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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111MagnesiumUniRule annotation1 Publication
Metal bindingi13 – 131Magnesium; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei161 – 1611SubstrateUniRule annotation
Metal bindingi186 – 1861MagnesiumUniRule annotation1 Publication

GO - Molecular functioni

  1. 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity Source: UniProtKB-HAMAP
  2. 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity Source: UniProtKB-HAMAP
  3. acireductone synthase activity Source: SGD
  4. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. L-methionine biosynthetic process from methylthioadenosine Source: SGD
  3. L-methionine biosynthetic process from S-adenosylmethionine Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30159-MONOMER.
YEAST:MONOMER3O-175.
ReactomeiREACT_350157. 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
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL038W.
SGDiS000000764. UTR4.

Subcellular locationi

  1. Cytoplasm UniRule annotation1 Publication
  2. Nucleus UniRule annotation1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Enolase-phosphatase E1PRO_0000065746Add
BLAST

Proteomic databases

MaxQBiP32626.
PaxDbiP32626.
PeptideAtlasiP32626.

Expressioni

Gene expression databases

GenevestigatoriP32626.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi36691. 25 interactions.
DIPiDIP-5487N.
MINTiMINT-513487.
STRINGi4932.YEL038W.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Turni14 – 163Combined sources
Helixi21 – 244Combined sources
Helixi26 – 3914Combined sources
Helixi46 – 527Combined sources
Helixi59 – 7113Combined sources
Helixi77 – 9216Combined sources
Helixi102 – 1109Combined sources
Beta strandi114 – 1174Combined sources
Helixi122 – 1309Combined sources
Helixi146 – 1483Combined sources
Beta strandi151 – 1533Combined sources
Helixi155 – 1584Combined sources
Helixi164 – 17411Combined sources
Helixi178 – 1803Combined sources
Beta strandi181 – 1866Combined sources
Helixi188 – 1958Combined sources
Turni196 – 1983Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi220 – 2223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G80X-ray2.28A/B/C/D1-227[»]
ProteinModelPortaliP32626.
SMRiP32626. Positions 3-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32626.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 1192Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG4229.
GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
InParanoidiP32626.
KOiK09880.
OMAiQGMVWEQ.
OrthoDBiEOG75B8GZ.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_03117. Salvage_MtnC_euk.
InterProiIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[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 AAA34939.1 differs from that shown. Reason: Frameshift at positions 139 and 216. Curated
The sequence AAA34939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB28443.1 differs from that shown. Reason: Frameshift at positions 139 and 216. Curated
The sequence AAB28443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB65004.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAD13973.1 differs from that shown. Reason: Frameshift at positions 139 and 216. Curated
The sequence AAD13973.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 572ID → MH in AAA34939 (PubMed:8411151).Curated
Sequence conflicti56 – 572ID → MH in AAD13973 (PubMed:8411151).Curated
Sequence conflicti56 – 572ID → MH in AAB28443 (PubMed:8411151).Curated
Sequence conflicti179 – 1791S → T in AAA34939 (PubMed:8411151).Curated
Sequence conflicti179 – 1791S → T in AAD13973 (PubMed:8411151).Curated
Sequence conflicti179 – 1791S → T in AAB28443 (PubMed:8411151).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2G80X-ray2.28A/B/C/D1-227[»]
ProteinModelPortaliP32626.
SMRiP32626. Positions 3-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36691. 25 interactions.
DIPiDIP-5487N.
MINTiMINT-513487.
STRINGi4932.YEL038W.

Proteomic databases

MaxQBiP32626.
PaxDbiP32626.
PeptideAtlasiP32626.

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

eggNOGiCOG4229.
GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
InParanoidiP32626.
KOiK09880.
OMAiQGMVWEQ.
OrthoDBiEOG75B8GZ.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00876.
UPA00904; UER00877.
BioCyciYEAST:G3O-30159-MONOMER.
YEAST:MONOMER3O-175.
ReactomeiREACT_350157. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTraceiP32626.
NextBioi982690.
PROiP32626.

Gene expression databases

GenevestigatoriP32626.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_03117. Salvage_MtnC_euk.
InterProiIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01691. enolase-ppase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry."
    Melnick L., Sherman F.
    J. Mol. Biol. 233:372-388(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: B-6441.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Crystal structure of UTR4 protein (unknown transcript 4 protein) (YEL038w) from Saccharomyces cerevisiae at 2.28 A resolution."
    Joint center for structural genomics (JCSG)
    Submitted (MAR-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.

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: April 29, 2015
This is version 120 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

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.