Q9SWR3 (MMT1_WOLBI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine S-methyltransferase
EC=2.1.1.12

Alternative name(s):
AdoMet:Met S-methyltransferase

Gene names

Name:	MMT1
Synonyms:	MMT

Organism

Wollastonia biflora (Beach sunflower) (Wedelia biflora)

Taxonomic identifier

101473 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Heliantheae alliance › Heliantheae › Wedelia

Protein attributes

Sequence length	1088 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the S-methylmethionine (SMM) biosynthesis from adenosyl-L-homocysteine (AdoMet) and methionine. SMM biosynthesis (by MMT1) and degradation (by HMT-1, HMT-2 and HMT-3) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level. Also able to catalyze the selenium-methylmethionine (SeMM) from AdoMet and selenium-methionine (SeMet). May play a role in phoem sulfur transport; such function is however not essential. Ref.1
Catalytic activity	S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine. Ref.2
Subunit structure	Homotetramer. Ref.2
Subcellular location	Cytoplasm Ref.3.
Sequence similarities	Belongs to the methyltransferase superfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 7.2. Ref.2

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	methionine S-methyltransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1088	1088	Methionine S-methyltransferase		PRO_0000204463

Sequences

	Sequence		Length	Mass (Da)
	Q9SWR3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 594CC75C1C4FB616	FASTA	1,088	121,565
	10 20 30 40 50 60 MAAVTGLYGS IDEFLNHCSQ SGDSAYSALR SLLERLEKPD TRTEARIFLA HLQKKLDNDG 70 80 90 100 110 120 ASQRCLETYH FQIQDIYLDR NEGTGYQNRK KFTMMVIPSI FMPEDWSFTF YEGINRHPDS 130 140 150 160 170 180 IFKDKTVAEL GCGNGWISIA IAEKWLPLKV YGLDINPRAV KISWINLYLN AFDEDGQPVY 190 200 210 220 230 240 DSESKTLLDR VEFYESDLLS YCRDNHIELE RIVGCIPQIL NPNPDAMSKL VTENASEEFL 250 260 270 280 290 300 HSLSNYCALQ GFVEDQFGLG LIARAVEEGI DVIKPMGIMI FNMGGRPGQG VCKRLFERRG 310 320 330 340 350 360 LSVNKLWQTK ILQASDTDIS ALVEIEKNNP HRFEFFMGLV GDRPICARTA WAFGKACGRI 370 380 390 400 410 420 SHALSVYSCQ LRHPNEVKKI FEFLKNGFHD ISNSLDLSFE DDSVADEKIP FLAYLAGVLK 430 440 450 460 470 480 DGSRFPYEPP TGNKRFRDLI ASFMKTYHHV PLSTDNVAIF PSRATAIENS LRLFTPRLAI 490 500 510 520 530 540 VEEHLTCNLP RQWLTSLEIE QTRDSKTPID GITVIEAPRQ SDLMIELIKK LKPQVVVTGI 550 560 570 580 590 600 AQFEAVTSSA FEHLLRVTRE IGSRLFIDIS DQFELSSLPS SIGVLKYLAR TPLPSHAAII 610 620 630 640 650 660 CGLLRNRVYT DLEVAFVISE EQTIFDALTR TVELLQGNTA LISQYYYGCL FHELLSFQIP 670 680 690 700 710 720 DRRQTAEREA ENVEASDIDM IGFSSSAISV LSQSELSVRV TEKSSLLHMD VDQIFLPTPT 730 740 750 760 770 780 PVKAAIFESF ARQNVTETEC DVTPILRQFI LNTWNFSVEH SAEFIYADFP LALFNKLVLC 790 800 810 820 830 840 CIEEGGSLCM PAGSNGNYAA AAKFLNANIM SIPTEAEVGF KLTAKQLSSV LETVHKPWVY 850 860 870 880 890 900 ISGPTINPTG LLYSNEEMKS LLTVCARYGA RTIIDTSFSG IKFNSQDWDG WNLDASLAGL 910 920 930 940 950 960 TGNPSFSVCL LGGLFFKIPT GGLSYGFLVL KSGFLADSFR SSFSGLNKPH NTVRYTAKKL 970 980 990 1000 1010 1020 LELGEQKGNL TGAAQGQEKL LATRLKRLKE TLENCGWEVI EARGGVSVIA KPSAYLGKNI 1030 1040 1050 1060 1070 1080 KLEKDGSTWV TKLDGTNIRE AMLRATGLCI NGPSWTGIPD YCRFTFALED GDFDRALDCI VKFNQLVK

References

[1]	"S-methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase." Bourgis F., Roje S., Nuccio M.L., Fisher D.B., Tarczynski M.C., Li C., Herschbach C., Rennenberg H., Pimenta M.J., Shen T.-L., Gage D.A., Hanson A.D. Plant Cell 11:1485-1498(1999) [PubMed: 10449582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-80; 162-196; 300-305; 380-385; 421-445; 450-462; 531-555; 704-712; 804-821; 823-825 AND 932-948, FUNCTION. Tissue: Leaf.
[2]	"Purification and properties of S-adenosyl-L-methionine:L-methionine S-methyltransferase from Wollastonia biflora leaves." James F., Nolte K.D., Hanson A.D. J. Biol. Chem. 270:22344-22350(1995) [PubMed: 7673218] [Abstract] Cited for: ENZYME ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Evidence that the pathway of dimethylsulfoniopropionate biosynthesis begins in the cytosol and ends in the chloroplast." Trossat C., Nolte K.D., Hanson A.D. Plant Physiol. 111:965-973(1996) [PubMed: 12226341] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF137023 mRNA. Translation: AAD49573.1.
3D structure databases
ProteinModelPortal	Q9SWR3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14235.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 2 hits. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MMT1_WOLBI

Accession

Primary (citable) accession number: Q9SWR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program