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Reviewed, UniProtKB/Swiss-Prot Q9SWR3 (MMT1_WOLBI)

Last modified June 16, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Methionine S-methyltransferase
    EC=2.1.1.12
Alternative name(s):
    AdoMet:Met S-methyltransferase
Gene names
Name: MMT1
Synonyms: MMT
OrganismWollastonia biflora (Beach sunflower) (Wedelia biflora)
Taxonomic identifier101473 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheaeWollastonia

Protein attributes

Sequence length1088 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmethionine S-methyltransferase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10881088Methionine S-methyltransferase
PRO_0000204463

Sequences

Sequence LengthMass (Da)Tools
Q9SWR3-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 594CC75C1C4FB616

FASTA1,088121,565
        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 

« Hide

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

AF137023 mRNA. Translation: AAD49573.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.1.1.12. 262380.

Family and domain databases

InterProIPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR007848. Small_mtfrase.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PfamPF05175. MTS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMT1_WOLBI
AccessionPrimary (citable) accession number: Q9SWR3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents