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Protein

S-adenosylmethionine synthase 1

Gene

SAM1

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 bindingi18 – 181MagnesiumBy similarity
Metal bindingi44 – 441PotassiumBy similarity
Binding sitei146 – 1461ATPSequence analysis
Metal bindingi270 – 2701PotassiumBy similarity
Metal bindingi278 – 2781MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi118 – 1236ATPSequence 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-404.
YEAST:YLR180W-MONOMER.
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 1 (EC:2.5.1.6)
Short name:
AdoMet synthase 1
Alternative name(s):
Methionine adenosyltransferase 1
Short name:
MAT 1
Gene namesi
Name:SAM1
Synonyms:ETH10
Ordered Locus Names:YLR180W
ORF Names:L9470.9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR180W.
SGDiS000004170. SAM1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382S-adenosylmethionine synthase 1PRO_0000174451Add
BLAST

Proteomic databases

MaxQBiP10659.
PeptideAtlasiP10659.
PRIDEiP10659.

Interactioni

Subunit structurei

Heterotetramer.

Protein-protein interaction databases

BioGridi31451. 128 interactions.
DIPiDIP-6667N.
IntActiP10659. 92 interactions.
MINTiMINT-626539.

Structurei

3D structure databases

ProteinModelPortaliP10659.
SMRiP10659. Positions 3-382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

GeneTreeiENSGT00830000129482.
HOGENOMiHOG000245710.
InParanoidiP10659.
KOiK00789.
OMAiQDGFHWE.
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.

P10659-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTFLFTSE SVGEGHPDKI CDQVSDAILD ACLAEDPHSK VACETAAKTG
60 70 80 90 100
MIMVFGEITT KAQLDYQKIV RDTIKKIGYD DSAKGFDYKT CNVLVAIEQQ
110 120 130 140 150
SPDIAQGVHE EKDLEDIGAG DQGIMFGYAT DETPEGLPLT ILLAHKLNMA
160 170 180 190 200
MADARRDGSL AWLRPDTKTQ VTVEYKDDHG RWVPQRIDTV VVSAQHADEI
210 220 230 240 250
TTEDLRAQLK SEIIEKVIPR DMLDENTKYF IQPSGRFVIG GPQGDAGLTG
260 270 280 290 300
RKIIVDAYGG ASSVGGGAFS GKDYSKVDRS AAYAARWVAK SLVAAGLCKR
310 320 330 340 350
VQVQFSYAIG IAEPLSLHVD TYGTATKSDE EIIDIISKNF DLRPGVLVKE
360 370 380
LDLARPIYLP TASYGHFTNQ EYPWEKPKTL KF
Length:382
Mass (Da):41,818
Last modified:February 1, 1996 - v2
Checksum:i18F82FC809EE4706
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2461A → T in AAA66932 (PubMed:3316224).Curated
Sequence conflicti357 – 3571I → F in AAA66932 (PubMed:3316224).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03477 Genomic DNA. Translation: AAA66932.1.
U17246 Genomic DNA. Translation: AAB67461.1.
BK006945 Genomic DNA. Translation: DAA09500.1.
PIRiS51425.
RefSeqiNP_013281.1. NM_001182067.1.

Genome annotation databases

EnsemblFungiiYLR180W; YLR180W; YLR180W.
GeneIDi850877.
KEGGisce:YLR180W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03477 Genomic DNA. Translation: AAA66932.1.
U17246 Genomic DNA. Translation: AAB67461.1.
BK006945 Genomic DNA. Translation: DAA09500.1.
PIRiS51425.
RefSeqiNP_013281.1. NM_001182067.1.

3D structure databases

ProteinModelPortaliP10659.
SMRiP10659. Positions 3-382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31451. 128 interactions.
DIPiDIP-6667N.
IntActiP10659. 92 interactions.
MINTiMINT-626539.

Proteomic databases

MaxQBiP10659.
PeptideAtlasiP10659.
PRIDEiP10659.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR180W; YLR180W; YLR180W.
GeneIDi850877.
KEGGisce:YLR180W.

Organism-specific databases

EuPathDBiFungiDB:YLR180W.
SGDiS000004170. SAM1.

Phylogenomic databases

GeneTreeiENSGT00830000129482.
HOGENOMiHOG000245710.
InParanoidiP10659.
KOiK00789.
OMAiQDGFHWE.
OrthoDBiEOG7SN8NV.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciMetaCyc:MONOMER-404.
YEAST:YLR180W-MONOMER.
ReactomeiR-SCE-156581. Methylation.
R-SCE-1614635. Sulfur amino acid metabolism.
R-SCE-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Miscellaneous databases

NextBioi967224.
PROiP10659.

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. "SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression."
    Thomas D., Surdin-Kerjan Y.
    J. Biol. Chem. 262:16704-16709(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
    Norbeck J., Blomberg A.
    FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 157-162; 187-196 AND 253-258.
    Strain: ATCC 38531 / Y41.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMETK1_YEAST
AccessioniPrimary (citable) accession number: P10659
Secondary accession number(s): D6VYI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 162 of the entry and version 2 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 103000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.