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P32626

- ENOPH_YEAST

UniProt

P32626 - ENOPH_YEAST

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Protein

Enolase-phosphatase E1

Gene

UTR4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

Binds 1 magnesium ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Magnesium1 PublicationUniRule annotation
Metal bindingi13 – 131Magnesium; via carbonyl oxygen1 PublicationUniRule annotation
Binding sitei161 – 1611SubstrateUniRule annotation
Metal bindingi186 – 1861Magnesium1 PublicationUniRule annotation

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_189018. 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: Chromosome V

Organism-specific databases

SGDiS000000764. UTR4.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
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 – 105
Turni14 – 163
Helixi21 – 244
Helixi26 – 3914
Helixi46 – 527
Helixi59 – 7113
Helixi77 – 9216
Helixi102 – 1109
Beta strandi114 – 1174
Helixi122 – 1309
Helixi146 – 1483
Beta strandi151 – 1533
Helixi155 – 1584
Helixi164 – 17411
Helixi178 – 1803
Beta strandi181 – 1866
Helixi188 – 1958
Turni196 – 1983
Beta strandi200 – 2045
Beta strandi220 – 2223

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiLLFGHTN.
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.
The sequence AAB28443.1 differs from that shown. Reason: Frameshift at positions 139 and 216.
The sequence AAD13973.1 differs from that shown. Reason: Frameshift at positions 139 and 216.
The sequence AAA34939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAB28443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAB65004.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAD13973.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G80 X-ray 2.28 A/B/C/D 1-227 [» ]
ProteinModelPortali P32626.
SMRi P32626. Positions 3-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36691. 25 interactions.
DIPi DIP-5487N.
MINTi MINT-513487.
STRINGi 4932.YEL038W.

Proteomic databases

MaxQBi P32626.
PaxDbi P32626.
PeptideAtlasi P32626.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YEL038W ; YEL038W ; YEL038W .
GeneIDi 856673.
KEGGi sce:YEL038W.

Organism-specific databases

SGDi S000000764. UTR4.

Phylogenomic databases

eggNOGi COG4229.
GeneTreei ENSGT00440000039914.
HOGENOMi HOG000237286.
InParanoidi P32626.
KOi K09880.
OMAi LLFGHTN.
OrthoDBi EOG75B8GZ.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00876 .
UPA00904 ; UER00877 .
BioCyci YEAST:G3O-30159-MONOMER.
YEAST:MONOMER3O-175.
Reactomei REACT_189018. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTracei P32626.
NextBioi 982690.
PROi P32626.

Gene expression databases

Genevestigatori P32626.

Family and domain databases

Gene3Di 3.40.50.1000. 1 hit.
HAMAPi MF_03117. Salvage_MtnC_euk.
InterProi IPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
[Graphical view ]
Pfami PF13419. HAD_2. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01691. enolase-ppase. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 116 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