Reviewed, UniProtKB/Swiss-Prot A6XMY9 (METK1_TRIMO)

Names and origin

Protein names

Recommended 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:

SAMS1

Organism

Triticum monococcum (Einkorn wheat) (Small spelt)

Taxonomic identifier

4568 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Induction	During compatible and incompatible interactions with Blumeria graminis f. sp. tritici, especially in the infected epidermis. Induced by abiotic stresses such as wounding, cold, drought, and salt. Ref.1
Sequence similarities	Belongs to the AdoMet synthetase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	S-adenosylmethionine synthetase 1		PRO_0000363053
Regions
	Nucleotide binding	121 – 126	6	ATP Potential
	Nucleotide binding	269 – 276	8	ATP Potential
Sites
	Metal binding	19	1	Magnesium By similarity
	Metal binding	45	1	Potassium By similarity
	Metal binding	273	1	Potassium By similarity
	Metal binding	281	1	Magnesium By similarity
	Binding site	149	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	A6XMY9-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 4D644A98DF53C29A	FASTA	394	42,818
	10 20 30 40 50 60 MAAETFLFTS ESVNEGHPDK LCDQVSDAVL DACLAQDADS KVACETCTKT NMVMVFGEIT 70 80 90 100 110 120 TKATVDYEKI VRDTCRNIGF ISDDVGLDAD RCKVLVNIEQ QSPDIAQGVH GHFTKRPEDI 130 140 150 160 170 180 GAGDQGIMFG YATDETPELM PLSHVLATKL GARLTEVRKN GTCAWLRPDG KTQVTVEYLN 190 200 210 220 230 240 EGGAMVPVRV HTVLISTQHD ETVTNDEIAA DLKEHVIKPV IPEKYLDEKT IFHLNPSGRF 250 260 270 280 290 300 VIGGPHGDAG LTGRKIIIDT YGGWGAHGGG AFSGKDPTKV DRSGAYIARQ AAKSIIASGL 310 320 330 340 350 360 ARRCIVQISY AIGVPEPLSV FVDSYGTGKI PDKEILKIVK ENFDFRPGMI SINLDLKKGG 370 380 390 NRFIKTAAYG HFGREDADFT WEVVKPLKFD KASA

References

[1]

"Transcriptional regulation of genes involved in the pathways of biosynthesis and supply of methyl units in response to powdery mildew attack and abiotic stresses in wheat." Bhuiyan N.H., Liu W., Liu G., Selvaraj G., Wei Y., King J. Plant Mol. Biol. 64:305-318(2007) [PubMed: 17406792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Tissue: Epidermis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ862831 mRNA. Translation: ABJ15731.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR002133. S-AdoMet_synthetase. [Graphical view]
PANTHER	PTHR11964. S-AdoMet_synt. 1 hit.
Pfam	PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view]
PIRSF	PIRSF000497. MAT. 1 hit.
TIGRFAMs	TIGR01034. metK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHETASE_1. 1 hit. PS00377. ADOMET_SYNTHETASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK1_TRIMO

Accession

Primary (citable) accession number: A6XMY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	August 21, 2007
Last modified:	October 13, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)