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B5VH97 (ENOPH_YEAS6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
ORF Names:AWRI1631_50320
OrganismSaccharomyces cerevisiae (strain AWRI1631) (Baker's yeast) [Complete proteome]
Taxonomic identifier545124 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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 By similarity. Nucleus By similarity.

Sequence similarities

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

Sequence caution

The sequence EDZ72697.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
Nucleus
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-methionine salvage from methylthioadenosine

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacireductone 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Enolase-phosphatase E1
PRO_0000377657

Regions

Region118 – 1192Substrate binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B5VH97 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: E29DD481FD450D49

FASTA22725,208
        10         20         30         40         50         60 
MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TKKVPQLVQQ DTRDSPVSNI LSQFHIDDKE 

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

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

       190        200        210        220 
VLFLSDNPLE LDAAAGVGIA TGLASRPGNA PVPDGQKYQV YKDFETL 

« Hide

References

[1]"Comparative genome analysis of a Saccharomyces cerevisiae wine strain."
Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.
FEMS Yeast Res. 8:1185-1195(2008) [PubMed: 18778279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AWRI1631.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ABSV01000631 Genomic DNA. Translation: EDZ72697.1. Different initiation.

3D structure databases

ProteinModelPortalB5VH97.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
IPR023214. HAD-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01691. Enolase-ppase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameENOPH_YEAS6
AccessionPrimary (citable) accession number: B5VH97
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 16, 2009
Last modified: June 28, 2011
This is version 19 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families