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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit.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.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201MagnesiumBy similarity
Metal bindingi46 – 461PotassiumBy similarity
Binding sitei148 – 1481ATPSequence analysis
Metal bindingi272 – 2721PotassiumBy similarity
Metal bindingi280 – 2801MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 1256ATPSequence analysis

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
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-429.
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:2.5.1.6)
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 384383S-adenosylmethionine synthase 2PRO_0000174452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki78 – 78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki86 – 86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP19358.
PeptideAtlasiP19358.
PRIDEiP19358.

PTM databases

iPTMnetiP19358.

Interactioni

Subunit structurei

Heterotetramer.

Protein-protein interaction databases

BioGridi32553. 42 interactions.
DIPiDIP-4001N.
IntActiP19358. 10 interactions.
MINTiMINT-476096.

Structurei

3D structure databases

ProteinModelPortaliP19358.
SMRiP19358. Positions 7-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
InParanoidiP19358.
KOiK00789.
OMAiHISAVVH.
OrthoDBiEOG7SN8NV.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301Y → H in AAT93205 (PubMed:17322287).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP19358.
SMRiP19358. Positions 7-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32553. 42 interactions.
DIPiDIP-4001N.
IntActiP19358. 10 interactions.
MINTiMINT-476096.

PTM databases

iPTMnetiP19358.

Proteomic databases

MaxQBiP19358.
PeptideAtlasiP19358.
PRIDEiP19358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR502C; YDR502C; YDR502C.
GeneIDi852113.
KEGGisce:YDR502C.

Organism-specific databases

EuPathDBiFungiDB:YDR502C.
SGDiS000002910. SAM2.

Phylogenomic databases

GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
InParanoidiP19358.
KOiK00789.
OMAiHISAVVH.
OrthoDBiEOG7SN8NV.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciMetaCyc:MONOMER-429.
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.

Miscellaneous databases

NextBioi970481.
PROiP19358.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-78 AND LYS-86.
    Strain: SUB592.

Entry informationi

Entry nameiMETK2_YEAST
AccessioniPrimary (citable) accession number: P19358
Secondary accession number(s): D6VTC4, E9P927
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.