Enolase-phosphatase E1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32626 (ENOPH_YEAST)

Last modified November 25, 2008. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Bifunctional enzyme that enolizes the substrate to form the intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one By similarity.
Catalytic activity	5-(methylthio)-2,3-dioxopentyl phosphate + H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
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. 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.
Subcellular location	Cytoplasm. Nucleus.
Miscellaneous	Present with 2850 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. MasA family.
Sequence caution	The sequence AAA34939.1 differs from that shown. Reason: Frameshift at positions 153 and 230. The sequence AAB28443.1 differs from that shown. Reason: Frameshift at positions 153 and 230. The sequence AAD13973.1 differs from that shown. Reason: Frameshift at positions 153 and 230.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine salvage Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.3 Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.3 Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acireductone synthase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglycolate phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 241

241

Enolase-phosphatase E1

PRO_0000065746

Regions

Region

132 – 133

Substrate binding By similarity

Sites

Metal binding

Magnesium

Metal binding

Magnesium; via carbonyl oxygen

Metal binding

200

Magnesium

Binding site

175

Substrate By similarity

Experimental info

Sequence conflict

70 – 71

ID → MH in AAA34939, AAD13973 and AAB28443. Ref.1

Sequence conflict

193

S → T in AAA34939, AAD13973 and AAB28443. Ref.1

Secondary structure

241

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P32626-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: BF6FBBC7FB14B5AD
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FASTA

241

26,735

        10         20         30         40         50         60 
MVIGQKVLLA RIPKMGDNYS TYLLDIEGTV CPISFVKETL FPYFTNKVPQ LVQQDTRDSP 

        70         80         90        100        110        120 
VSNILSQFHI DNKEQLQAHI LELVAKDVKD PILKQLQGYV WAHGYESGQI KAPVYADAID 

       130        140        150        160        170        180 
FIKRKKRVFI YSSGSVKAQK LLFGYVQDPN APAHDSLDLN SYIDGYFDIN TSGKKTETQS 

       190        200        210        220        230        240 
YANILRDIGA KASEVLFLSD NPLELDAAAG VGIATGLASR PGNAPVPDGQ KYQVYKNFET 


L

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References

	« Hide 'large scale' referencesShow '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: 8411151] [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. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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.

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Cross-references

Sequence databases

L22173 Genomic DNA. Translation: AAA34939.1. Frameshift.
S65964 Genomic DNA. Translation: AAD13973.1. Frameshift.
S66121 mRNA. Translation: AAB28443.1. Frameshift.
U18779 Genomic DNA. Translation: AAB65004.1.

PIR

S30843.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G80	X-ray	2.28	A/B/C/D	1-241	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5487N.

IntAct

P32626.

Proteomic databases

PeptideAtlas

P32626.

Genome annotation databases

Ensembl

YEL038W. Saccharomyces cerevisiae. [Contig view]

GenomeReviews

Gene locus YEL038W in contig U00092_GR.

NMPDR

fig|4932.3.peg.1927.

Organism-specific databases

CYGD

YEL038w.

SGD

S000000764. UTR4.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P32626.

Gene expression databases

GermOnline

YEL038W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
IPR006439. HAD-SF_hydro_IA_v1.
[Graphical view]

PANTHER

PTHR20371. Enolase_ppase. 1 hit.

Pfam

PF00702. Hydrolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.

ProtoNet

Search...

Other Resources

LinkHub

P32626.

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Entry information

Entry name

ENOPH_YEAST

Accession

Primary (citable) accession number: P32626

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

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

Yeast

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

Yeast chromosome V

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents