Enolase-phosphatase E1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32626 (ENOPH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	5-(methylthio)-2,3-dioxopentyl phosphate + H₂O = 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 Ref.5.
Miscellaneous	Present with 2850 molecules/cell in log phase SD medium. Ref.6
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.

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 Reference proteome
Gene Ontology (GO)
Biological process	L-methionine salvage from methylthioadenosine Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay Ref.5. Source: SGD nucleus Inferred from direct assay Ref.5. Source: SGD
Molecular function	acireductone synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 227

227

Enolase-phosphatase E1

PRO_0000065746

Regions

Region

118 – 119

Substrate binding By similarity

Sites

Metal binding

Magnesium

Metal binding

Magnesium; via carbonyl oxygen

Metal binding

186

Magnesium

Binding site

161

Substrate By similarity

Experimental info

Sequence conflict

56 – 57

ID → MH in AAA34939. Ref.1

Sequence conflict

56 – 57

ID → MH in AAD13973. Ref.1

Sequence conflict

56 – 57

ID → MH in AAB28443. Ref.1

Sequence conflict

179

S → T in AAA34939. Ref.1

Sequence conflict

179

S → T in AAD13973. Ref.1

Sequence conflict

179

S → T in AAB28443. Ref.1

Secondary structure

227

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32626 [UniParc].

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

FASTA

227

25,187

        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' 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 12748633] [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: 14562095] [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: 14562106] [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.

PIR

S30843.

RefSeq

NP_010876.2. NM_001178853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G80	X-ray	2.28	A/B/C/D	1-227	[»]

ProteinModelPortal

P32626.

SMR

P32626. Positions 3-227.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5487N.

MINT

MINT-513487.

STRING

P32626.

Proteomic databases

PeptideAtlas

P32626.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YEL038W; YEL038W; YEL038W.

GeneID

856673.

KEGG

sce:YEL038W.

NMPDR

fig|4932.3.peg.1927.

Organism-specific databases

SGD

S000000764. UTR4.

Phylogenomic databases

eggNOG

fuNOG09254.

GeneTree

EFGT00050000008472.

HOGENOM

HBG294242.

OMA

TTDLNFI.

OrthoDB

EOG4NZZ3B.

Gene expression databases

ArrayExpress

P32626.

Genevestigator

P32626.

GermOnline

YEL038W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
IPR023214. HAD-like_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.

K09880.

Pfam

PF00702. Hydrolase. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01691. Enolase-ppase. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ENOPH_YEAST

Accession

Primary (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:	December 14, 2011
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents