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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

MEU1

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 reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. Seems to be implicated in the regulation of the expression of the ADH2 gene.UniRule annotation4 Publications

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411PhosphateUniRule annotation
Sitei212 – 2121Important for substrate specificityUniRule annotation
Binding sitei230 – 2301Substrate; via amide nitrogenUniRule annotation
Binding sitei231 – 2311PhosphateUniRule annotation
Sitei267 – 2671Important for substrate specificityUniRule annotation

GO - Molecular functioni

  1. mRNA binding Source: SGD
  2. phosphorylase activity Source: InterPro
  3. S-methyl-5-thioadenosine phosphorylase activity Source: SGD

GO - Biological processi

  1. glutamate biosynthetic process Source: SGD
  2. L-methionine biosynthetic process from methylthioadenosine Source: SGD
  3. purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BioCyciYEAST:G3O-32178-MONOMER.
YEAST:MONOMER3O-157.
ReactomeiREACT_350157. Methionine salvage pathway.
UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
Alternative name(s):
5'-methylthioadenosine phosphorylaseUniRule annotation
Short name:
MTA phosphorylaseUniRule annotation
Short name:
MTAPUniRule annotation
Short name:
MTAPaseUniRule annotation
Multicopy enhancer of UAS2
Gene namesi
Name:MEU1UniRule annotation
Ordered Locus Names:YLR017W
ORF Names:L1595
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR017w.
EuPathDBiFungiDB:YLR017W.
SGDiS000004007. MEU1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337S-methyl-5'-thioadenosine phosphorylasePRO_0000184556Add
BLAST

Proteomic databases

MaxQBiQ07938.
PaxDbiQ07938.
PeptideAtlasiQ07938.

Expressioni

Gene expression databases

GenevestigatoriQ07938.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

BioGridi31291. 27 interactions.
DIPiDIP-989N.
IntActiQ07938. 2 interactions.
MINTiMINT-4494408.

Structurei

3D structure databases

ProteinModelPortaliQ07938.
SMRiQ07938. Positions 30-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 892Phosphate bindingUniRule annotation
Regioni121 – 1222Phosphate bindingUniRule annotation
Regioni254 – 2563Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
KOiK00772.
OMAiHTPYGRP.
OrthoDBiEOG77DJGM.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRIKNTFSV AKRLKLSKVM TNSELPSIFE GTVDLGIIGG TGLYNLDCLE
60 70 80 90 100
PIALLPPMVT PWGTTSSPVT ISQFVGTNSH FHVAFIARHG INHEYPPTKV
110 120 130 140 150
PFRANMAALK NLNCKAVLSF SAVGSLQPHI KPRDFVLPQQ IIDRTKGIRH
160 170 180 190 200
SSYFNDEGLV GHVGFGQPFS QKFAEYIYQF KNEITNPESE EPCHLHYDKD
210 220 230 240 250
MTVVCMEGPQ FSTRAESKMY RMFGGHVINM SVIPEAKLAR ECELPYQMIC
260 270 280 290 300
MSTDYDAWRD EAEPVTVETV IGNLTNNGRN ANILASKIIV SMAKEIPEFM
310 320 330
HTGDGLRGSI KKSISTKPEA MSKETLERLR YLFPNYW
Length:337
Mass (Da):37,857
Last modified:November 1, 1997 - v1
Checksum:i99B54F62ED8A9389
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551L → V in CAA62156 (Ref. 1) Curated
Sequence conflicti157 – 1571E → G in AAT93089 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90564 Genomic DNA. Translation: CAA62156.1.
Z73189 Genomic DNA. Translation: CAA97539.1.
AY693070 Genomic DNA. Translation: AAT93089.1.
BK006945 Genomic DNA. Translation: DAA09335.1.
PIRiS64839.
RefSeqiNP_013117.1. NM_001181904.1.

Genome annotation databases

EnsemblFungiiYLR017W; YLR017W; YLR017W.
GeneIDi850704.
KEGGisce:YLR017W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90564 Genomic DNA. Translation: CAA62156.1.
Z73189 Genomic DNA. Translation: CAA97539.1.
AY693070 Genomic DNA. Translation: AAT93089.1.
BK006945 Genomic DNA. Translation: DAA09335.1.
PIRiS64839.
RefSeqiNP_013117.1. NM_001181904.1.

3D structure databases

ProteinModelPortaliQ07938.
SMRiQ07938. Positions 30-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31291. 27 interactions.
DIPiDIP-989N.
IntActiQ07938. 2 interactions.
MINTiMINT-4494408.

Proteomic databases

MaxQBiQ07938.
PaxDbiQ07938.
PeptideAtlasiQ07938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR017W; YLR017W; YLR017W.
GeneIDi850704.
KEGGisce:YLR017W.

Organism-specific databases

CYGDiYLR017w.
EuPathDBiFungiDB:YLR017W.
SGDiS000004007. MEU1.

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
KOiK00772.
OMAiHTPYGRP.
OrthoDBiEOG77DJGM.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
BioCyciYEAST:G3O-32178-MONOMER.
YEAST:MONOMER3O-157.
ReactomeiREACT_350157. Methionine salvage pathway.

Miscellaneous databases

NextBioi966748.
PROiQ07938.

Gene expression databases

GenevestigatoriQ07938.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 7.8kb fragment from chromosome XII of Saccharomyces cerevisiae does not harbour PKC2."
    Saville S.P., Atkinson S., Jamieson L., Pocklington M.J., Orr E.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Isolation and identification of genes activating UAS2-dependent ADH2 expression in Saccharomyces cerevisiae."
    Donoviel M.S., Young E.T.
    Genetics 143:1137-1148(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites."
    Subhi A.L., Diegelman P., Porter C.W., Tang B., Lu Z.J., Markham G.D., Kruger W.D.
    J. Biol. Chem. 278:49868-49873(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Methylthioadenosine and polyamine biosynthesis in a Saccharomyces cerevisiae meu1delta mutant."
    Chattopadhyay M.K., Tabor C.W., Tabor H.
    Biochem. Biophys. Res. Commun. 343:203-207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A complete inventory of all enzymes in the eukaryotic methionine salvage pathway."
    Pirkov I., Norbeck J., Gustafsson L., Albers E.
    FEBS J. 275:4111-4120(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMTAP_YEAST
AccessioniPrimary (citable) accession number: Q07938
Secondary accession number(s): D6VY19, E9P915, Q06899
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4820 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

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 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.