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Protein

S-adenosylmethionine synthase 2

Gene

SAM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.1 Publication

Miscellaneous

In yeast, there are two genes coding for AdoMet synthase.
Present with 22000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.By similarity

Pathwayi: S-adenosyl-L-methionine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase 1 (SAM1), S-adenosylmethionine synthase 2 (SAM2)
This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12MagnesiumBy similarity1
Binding sitei18ATPBy similarity1
Metal bindingi46PotassiumBy similarity1
Binding sitei59MethionineBy similarity1
Binding sitei102MethionineBy similarity1
Binding sitei247ATPBy similarity1
Binding sitei247Methionine; shared with neighboring subunitBy similarity1
Binding sitei270ATP; via amide nitrogen; shared with neighboring subunitBy similarity1
Binding sitei274ATP; shared with neighboring subunitBy similarity1
Binding sitei278ATP; shared with neighboring subunitBy similarity1
Binding sitei278MethionineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi168 – 170ATPBy similarity3
Nucleotide bindingi236 – 239ATPBy similarity4
Nucleotide bindingi253 – 254ATPBy similarity2

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • methionine adenosyltransferase activity Source: SGD

GO - Biological processi

  • methionine metabolic process Source: SGD
  • one-carbon metabolic process Source: UniProtKB-KW
  • S-adenosylmethionine biosynthetic process Source: SGD

Keywordsi

Molecular functionTransferase
Biological processOne-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-1014
YEAST:MONOMER3O-1014
BRENDAi2.5.1.6 984
ReactomeiR-SCE-156581 Methylation
R-SCE-1614635 Sulfur amino acid metabolism
R-SCE-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se
UniPathwayiUPA00315; UER00080

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase 2 (EC:2.5.1.61 Publication)
Short name:
AdoMet synthase 2
Alternative name(s):
Methionine adenosyltransferase 2
Short name:
MAT 2
Gene namesi
Name:SAM2
Synonyms:ETH2
Ordered Locus Names:YDR502C
ORF Names:D9719.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR502C
SGDiS000002910 SAM2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001744522 – 384S-adenosylmethionine synthase 2Add BLAST383

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP19358
PaxDbiP19358
PRIDEiP19358

PTM databases

iPTMnetiP19358

Interactioni

Subunit structurei

Heterotetramer.

Protein-protein interaction databases

BioGridi32553, 82 interactors
DIPiDIP-4001N
IntActiP19358, 38 interactors
MINTiP19358
STRINGi4932.YDR502C

Structurei

3D structure databases

ProteinModelPortaliP19358
SMRiP19358
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

GeneTreeiENSGT00500000044811
HOGENOMiHOG000245710
InParanoidiP19358
KOiK00789
OMAiPGHFLFT
OrthoDBiEOG092C2SCC

Family and domain databases

HAMAPiMF_00086 S_AdoMet_synth1, 1 hit
InterProiView protein in 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
PANTHERiPTHR11964 PTHR11964, 1 hit
PfamiView protein in Pfam
PF02773 S-AdoMet_synt_C, 1 hit
PF02772 S-AdoMet_synt_M, 1 hit
PF00438 S-AdoMet_synt_N, 1 hit
PIRSFiPIRSF000497 MAT, 1 hit
SUPFAMiSSF55973 SSF55973, 3 hits
TIGRFAMsiTIGR01034 metK, 1 hit
PROSITEiView protein in PROSITE
PS00376 ADOMET_SYNTHASE_1, 1 hit
PS00377 ADOMET_SYNTHASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSKTFLFT SESVGEGHPD KICDQVSDAI LDACLEQDPF SKVACETAAK
60 70 80 90 100
TGMIMVFGEI TTKARLDYQQ IVRDTIKKIG YDDSAKGFDY KTCNVLVAIE
110 120 130 140 150
QQSPDIAQGL HYEKSLEDLG AGDQGIMFGY ATDETPEGLP LTILLAHKLN
160 170 180 190 200
MAMADARRDG SLPWLRPDTK TQVTVEYEDD NGRWVPKRID TVVISAQHAD
210 220 230 240 250
EISTADLRTQ LQKDIVEKVI PKDMLDENTK YFIQPSGRFV IGGPQGDAGL
260 270 280 290 300
TGRKIIVDAY GGASSVGGGA FSGKDYSKVD RSAAYAARWV AKSLVAAGLC
310 320 330 340 350
KRVQVQFSYA IGIAEPLSLH VDTYGTATKS DDEIIEIIKK NFDLRPGVLV
360 370 380
KELDLARPIY LPTASYGHFT NQEYSWEKPK KLEF
Length:384
Mass (Da):42,256
Last modified:January 23, 2007 - v3
Checksum:i0AFCB0BA386F088B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti130Y → H in AAT93205 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23368 Genomic DNA Translation: AAA35017.1
U33057 Genomic DNA Translation: AAB64944.1
AY693186 Genomic DNA Translation: AAT93205.1
BK006938 Genomic DNA Translation: DAA12334.1
PIRiA31398
RefSeqiNP_010790.3, NM_001180810.3

Genome annotation databases

EnsemblFungiiYDR502C; YDR502C; YDR502C
GeneIDi852113
KEGGisce:YDR502C

Similar proteinsi

Entry informationi

Entry nameiMETK2_YEAST
AccessioniPrimary (citable) accession number: P19358
Secondary accession number(s): D6VTC4, E9P927
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 174 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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