UniProtKB - P32626 (ENOPH_YEAST)
Protein
Enolase-phosphatase E1
Gene
UTR4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).UniRule annotation
Miscellaneous
Present with 2850 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphateUniRule annotationEC:3.1.3.77UniRule annotation
Cofactori
Mg2+Note: Binds 1 Mg2+ ion per subunit.
: L-methionine biosynthesis via salvage pathway Pathwayi
This protein is involved in step 3 and 4 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotationProteins known to be involved in the 6 steps of the subpathway in this organism are:
- Methylthioribose-1-phosphate isomerase (MRI1)
- Methylthioribulose-1-phosphate dehydratase (MDE1)
- Enolase-phosphatase E1 (UTR4)
- Enolase-phosphatase E1 (UTR4)
- 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
- Aromatic amino acid aminotransferase 2 (ARO9), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Aromatic/aminoadipate aminotransferase 1 (ARO8)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 11 | MagnesiumUniRule annotation1 Publication | 1 | |
Metal bindingi | 13 | Magnesium; via carbonyl oxygenUniRule annotation1 Publication | 1 | |
Binding sitei | 161 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 186 | MagnesiumUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity Source: UniProtKB-UniRule
- 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity Source: UniProtKB-UniRule
- acireductone synthase activity Source: SGD
- magnesium ion binding Source: UniProtKB-UniRule
GO - Biological processi
- L-methionine salvage from methylthioadenosine Source: SGD
- L-methionine salvage from S-adenosylmethionine Source: UniProtKB-UniRule
Keywordsi
Molecular function | Hydrolase |
Biological process | Amino-acid biosynthesis, Methionine biosynthesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-SCE-1237112, Methionine salvage pathway |
UniPathwayi | UPA00904;UER00876 UPA00904;UER00877 |
Names & Taxonomyi
Protein namesi | Recommended name: Enolase-phosphatase E1UniRule annotation (EC:3.1.3.77UniRule annotation)Alternative name(s): 2,3-diketo-5-methylthio-1-phosphopentane phosphataseUniRule annotation Unknown transcript 4 proteinUniRule annotation |
Gene namesi | Name:UTR4UniRule annotation Ordered Locus Names:YEL038W ORF Names:SYGP-ORF20 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000000764, UTR4 |
VEuPathDBi | FungiDB:YEL038W |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000065746 | 1 – 227 | Enolase-phosphatase E1Add BLAST | 227 |
Proteomic databases
MaxQBi | P32626 |
PaxDbi | P32626 |
PRIDEi | P32626 |
Interactioni
Subunit structurei
Monomer.
UniRule annotationProtein-protein interaction databases
BioGRIDi | 36691, 32 interactors |
DIPi | DIP-5487N |
STRINGi | 4932.YEL038W |
Miscellaneous databases
RNActi | P32626, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P32626 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P32626 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 118 – 119 | Substrate bindingUniRule annotation | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2630, Eukaryota |
GeneTreei | ENSGT00440000039914 |
HOGENOMi | CLU_023273_1_1_1 |
InParanoidi | P32626 |
OMAi | HFDTHVG |
Family and domain databases
CDDi | cd01629, HAD_EP, 1 hit |
Gene3Di | 3.40.50.1000, 1 hit |
HAMAPi | MF_03117, Salvage_MtnC_euk, 1 hit |
InterProi | View protein in InterPro IPR023943, Enolase-ppase_E1 IPR027511, ENOPH1_eukaryotes IPR036412, HAD-like_sf IPR023214, HAD_sf |
SUPFAMi | SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR01691, enolase-ppase, 1 hit |
i Sequence
Sequence statusi: Complete.
P32626-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TNKVPQLVQQ DTRDSPVSNI
60 70 80 90 100
LSQFHIDNKE QLQAHILELV AKDVKDPILK QLQGYVWAHG YESGQIKAPV
110 120 130 140 150
YADAIDFIKR KKRVFIYSSG SVKAQKLLFG YVQDPNAPAH DSLDLNSYID
160 170 180 190 200
GYFDINTSGK KTETQSYANI LRDIGAKASE VLFLSDNPLE LDAAAGVGIA
210 220
TGLASRPGNA PVPDGQKYQV YKNFETL
Sequence cautioni
The sequence AAA34939 differs from that shown. Reason: Frameshift.Curated
The sequence AAA34939 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAB28443 differs from that shown. Reason: Frameshift.Curated
The sequence AAB28443 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAB65004 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAD13973 differs from that shown. Reason: Frameshift.Curated
The sequence AAD13973 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 56 – 57 | ID → MH in AAA34939 (PubMed:8411151).Curated | 2 | |
Sequence conflicti | 56 – 57 | ID → MH in AAD13973 (PubMed:8411151).Curated | 2 | |
Sequence conflicti | 56 – 57 | ID → MH in AAB28443 (PubMed:8411151).Curated | 2 | |
Sequence conflicti | 179 | S → T in AAA34939 (PubMed:8411151).Curated | 1 | |
Sequence conflicti | 179 | S → T in AAD13973 (PubMed:8411151).Curated | 1 | |
Sequence conflicti | 179 | S → T in AAB28443 (PubMed:8411151).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L22173 Genomic DNA Translation: AAA34939.1 Sequence problems. S65964 Genomic DNA Translation: AAD13973.1 Sequence problems. S66121 mRNA Translation: AAB28443.1 Sequence problems. U18779 Genomic DNA Translation: AAB65004.1 Different initiation. BK006939 Genomic DNA Translation: DAA07615.1 |
PIRi | S30843 |
RefSeqi | NP_010876.2, NM_001178853.1 |
Genome annotation databases
EnsemblFungii | YEL038W_mRNA; YEL038W; YEL038W |
GeneIDi | 856673 |
KEGGi | sce:YEL038W |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L22173 Genomic DNA Translation: AAA34939.1 Sequence problems. S65964 Genomic DNA Translation: AAD13973.1 Sequence problems. S66121 mRNA Translation: AAB28443.1 Sequence problems. U18779 Genomic DNA Translation: AAB65004.1 Different initiation. BK006939 Genomic DNA Translation: DAA07615.1 |
PIRi | S30843 |
RefSeqi | NP_010876.2, NM_001178853.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2G80 | X-ray | 2.28 | A/B/C/D | 1-227 | [»] | |
SMRi | P32626 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 36691, 32 interactors |
DIPi | DIP-5487N |
STRINGi | 4932.YEL038W |
Proteomic databases
MaxQBi | P32626 |
PaxDbi | P32626 |
PRIDEi | P32626 |
Genome annotation databases
EnsemblFungii | YEL038W_mRNA; YEL038W; YEL038W |
GeneIDi | 856673 |
KEGGi | sce:YEL038W |
Organism-specific databases
SGDi | S000000764, UTR4 |
VEuPathDBi | FungiDB:YEL038W |
Phylogenomic databases
eggNOGi | KOG2630, Eukaryota |
GeneTreei | ENSGT00440000039914 |
HOGENOMi | CLU_023273_1_1_1 |
InParanoidi | P32626 |
OMAi | HFDTHVG |
Enzyme and pathway databases
UniPathwayi | UPA00904;UER00876 UPA00904;UER00877 |
Reactomei | R-SCE-1237112, Methionine salvage pathway |
Miscellaneous databases
EvolutionaryTracei | P32626 |
PROi | PR:P32626 |
RNActi | P32626, protein |
Family and domain databases
CDDi | cd01629, HAD_EP, 1 hit |
Gene3Di | 3.40.50.1000, 1 hit |
HAMAPi | MF_03117, Salvage_MtnC_euk, 1 hit |
InterProi | View protein in InterPro IPR023943, Enolase-ppase_E1 IPR027511, ENOPH1_eukaryotes IPR036412, HAD-like_sf IPR023214, HAD_sf |
SUPFAMi | SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR01691, enolase-ppase, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ENOPH_YEAST | |
Accessioni | P32626Primary (citable) accession number: P32626 Secondary accession number(s): D3DLL1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | June 16, 2009 | |
Last modified: | February 10, 2021 | |
This is version 159 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome V
Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families