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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: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. S-methyl-5'-thioadenosine phosphorylase (MEU1)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, 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-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41PhosphateUniRule annotation1
Sitei212Important for substrate specificityUniRule annotation1
Binding sitei230Substrate; via amide nitrogenUniRule annotation1
Binding sitei231PhosphateUniRule annotation1
Sitei267Important for substrate specificityUniRule annotation1

GO - Molecular functioni

  • mRNA binding Source: SGD
  • S-methyl-5-thioadenosine phosphorylase activity Source: SGD

GO - Biological processi

  • glutamate biosynthetic process Source: SGD
  • L-methionine biosynthetic process from methylthioadenosine Source: SGD
  • purine-containing compound salvage Source: GO_Central
  • purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-157.
ReactomeiR-SCE-1237112. 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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR017W.
SGDiS000004007. MEU1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001845561 – 337S-methyl-5'-thioadenosine phosphorylaseAdd BLAST337

Proteomic databases

MaxQBiQ07938.
PRIDEiQ07938.

PTM databases

iPTMnetiQ07938.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ07938.
SMRiQ07938.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 89Phosphate bindingUniRule annotation2
Regioni121 – 122Phosphate bindingUniRule annotation2
Regioni254 – 256Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
KOiK00772.
OMAiPEERKCG.
OrthoDBiEOG092C46SL.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti55L → V in CAA62156 (Ref. 1) Curated1
Sequence conflicti157E → G in AAT93089 (PubMed:17322287).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ07938.

Proteomic databases

MaxQBiQ07938.
PRIDEiQ07938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR017W.
SGDiS000004007. MEU1.

Phylogenomic databases

GeneTreeiENSGT00550000074874.
HOGENOMiHOG000228986.
KOiK00772.
OMAiPEERKCG.
OrthoDBiEOG092C46SL.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
BioCyciYEAST:MONOMER3O-157.
ReactomeiR-SCE-1237112. Methionine salvage pathway.

Miscellaneous databases

PROiQ07938.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP. 1 hit.
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...

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: November 2, 2016
This is version 123 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

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.