Reviewed, UniProtKB/Swiss-Prot P49612 (METK1_PEA)

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

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	366 AA.
Sequence status	Fragment.
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.
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 – 366	›366	S-adenosylmethionine synthetase 1		PRO_0000174472
Regions
	Nucleotide binding	94 – 99	6	ATP Potential
	Nucleotide binding	242 – 249	8	ATP Potential
Sites
	Metal binding	18	1	Potassium By similarity
	Metal binding	246	1	Potassium By similarity
	Metal binding	254	1	Magnesium By similarity
	Binding site	122	1	ATP Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P49612-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: EDB446F65D407627	FASTA	366	39,940
	10 20 30 40 50 60 VAVDACLEQD SDSKVACETC TKTNLVMVFG EITTKANVDY EKIVRNTCRN IGFVSADVGL 70 80 90 100 110 120 DADNCKVLVN IEQQSPDIAQ GVHGHFTKKP EEIGAGDQGH MFGYATDETP ELMPLSHVLA 130 140 150 160 170 180 TKLGARLTEV RKNGTCAWLR PDGNTQVTVE YYNDKGAMVP IRVHTVLIST QHDETVTNDE 190 200 210 220 230 240 IAADLKEHVI KPVIPEKYLD SKTICHLNPS GRFVIGGPHG DAGLTGRKII IDTYGGWGAH 250 260 270 280 290 300 GGGAFSGKDP TKVDRRGAYI VRQAAKSIVA SGLARRAIVQ LLRAIGVPEP LSVFVDTYGT 310 320 330 340 350 360 GKIPDREILK IVKETFDFRP GMISINLDLL RGGNGRFLKT AAYGHFGRED PDFTWEVVKP LKWEKA

References

[1]	"Hormonal regulation of S-adenosylmethionine synthase transcripts in pea ovaries." Gomez-Gomez L., Carrasco P. Plant Mol. Biol. 30:821-832(1996) [PubMed: 8624412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Alaska. Tissue: Ovary.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X82076 mRNA. Translation: CAA57580.1. L36680 mRNA. Translation: AAA58772.1. Sequence problems.
PIR	S66351. T06592.
3D structure databases
HSSP	HSSP built from PDB template 1QM4 based on UniProtKB P13444.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.5.1.6. 287.
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_PEA

Accession

Primary (citable) accession number: P49612

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 22, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)