Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enolase-phosphatase E1

Gene

UTR4

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

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

Catalytic activityi

5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.UniRule annotation

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Pathwayi: L-methionine biosynthesis via salvage pathway

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 annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (MRI1)
  2. Methylthioribulose-1-phosphate dehydratase (MDE1)
  3. Enolase-phosphatase E1 (UTR4)
  4. Enolase-phosphatase E1 (UTR4)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
  6. 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)
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 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi11MagnesiumUniRule annotation1 Publication1
Metal bindingi13Magnesium; via carbonyl oxygenUniRule annotation1 Publication1
Binding sitei161SubstrateUniRule annotation1
Metal bindingi186MagnesiumUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-175.
ReactomeiR-SCE-1237112. Methionine salvage pathway.
UniPathwayiUPA00904; 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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL038W.
SGDiS000000764. UTR4.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000657461 – 227Enolase-phosphatase E1Add BLAST227

Proteomic databases

MaxQBiP32626.
PRIDEiP32626.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi36691. 25 interactors.
DIPiDIP-5487N.
MINTiMINT-513487.

Structurei

Secondary structure

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Turni14 – 16Combined sources3
Helixi21 – 24Combined sources4
Helixi26 – 39Combined sources14
Helixi46 – 52Combined sources7
Helixi59 – 71Combined sources13
Helixi77 – 92Combined sources16
Helixi102 – 110Combined sources9
Beta strandi114 – 117Combined sources4
Helixi122 – 130Combined sources9
Helixi146 – 148Combined sources3
Beta strandi151 – 153Combined sources3
Helixi155 – 158Combined sources4
Helixi164 – 174Combined sources11
Helixi178 – 180Combined sources3
Beta strandi181 – 186Combined sources6
Helixi188 – 195Combined sources8
Turni196 – 198Combined sources3
Beta strandi200 – 204Combined sources5
Beta strandi220 – 222Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G80X-ray2.28A/B/C/D1-227[»]
ProteinModelPortaliP32626.
SMRiP32626.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32626.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni118 – 119Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
InParanoidiP32626.
KOiK09880.
OMAiQGMVWEQ.
OrthoDBiEOG092C4XPI.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_03117. Salvage_MtnC_euk. 1 hit.
InterProiIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01691. enolase-ppase. 1 hit.

Sequencei

Sequence statusi: Complete.

P32626-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:227
Mass (Da):25,187
Last modified:June 16, 2009 - v2
Checksum:i147305E847F765DB
GO

Sequence cautioni

The sequence AAA34939 differs from that shown. Reason: Frameshift at positions 139 and 216.Curated
The sequence AAA34939 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB28443 differs from that shown. Reason: Frameshift at positions 139 and 216.Curated
The sequence AAB28443 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB65004 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAD13973 differs from that shown. Reason: Frameshift at positions 139 and 216.Curated
The sequence AAD13973 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56 – 57ID → MH in AAA34939 (PubMed:8411151).Curated2
Sequence conflicti56 – 57ID → MH in AAD13973 (PubMed:8411151).Curated2
Sequence conflicti56 – 57ID → MH in AAB28443 (PubMed:8411151).Curated2
Sequence conflicti179S → T in AAA34939 (PubMed:8411151).Curated1
Sequence conflicti179S → T in AAD13973 (PubMed:8411151).Curated1
Sequence conflicti179S → T in AAB28443 (PubMed:8411151).Curated1

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.
PIRiS30843.
RefSeqiNP_010876.2. NM_001178853.1.

Genome annotation databases

EnsemblFungiiYEL038W; YEL038W; YEL038W.
GeneIDi856673.
KEGGisce:YEL038W.

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.
PIRiS30843.
RefSeqiNP_010876.2. NM_001178853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G80X-ray2.28A/B/C/D1-227[»]
ProteinModelPortaliP32626.
SMRiP32626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36691. 25 interactors.
DIPiDIP-5487N.
MINTiMINT-513487.

Proteomic databases

MaxQBiP32626.
PRIDEiP32626.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL038W; YEL038W; YEL038W.
GeneIDi856673.
KEGGisce:YEL038W.

Organism-specific databases

EuPathDBiFungiDB:YEL038W.
SGDiS000000764. UTR4.

Phylogenomic databases

GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
InParanoidiP32626.
KOiK09880.
OMAiQGMVWEQ.
OrthoDBiEOG092C4XPI.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00876.
UPA00904; UER00877.
BioCyciYEAST:MONOMER3O-175.
ReactomeiR-SCE-1237112. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTraceiP32626.
PROiP32626.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_03117. Salvage_MtnC_euk. 1 hit.
InterProiIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01691. enolase-ppase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENOPH_YEAST
AccessioniPrimary (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: November 2, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2850 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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