P49613 (METK2_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase 2
Short name=AdoMet synthase 2
EC=2.5.1.6

Alternative name(s):
Methionine adenosyltransferase 2
Short name=MAT 2

Gene names

Name:

SAMS2

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
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.
Tissue specificity	Expressed in vegetative and reproductive tissues. Ref.1
Induction	Up regulated by auxin. Ref.1
Sequence similarities	Belongs to the AdoMet synthase 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	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: InterPro 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 374	374	S-adenosylmethionine synthase 2		PRO_0000174473
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)
	P49613 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 9D921A5AE7420882	FASTA	374	40,976
	10 20 30 40 50 60 MATETFLFTS ESVNEGHPDK LCDQISDAVL DACLEQDPES KVACETCTKT NMVMVFGEIT 70 80 90 100 110 120 TKANVDYEKI VRDTCRNIGF VSDDVGLDAD NCKVLVNIEQ QSPDIAQGVH GHLTKRPEDI 130 140 150 160 170 180 GAGDQGHMFG YATDETPEFM PLSHVLATKL GASLTEVRKN GTCPWLRPDG KTQVTVEYYN 190 200 210 220 230 240 DKGAMVPIRV HTVLISTQHD ETVTNDEIAA DLKEHVIKPV IPEKYLDEKT IFHLNPSGRF 250 260 270 280 290 300 RHGGPHGDAG LTGRKIIIDT YGGWGAHGGG AFSGKDPTKV DRSGAYIVRE AAKSIVANGL 310 320 330 340 350 360 ARRCLVQVSY AIGVPEPLSV FVDSYGTGKI PDREILNIVK EAFDFRPGMI SISLDLLRGG 370 NGRFFEDSCI WTFW

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], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Alaska. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82077 mRNA. Translation: CAA57581.1. L36681 mRNA. Translation: AAA58773.1.
PIR	S66352.
3D structure databases
ProteinModelPortal	P49613.
SMR	P49613. Positions 5-371.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR022631. ADOMET_SYNTHASE_CS. IPR022630. S-AdoMet_synt_C. IPR022629. S-AdoMet_synt_central. IPR022628. S-AdoMet_synt_N. IPR002133. S-AdoMet_synthetase. IPR022636. S-AdoMet_synthetase_sfam. [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.
SUPFAM	SSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMs	TIGR01034. MetK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK2_PEA

Accession

Primary (citable) accession number: P49613

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 28, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program