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Reviewed, UniProtKB/Swiss-Prot Q9MBC2 (MMT1_HORVU)

Last modified June 16, 2009. Version 40. 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
    Hv-MMT1
Gene names
Name: MMT1
Synonyms: MMT
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

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.

Catalytic activity

S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine. Ref.2

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in the shoot, scutellum, and aleurone cells but not in the root or endosperm. Ref.2

Developmental stage

Increases during germination.

Sequence similarities

Belongs to the methyltransferase superfamily.

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_0000204461

Sequences

Sequence LengthMass (Da)Tools
Q9MBC2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F1CB112F456C050B

FASTA1,088119,881
        10         20         30         40         50         60 
MAAAAGDVEA FLAACQASGD AAYGAAKAVL ERLEAPATRA EARRLLGAVR RRFAAGGPAA 

        70         80         90        100        110        120 
GLECFRTFHF RIHDVVLDPH LQGFQQRKKL TMMEIPSIFI PEDWSFTFYE GLNRHPDSIF 

       130        140        150        160        170        180 
RDKTVAELGC GNGWISIALA EKWCPSKVYG LDINPRPIKI AWINLYLNAL DDDGLPIYDA 

       190        200        210        220        230        240 
EGKTLLDRVE FYESDLLSYC RDNKIELDRI VGCIPQILNP NPEAMSKIVT ENSSEEFLYS 

       250        260        270        280        290        300 
LSNYCALQGF VEDQFGLGLI ARAVEEGISV IKPSGLMVFN MGGRPGQGVC ERLFLRRGFR 

       310        320        330        340        350        360 
INKLWQTKIM QAADTDISAL VEIEKNSRHR FEFFMDLVGD QPVCARTAWA YMKSGGRISH 

       370        380        390        400        410        420 
ALSVYSCQLR QPNQVKKIFE FLKDGFHEVS SSLDLSFDDD SVADEKIPFL AYLASFLQEN 

       430        440        450        460        470        480 
KSNPCEPPAG CLNFRNLVAG FMKSYHHIPL TPDNVVVFPS RAVAIENALR LFSPGLAIVD 

       490        500        510        520        530        540 
EHLTRHLPKQ WLTSLAIEES NHAKDTVTVI EAPRQSDLLI ELIRKLKPQV VVTGMAQFEA 

       550        560        570        580        590        600 
ITSAAFVNLL SVTKDVGSRL LLDISEHLEL SSLPSSNGVL KYLAGKTLPS HAAILCGLVK 

       610        620        630        640        650        660 
NQVYSDLEVA FAISEDPTVY KALSQTIELL EGHTSVISQH YYGCLFHELL AFQIGDRHPQ 

       670        680        690        700        710        720 
QEREPAEVIS KEMIGFSSSA MSTLEGAEFF VPGSMESGVI HMDLDRSFLP VPSAVNASIF 

       730        740        750        760        770        780 
ESFVRQNITD SETDVRSSIQ QLVKDSYGFS AGGASEIIYG NTCLALFNKL VLCCMQEQGT 

       790        800        810        820        830        840 
LLFPLGTNGH YVNAAKFVNA TTLTIPTKAD SGFKIEPSAL ADTLEKVSQP WVYISGPTIN 

       850        860        870        880        890        900 
PTGFLYSDDD IAELLSVCAT YGARVVIDTS SSGLEFQATG CSQWNLERCL SNVKSSKPSF 

       910        920        930        940        950        960 
SVVLLGELSF ELTTAGLDFG FLIMSDSSLV DTFYSFPSLS RPHSTLKYTF RKLLGLKNQK 

       970        980        990       1000       1010       1020 
DQHFSDLILE QKETLKNRAD QLIKMLESCG WDAVGCHGGI SMLAKPTAYI GKSLKVDGFE 

      1030       1040       1050       1060       1070       1080 
GKLDSHNMRE ALLRSTGLCI SSSGWTGVPD YCRFSFALES GDFDRAMECI ARFRELVLGG 


GAKVNGSN 

« Hide

References

[1]"Cloning and expression studies of S-adenosyl-L-methionine:L-methionine S-methyltransferase (MMT) in germinating barley."
Pimenta M., Kaneta T., Kamiya Y.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Haruna Nijo.
[2]"S-adenosyl-L-methionine:L-methionine S-methyltransferase from germinating barley. Purification and localization."
Pimenta M.J., Kaneta T., Larondelle Y., Dohmae N., Kamiya Y.
Plant Physiol. 118:431-438(1998) [PubMed: 9765528] [Abstract]
Cited for: PROTEIN SEQUENCE OF 159-183, ENZYME ACTIVITY, TISSUE SPECIFICITY.

Cross-references

Sequence databases

AB028870 mRNA. Translation: BAA94795.1.

3D structure databases

ModBaseSearch...

Organism-specific databases

GrameneQ9MBC2.

Enzyme and pathway databases

BRENDA2.1.1.12. 283.

Family and domain databases

InterProIPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR007848. Small_mtfrase.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PfamPF05175. MTS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMT1_HORVU
AccessionPrimary (citable) accession number: Q9MBC2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 40 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