Reviewed, UniProtKB/Swiss-Prot P17562 (METK2_ARATH)

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:	SAM2
Ordered Locus Names:	At4g01850
ORF Names:	T7B11.11

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	393 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.
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.
Enzyme regulation	Repressed by 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) and N-ethylmaleimide (NEM). Ref.5
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	Highly expressed in stems and roots. 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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from direct assay. Source: TAIR cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from direct assay. Source: TAIR 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 – 393	393	S-adenosylmethionine synthetase 2		PRO_0000174457
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)
	P17562-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: CE008EA565FD1FBC	FASTA	393	43,255
	10 20 30 40 50 60 METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK 70 80 90 100 110 120 ATIDYEKIVR DTCRSIGFIS DDVGLDADKC KVLVNIEQQS PDIAQGVHGH FTKRPEDIGA 130 140 150 160 170 180 GDQGHMFGYA TDETPELMPL SHVLATKIGA RLTEVRKNGT CRWLRPDGKT QVTVEYYNDN 190 200 210 220 230 240 GAMVPVRVHT VLISTQHDET VTNDEIARDL KEHVIKPIIP EKYLDDKTIF HLNPSGRFVI 250 260 270 280 290 300 GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVANGMAR 310 320 330 340 350 360 RALVQVSYAI GVPEPLSVFV DTYGTGLIPD KEILKIVKET FDFRPGMMTI NLDLKRGGNG 370 380 390 RFQKTAAYGH FGRDDPDFTW EVVKPLKWDK PQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression analyses of the S-adenosylmethionine synthetase gene family in Arabidopsis thaliana." Peleman J., Saito K., Cottyn B., Engler G., Seurinck J., van Montagu M., Inze D. Gene 84:359-369(1989) [PubMed: 2482229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs." Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H. Plant J. 9:101-124(1996) [PubMed: 8580968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-248 AND 322-393. Strain: cv. Columbia. Tissue: Seedling.
[5]	"Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation." Lindermayr C., Saalbach G., Bahnweg G., Durner J. J. Biol. Chem. 281:4285-4291(2006) [PubMed: 16365035] [Abstract] Cited for: ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M33217 Genomic DNA. Translation: AAA32869.1. AC007138 Genomic DNA. Translation: AAD22647.1. AL161493 Genomic DNA. Translation: CAB80678.1. AY072327 mRNA. Translation: AAL61934.1. AY094454 mRNA. Translation: AAM19825.1. BT000575 mRNA. Translation: AAN18144.1. Z33778 mRNA. Translation: CAA83930.1. Z29136 mRNA. Translation: CAA82393.1.
IPI	IPI00529348.
PIR	JQ0410.
RefSeq	NP_001078345.1. NP_192094.1.
UniGene	At.24433 At.24731 At.71920
3D structure databases
HSSP	HSSP built from PDB template 1QM4 based on UniProtKB P13444.
ModBase	Search...
Protein-protein interaction databases
STRING	P17562.
Proteomic databases
PRIDE	P17562.
ProMEX	P17562.
Genome annotation databases
GeneID	826987.
GenomeReviews	Gene locus AT4G01850 in contig CT486007_GR.
KEGG	ath:AT4G01850.
NMPDR	fig|3702.1.peg.17979.
Organism-specific databases
TAIR	At4g01850.
Phylogenomic databases
OMA	VEYYNDN.
Enzyme and pathway databases
BRENDA	2.5.1.6. 302.
Gene expression databases
ArrayExpress	P17562.
Genevestigator	P17562.
GermOnline	AT4G01850. Arabidopsis thaliana.
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_ARATH

Accession

Primary (citable) accession number: P17562
Secondary accession number(s): Q42263

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 3, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)