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Reviewed, UniProtKB/Swiss-Prot P43280 (METK1_SOLLC)

Last modified September 22, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    S-adenosylmethionine synthetase 1
      Short name=AdoMet synthetase 1
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 1
      Short name=MAT 1
Gene names
Name: SAM1
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme By similarity.

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

Cofactor

Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.

Binds 1 potassium ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Mostly expressed in stems. Ref.1

Induction

By salt stress, ABA, and mannitol in roots and leaves. Ref.1

Sequence similarities

Belongs to the AdoMet synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393S-adenosylmethionine synthetase 1
PRO_0000174464

Regions

Nucleotide binding119 – 1246ATP Potential
Nucleotide binding267 – 2748ATP Potential

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2711Potassium By similarity
Metal binding2791Magnesium By similarity
Binding site1471ATP Potential

Sequences

Sequence LengthMass (Da)Tools
P43280-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 81433A565A68039B

FASTA39343,301
        10         20         30         40         50         60 
METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPESKV ACETCTKTNL VMVFGEITTK 

        70         80         90        100        110        120 
AIVDYEKIVR DTCRNIGFVS DDVGLDADNC KVLVYIEQQS PDIAQGVHGH LTKRPEEIGA 

       130        140        150        160        170        180 
GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CAWLRPDGKT QVTVEYSNDN 

       190        200        210        220        230        240 
GAMVPIRVHT VLISTQHDET VTNDEIARDL KEHVIKPVIP EKYLDENTIF HLNPSGRFVI 

       250        260        270        280        290        300 
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVASGLAR 

       310        320        330        340        350        360 
RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD REILKIVKEN FDFRPGMMSI NLDLKRGGNR 

       370        380        390 
RFLKTAAYGH FGRDDPDFTW EVVKPLKWEK PQD 

« Hide

References

[1]"Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress."
Espartero J., Pintor-Toro J.A., Pardo J.M.
Plant Mol. Biol. 25:217-227(1994) [PubMed: 8018871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Rutgers.
Tissue: Seedling.

Cross-references

Sequence databases

Z24741 mRNA. Translation: CAA80865.1.
PIRS46538.
UniGeneLes.19585

3D structure databases

HSSPHSSP built from PDB template 1QM4 based on UniProtKB P13444.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.6. 281054.

Family and domain databases

InterProIPR002133. S-AdoMet_synthetase.
[Graphical view]
PANTHERPTHR11964. S-AdoMet_synt. 1 hit.
PfamPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000497. MAT. 1 hit.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHETASE_1. 1 hit.
PS00377. ADOMET_SYNTHETASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK1_SOLLC
AccessionPrimary (citable) accession number: P43280
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 22, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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