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Reviewed, UniProtKB/Swiss-Prot P50299 (METK1_HORVU)

Last modified October 13, 2009. Version 61. 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
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length394 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.

Sequence similarities

Belongs to the AdoMet synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394S-adenosylmethionine synthetase 1
PRO_0000174463

Regions

Nucleotide binding121 – 1266ATP Potential
Nucleotide binding269 – 2768ATP Potential

Sites

Metal binding191Magnesium By similarity
Metal binding451Potassium By similarity
Metal binding2731Potassium By similarity
Metal binding2811Magnesium By similarity
Binding site1491ATP Potential

Experimental info

Sequence conflict2531A → G in CAJ01702. Ref.1
Sequence conflict3511T → S in CAJ01702. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50299-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2ED786F333530013

FASTA39442,842
        10         20         30         40         50         60 
MAAETFLFTS ESVNEGHPDK LCDQVSDAVL DACLAQDPDS KVACETCTKT NMVMVFGEIT 

        70         80         90        100        110        120 
TKATVDYEKI VRDTCRDIGF ISDDVGLDAD HCKVLVNIEQ QSPDIAQGVH GHFTKRPEEV 

       130        140        150        160        170        180 
GAGDQGIMFG YATDETPELM PLTHMLATKL GARLTEVRKN GTCAWLRPDG KTQVTIEYLN 

       190        200        210        220        230        240 
EGGAMVPVRV HTVLISTQHD ETVTNDEIAA DLKEHVIKPV IPGKYLDENT IFHLNPSGRF 

       250        260        270        280        290        300 
VIGGPHGDAG LTARKIIIDT YGGWGAHGGG AFSGKDPTKV DRSGAYIARQ AAKSIIASGL 

       310        320        330        340        350        360 
ARRCIVQISY AIGVPEPLSV FVDSYGTGKI PDREILKLVK ENFDFRPGMI TINLDLKKGG 

       370        380        390 
NRFIKTAAYG HFGRDDADFT WEVVKPLKFD KASA 

« Hide

References

[1]"The methylation cycle and its possible functions in barley endosperm development."
Radchuk V.V., Sreenivasulu N., Radchuk R.I., Wobus U., Weschke W.
Plant Mol. Biol. 59:289-307(2005) [PubMed: 16247558] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Barke.
Tissue: Seed.
[2]Mori S., Takizawa R.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Mori S., Takizawa R., Nakanishi H.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 285-322.
Tissue: Root and Seedling.

Cross-references

Sequence databases

AM039893 mRNA. Translation: CAJ01702.1.
D63835 mRNA. Translation: BAA09895.1.
D49655 mRNA. Translation: BAA08531.1.
PIRT06180.
UniGeneHv.26214

3D structure databases

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

Organism-specific databases

GrameneP50299.

Enzyme and pathway databases

BRENDA2.5.1.6. 283.

Gene expression databases

GenevestigatorP50299.

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_HORVU
AccessionPrimary (citable) accession number: P50299
Secondary accession number(s): Q4LB24
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 13, 2009
This is version 61 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