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P32626

- ENOPH_YEAST

UniProt

P32626 - ENOPH_YEAST

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
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    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

    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-SubCell
    2. nucleus Source: UniProtKB-SubCell

    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. 24 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.
    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

    MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TNKVPQLVQQ DTRDSPVSNI    50
    LSQFHIDNKE QLQAHILELV AKDVKDPILK QLQGYVWAHG YESGQIKAPV 100
    YADAIDFIKR KKRVFIYSSG SVKAQKLLFG YVQDPNAPAH DSLDLNSYID 150
    GYFDINTSGK KTETQSYANI LRDIGAKASE VLFLSDNPLE LDAAAGVGIA 200
    TGLASRPGNA PVPDGQKYQV YKNFETL 227
    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. 24 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.
    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

    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 1, 2014
    This is version 115 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