Q4H1G3 (METK2_BETVU) 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

Beta vulgaris (Sugar beet)

Taxonomic identifier

161934 [NCBI]

Taxonomic lineage

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

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. May be involved in the synthesis of betain in response to abiotic stress such as high salinity. Ref.1
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	Follow a circadian regulation with higher levels in the light. 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_0000363010
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)
	Q4H1G3 [UniParc]. Last modified August 30, 2005. Version 1. Checksum: 8C59D838FC527CC4	FASTA	393	42,961
	10 20 30 40 50 60 METFLFTSES VNEGHPDKLC DQVSDAVLDA CLAQDPESKV ACETCTKTNM VMVFGEITTK 70 80 90 100 110 120 AEVDYEKIVR DTCRSIGFTS DDVGLDADKC KVLVNIEQQS PDIAQGVHGH LTKRPEEIGA 130 140 150 160 170 180 GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGA CAWLRPDGKT QVTVEYYNDN 190 200 210 220 230 240 GAMVPVRVHT VLISTQHDET VSNDEIAADL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI 250 260 270 280 290 300 GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVANGLAR 310 320 330 340 350 360 RAIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILKIVKET FDFRPGMMSI NLDLKRGGNG 370 380 390 RFQKTAAYGH FGRDDPDFTW EVVKPLKWEK IPA

References

[1]	"Transcriptional response of glycinebetaine-related genes to salt stress and light in leaf beet." Tabuchi T., Okada T., Takashima Y., Azuma T., Nanmori T., Yasuda T. Plant Biotechnol. 23:317-320(2006) Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB221010 mRNA. Translation: BAE07180.1.
3D structure databases
ProteinModelPortal	Q4H1G3.
SMR	Q4H1G3. 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_BETVU

Accession

Primary (citable) accession number: Q4H1G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	August 30, 2005
Last modified:	June 28, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program