Reviewed, UniProtKB/Swiss-Prot P19358 (METK2_YEAST)

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
Synonyms:	ETH2
Ordered Locus Names:	YDR502C
ORF Names:	D9719.8

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
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	Heterotetramer.
Miscellaneous	In yeast, there are two genes coding for AdoMet synthetase. Present with 22000 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the AdoMet synthetase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Inferred from mutant phenotype. Source: SGD methionine metabolic process Inferred from mutant phenotype. Source: SGD one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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 direct assay. Source: SGD potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KAP120	Q02932	1	EBI-10795,EBI-33816

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 384	383	S-adenosylmethionine synthetase 2		PRO_0000174452
Regions
	Nucleotide binding	120 – 125	6	ATP Potential
Sites
	Metal binding	20	1	Magnesium By similarity
	Metal binding	46	1	Potassium By similarity
	Metal binding	272	1	Potassium By similarity
	Metal binding	280	1	Magnesium By similarity
	Binding site	148	1	ATP Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.3
	Modified residue	195	1	Phosphoserine Ref.6
	Cross-link	77		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
	Cross-link	78		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
	Cross-link	86		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P19358-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0AFCB0BA386F088B	FASTA	384	42,256
	10 20 30 40 50 60 MSKSKTFLFT SESVGEGHPD KICDQVSDAI LDACLEQDPF SKVACETAAK TGMIMVFGEI 70 80 90 100 110 120 TTKARLDYQQ IVRDTIKKIG YDDSAKGFDY KTCNVLVAIE QQSPDIAQGL HYEKSLEDLG 130 140 150 160 170 180 AGDQGIMFGY ATDETPEGLP LTILLAHKLN MAMADARRDG SLPWLRPDTK TQVTVEYEDD 190 200 210 220 230 240 NGRWVPKRID TVVISAQHAD EISTADLRTQ LQKDIVEKVI PKDMLDENTK YFIQPSGRFV 250 260 270 280 290 300 IGGPQGDAGL TGRKIIVDAY GGASSVGGGA FSGKDYSKVD RSAAYAARWV AKSLVAAGLC 310 320 330 340 350 360 KRVQVQFSYA IGIAEPLSLH VDTYGTATKS DDEIIEIIKK NFDLRPGVLV KELDLARPIY 370 380 LPTASYGHFT NQEYSWEKPK KLEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes." Thomas D., Rothstein R., Rosenberg N., Surdin-Kerjan Y. Mol. Cell. Biol. 8:5132-5139(1988) [PubMed: 3072475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-78 AND LYS-86, MASS SPECTROMETRY.
[6]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M23368 Genomic DNA. Translation: AAA35017.1. U33057 Genomic DNA. Translation: AAB64944.1.
PIR	A31398.
RefSeq	NP_010790.1.
3D structure databases
SMR	P19358. Positions 7-384.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4001N.
IntAct	P19358. 13 interactions.
STRING	P19358.
Proteomic databases
PeptideAtlas	P19358.
PRIDE	P19358.
Genome annotation databases
Ensembl	YDR502C; YDR502C; YDR502C; Saccharomyces cerevisiae. [Genome view]
GeneID	852113.
KEGG	sce:YDR502C.
NMPDR	fig|4932.3.peg.1563.
Organism-specific databases
CYGD	YDR502c.
SGD	S000002910. SAM2.
Phylogenomic databases
HOGENOM	HBG443662.
OMA	RTAAYMA.
OrthoDB	EOG9KWM8W.
PhylomeDB	P19358.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-429.
BRENDA	2.5.1.6. 250.
Gene expression databases
ArrayExpress	P19358.
Genevestigator	P19358.
GermOnline	YDR502C. Saccharomyces cerevisiae.
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...
Other Resources
NextBio	970481.

Entry information

Entry name

METK2_YEAST

Accession

Primary (citable) accession number: P19358

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)