Reviewed, UniProtKB/Swiss-Prot Q6F3F3 (METK2_ATRNU)

Names and origin

Protein names

Recommended name:
    S-adenosylmethionine synthetase 2
      Short name=AdoMet synthetase 2
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 2
      Short name=MAT 2

Gene names

Name:

SAMS2

Organism

Atriplex nummularia (Old man saltbush)

Taxonomic identifier

3553 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Atriplex

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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. May be involved in the synthesis of betain in response to abiotic stress such as high salinity.
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 roots, stems and leaves (at protein level). Ref.1
Induction	By salt stress, in stems and leaves (at protein level). Follow a circadian regulation with higher levels in the light. 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 – 396	396	S-adenosylmethionine synthetase 2		PRO_0000363006
Regions
	Nucleotide binding	123 – 128	6	ATP Potential
	Nucleotide binding	271 – 278	8	ATP Potential
Sites
	Metal binding	21	1	Magnesium By similarity
	Metal binding	47	1	Potassium By similarity
	Metal binding	275	1	Potassium By similarity
	Metal binding	283	1	Magnesium By similarity
	Binding site	151	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6F3F3-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 9DEC1337C8F42940	FASTA	396	43,175
	10 20 30 40 50 60 MAAAVDTFLF TSESVNEGHP DKLCDQISDA VLDACLAQDP ESKVACETCT KTNLVMVFGE 70 80 90 100 110 120 ITTKADVDYE KIVRQTCRDI GFVSADVGLD ADNCKVLVYI EQQSPDIAQG VHGHLSRRPE 130 140 150 160 170 180 EIGAGDQGHM FGYASDETPE LMPLSHVLAT KLGARLTEVR KNGTCPWLRP DGKTQVTVEY 190 200 210 220 230 240 YNENGAMVPI RVHTVLISTQ HDETVTNDEI AADLKEHVIK PVIPEKYLDE KTIFHLNPSG 250 260 270 280 290 300 RFVIGGPHGD AGLTGRKIII DTYGGWGAHG GGAFSGKDPT KVDRSGAYIA RQAAKSIVAA 310 320 330 340 350 360 GLARRCIVQI SYAIGVPEPL SVFVDTYGTG KIPDKEILKI VKETFDFRPG MIAINLDLLK 370 380 390 GGSRYLKTAA YGHFGRDDAD FTWETVKPLK WEKPQA

References

[1]

"Similar regulation patterns of choline monooxygenase, phosphoethanolamine N-methyltransferase and S-adenosyl-L-methionine synthetase in leaves of the halophyte Atriplex nummularia L." Tabuchi T., Kawaguchi Y., Azuma T., Nanmori T., Yasuda T. Plant Cell Physiol. 46:505-513(2005) [PubMed: 15695433] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION. Tissue: Shoot.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB183562 mRNA. Translation: BAD29708.1.
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

METK2_ATRNU

Accession

Primary (citable) accession number: Q6F3F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	August 16, 2004
Last modified:	September 22, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)