P43281 (METK2_SOLLC) 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:

SAM2

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	393 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	Mostly expressed in roots. Also present in stems and leaves. Ref.1
Induction	Repressed in roots by ABA and mannitol. 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 – 393	393	S-adenosylmethionine synthase 2		PRO_0000174465
Regions
	Nucleotide binding	119 – 124	6	ATP Potential
	Nucleotide binding	267 – 274	8	ATP Potential
Sites
	Metal binding	17	1	Magnesium By similarity
	Metal binding	43	1	Potassium By similarity
	Metal binding	271	1	Potassium By similarity
	Metal binding	279	1	Magnesium By similarity
	Binding site	147	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	P43281 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4E77D0D1B21BFD79	FASTA	393	43,082
	10 20 30 40 50 60 METFLFTSES VNEGHPDKLC DQVSDAVLDA CLAQDPESKV ACETCTKTNL VMVFGEITTK 70 80 90 100 110 120 ANIDYEKIVR DTCREIGFVS PDVGLDADNC RVLVNIEQQS PDIAQGVHGH LTKRPEEIGA 130 140 150 160 170 180 GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CSWLRPDGKT QVTVEYHNDN 190 200 210 220 230 240 GAMVPLRVHT VLISTQHDET VTNDEIARDL KEHVIKPVIP EKYLDENTIF HLNPSGRFVI 250 260 270 280 290 300 GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVANGLAR 310 320 330 340 350 360 RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILNIVKEN FDFRPGMISI NLDLLRGGNG 370 380 390 RFLKTAAYGH FGRDDPDFTW EVVKPLKWDK PEA

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 [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Rutgers. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z24742 Genomic DNA. Translation: CAA80866.1.
PIR	S38875. S46539.
3D structure databases
ProteinModelPortal	P43281.
SMR	P43281. Positions 3-388.
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_SOLLC

Accession

Primary (citable) accession number: P43281

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 28, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program