ASQRCLETYH FQIQDIYLDR NEGTGYQNRK KFTMMVIPSI FMPEDWSFTF YEGINRHPDS
IFKDKTVAEL GCGNGWISIA IAEKWLPLKV YGLDINPRAV KISWINLYLN AFDEDGQPVY
DSESKTLLDR VEFYESDLLS YCRDNHIELE RIVGCIPQIL NPNPDAMSKL VTENASEEFL
HSLSNYCALQ GFVEDQFGLG LIARAVEEGI DVIKPMGIMI FNMGGRPGQG VCKRLFERRG
LSVNKLWQTK ILQASDTDIS ALVEIEKNNP HRFEFFMGLV GDRPICARTA WAFGKACGRI
SHALSVYSCQ LRHPNEVKKI FEFLKNGFHD ISNSLDLSFE DDSVADEKIP FLAYLAGVLK
DGSRFPYEPP TGNKRFRDLI ASFMKTYHHV PLSTDNVAIF PSRATAIENS LRLFTPRLAI
VEEHLTCNLP RQWLTSLEIE QTRDSKTPID GITVIEAPRQ SDLMIELIKK LKPQVVVTGI
AQFEAVTSSA FEHLLRVTRE IGSRLFIDIS DQFELSSLPS SIGVLKYLAR TPLPSHAAII
CGLLRNRVYT DLEVAFVISE EQTIFDALTR TVELLQGNTA LISQYYYGCL FHELLSFQIP
DRRQTAEREA ENVEASDIDM IGFSSSAISV LSQSELSVRV TEKSSLLHMD VDQIFLPTPT
PVKAAIFESF ARQNVTETEC DVTPILRQFI LNTWNFSVEH SAEFIYADFP LALFNKLVLC
CIEEGGSLCM PAGSNGNYAA AAKFLNANIM SIPTEAEVGF KLTAKQLSSV LETVHKPWVY
ISGPTINPTG LLYSNEEMKS LLTVCARYGA RTIIDTSFSG IKFNSQDWDG WNLDASLAGL
TGNPSFSVCL LGGLFFKIPT GGLSYGFLVL KSGFLADSFR SSFSGLNKPH NTVRYTAKKL
LELGEQKGNL TGAAQGQEKL LATRLKRLKE TLENCGWEVI EARGGVSVIA KPSAYLGKNI
KLEKDGSTWV TKLDGTNIRE AMLRATGLCI NGPSWTGIPD YCRFTFALED GDFDRALDCI
VKFNQLVK
