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P32626 (ENOPH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enolase-phosphatase E1

EC=3.1.3.77
Alternative name(s):
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Unknown transcript 4 protein
Gene names
Name:UTR4
Ordered Locus Names:YEL038W
ORF Names:SYGP-ORF20
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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) By similarity. HAMAP-Rule MF_03117

Catalytic activity

5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate. HAMAP-Rule MF_03117

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. HAMAP-Rule MF_03117

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03117

Subcellular location

Cytoplasm. Nucleus Ref.5.

Miscellaneous

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

Sequence similarities

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

Sequence caution

The sequence AAA34939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA34939.1 differs from that shown. Reason: Frameshift at positions 139 and 216.

The sequence AAB28443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAB28443.1 differs from that shown. Reason: Frameshift at positions 139 and 216.

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.

The sequence AAD13973.1 differs from that shown. Reason: Frameshift at positions 139 and 216.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Enolase-phosphatase E1 HAMAP-Rule MF_03117
PRO_0000065746

Regions

Region118 – 1192Substrate binding By similarity

Sites

Metal binding111Magnesium
Metal binding131Magnesium; via carbonyl oxygen
Metal binding1861Magnesium
Binding site1611Substrate By similarity

Experimental info

Sequence conflict56 – 572ID → MH in AAA34939. Ref.1
Sequence conflict56 – 572ID → MH in AAD13973. Ref.1
Sequence conflict56 – 572ID → MH in AAB28443. Ref.1
Sequence conflict1791S → T in AAA34939. Ref.1
Sequence conflict1791S → T in AAD13973. Ref.1
Sequence conflict1791S → T in AAB28443. Ref.1

Secondary structure

....................................... 227
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32626 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 147305E847F765DB

FASTA22725,187
        10         20         30         40         50         60 
MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TNKVPQLVQQ DTRDSPVSNI LSQFHIDNKE 

        70         80         90        100        110        120 
QLQAHILELV AKDVKDPILK QLQGYVWAHG YESGQIKAPV YADAIDFIKR KKRVFIYSSG 

       130        140        150        160        170        180 
SVKAQKLLFG YVQDPNAPAH DSLDLNSYID GYFDINTSGK KTETQSYANI LRDIGAKASE 

       190        200        210        220 
VLFLSDNPLE LDAAAGVGIA TGLASRPGNA PVPDGQKYQV YKNFETL 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS30843.
RefSeqNP_010876.2. NM_001178853.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G80X-ray2.28A/B/C/D1-227[»]
ProteinModelPortalP32626.
SMRP32626. Positions 3-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36691. 24 interactions.
DIPDIP-5487N.
MINTMINT-513487.
STRING4932.YEL038W.

Proteomic databases

MaxQBP32626.
PaxDbP32626.
PeptideAtlasP32626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL038W; YEL038W; YEL038W.
GeneID856673.
KEGGsce:YEL038W.

Organism-specific databases

SGDS000000764. UTR4.

Phylogenomic databases

eggNOGCOG4229.
GeneTreeENSGT00440000039914.
HOGENOMHOG000237286.
KOK09880.
OMALLFGHTN.
OrthoDBEOG75B8GZ.

Enzyme and pathway databases

BioCycYEAST:G3O-30159-MONOMER.
YEAST:MONOMER3O-175.
UniPathwayUPA00904; UER00876.
UPA00904; UER00877.

Gene expression databases

GenevestigatorP32626.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
HAMAPMF_03117. Salvage_MtnC_euk.
InterProIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32626.
NextBio982690.
PROP32626.

Entry information

Entry nameENOPH_YEAST
AccessionPrimary (citable) accession number: P32626
Secondary accession number(s): D3DLL1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways