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Protein

Glutathione-independent glyoxalase HSP31

Gene

HSP31

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals (PubMed:24302734). Involved in protection against reactive oxygen species (ROS) (PubMed:17395014). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed:24706893).3 Publications

Catalytic activityi

(R)-lactate = methylglyoxal + H2O.2 Publications

Kineticsi

kcat is 75.0 min(-1) with methylglyoxal as substrate.1 Publication

  1. KM=1.5 mM for methylglyoxal1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei138 – 13812 Publications
    Active sitei139 – 13912 Publications
    Active sitei170 – 17012 Publications

    GO - Molecular functioni

    • glyoxalase III activity Source: SGD

    GO - Biological processi

    • cellular response to nutrient levels Source: SGD
    • cellular response to oxidative stress Source: SGD
    • lactate biosynthetic process Source: GOC
    • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30044-MONOMER.

    Protein family/group databases

    MEROPSiC56.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione-independent glyoxalase HSP311 Publication (EC:4.2.1.1302 Publications)
    Alternative name(s):
    Glyoxalase 3 homolog 1By similarity
    Heat shock protein 311 Publication
    Gene namesi
    Name:HSP311 Publication
    Ordered Locus Names:YDR533CImported
    ORF Names:D9719.36
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDR533C.
    SGDiS000002941. HSP31.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasmic mRNA processing body Source: SGD
    • cytoplasmic stress granule Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Results in higher sensitivity to oxidative stress, reduced thermotolerance, accumulation of higher levels of reactive oxygen species, and reduced chronological life span.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 237237Glutathione-independent glyoxalase HSP31PRO_0000157852Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei138 – 1381Cysteine sulfinic acid (-SO2H)1 Publication

    Post-translational modificationi

    Cys-138 is easily oxidized to sulfinic acid.1 Publication

    Keywords - PTMi

    Oxidation

    Proteomic databases

    MaxQBiQ04432.
    PeptideAtlasiQ04432.
    TopDownProteomicsiQ04432.

    Expressioni

    Inductioni

    Up-regulated 10- to 30-fold during entry into stationary phase, by hydrogen peroxide or diamide stress, by heat stress, and by growth in the presence of the proline analog azetidine-2-carboxylic acid.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi32582. 18 interactions.
    DIPiDIP-4315N.
    IntActiQ04432. 3 interactions.
    MINTiMINT-525838.

    Structurei

    Secondary structure

    1
    237
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106Combined sources
    Helixi28 – 4013Combined sources
    Beta strandi44 – 496Combined sources
    Beta strandi50 – 523Combined sources
    Helixi58 – 614Combined sources
    Turni63 – 653Combined sources
    Helixi68 – 758Combined sources
    Helixi80 – 856Combined sources
    Helixi91 – 933Combined sources
    Helixi96 – 983Combined sources
    Beta strandi100 – 1045Combined sources
    Helixi110 – 1134Combined sources
    Helixi114 – 1163Combined sources
    Helixi118 – 12912Combined sources
    Beta strandi133 – 1375Combined sources
    Helixi140 – 1445Combined sources
    Turni150 – 1523Combined sources
    Beta strandi153 – 1553Combined sources
    Turni156 – 1594Combined sources
    Helixi167 – 1726Combined sources
    Helixi176 – 1816Combined sources
    Helixi187 – 1937Combined sources
    Beta strandi209 – 2124Combined sources
    Beta strandi215 – 2184Combined sources
    Helixi221 – 2233Combined sources
    Helixi224 – 23512Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QVVX-ray2.35A/B/C/D1-237[»]
    1QVWX-ray1.90A/B1-237[»]
    1QVZX-ray1.85A/B1-237[»]
    4QYXX-ray1.69A1-237[»]
    ProteinModelPortaliQ04432.
    SMRiQ04432. Positions 2-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04432.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00390000013431.
    HOGENOMiHOG000181653.
    InParanoidiQ04432.
    OMAiPWRIEDE.
    OrthoDBiEOG73547H.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR002818. DJ-1/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q04432-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAPKKVLLAL TSYNDVFYSD GAKTGVFVVE ALHPFNTFRK EGFEVDFVSE
    60 70 80 90 100
    TGKFGWDEHS LAKDFLNGQD ETDFKNKDSD FNKTLAKIKT PKEVNADDYQ
    110 120 130 140 150
    IFFASAGHGT LFDYPKAKDL QDIASEIYAN GGVVAAVCHG PAIFDGLTDK
    160 170 180 190 200
    KTGRPLIEGK SITGFTDVGE TILGVDSILK AKNLATVEDV AKKYGAKYLA
    210 220 230
    PVGPWDDYSI TDGRLVTGVN PASAHSTAVR SIDALKN
    Length:237
    Mass (Da):25,670
    Last modified:November 1, 1996 - v1
    Checksum:i088697FB888DF7D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311A → T in AAS56663 (PubMed:17322287).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U33057 Genomic DNA. Translation: AAB64972.1.
    AY558337 Genomic DNA. Translation: AAS56663.1.
    BK006938 Genomic DNA. Translation: DAA12364.1.
    PIRiS69588.
    RefSeqiNP_010822.1. NM_001180841.1.

    Genome annotation databases

    EnsemblFungiiYDR533C; YDR533C; YDR533C.
    GeneIDi852146.
    KEGGisce:YDR533C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U33057 Genomic DNA. Translation: AAB64972.1.
    AY558337 Genomic DNA. Translation: AAS56663.1.
    BK006938 Genomic DNA. Translation: DAA12364.1.
    PIRiS69588.
    RefSeqiNP_010822.1. NM_001180841.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QVVX-ray2.35A/B/C/D1-237[»]
    1QVWX-ray1.90A/B1-237[»]
    1QVZX-ray1.85A/B1-237[»]
    4QYXX-ray1.69A1-237[»]
    ProteinModelPortaliQ04432.
    SMRiQ04432. Positions 2-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32582. 18 interactions.
    DIPiDIP-4315N.
    IntActiQ04432. 3 interactions.
    MINTiMINT-525838.

    Protein family/group databases

    MEROPSiC56.004.

    Proteomic databases

    MaxQBiQ04432.
    PeptideAtlasiQ04432.
    TopDownProteomicsiQ04432.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDR533C; YDR533C; YDR533C.
    GeneIDi852146.
    KEGGisce:YDR533C.

    Organism-specific databases

    EuPathDBiFungiDB:YDR533C.
    SGDiS000002941. HSP31.

    Phylogenomic databases

    GeneTreeiENSGT00390000013431.
    HOGENOMiHOG000181653.
    InParanoidiQ04432.
    OMAiPWRIEDE.
    OrthoDBiEOG73547H.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30044-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ04432.
    NextBioi970567.
    PROiQ04432.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR002818. DJ-1/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease."
      Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF PROTEASE ACTIVITY.
    6. "Saccharomyces cerevisiae Hsp31p, a stress response protein conferring protection against reactive oxygen species."
      Skoneczna A., Micialkiewicz A., Skoneczny M.
      Free Radic. Biol. Med. 42:1409-1420(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
    7. "Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe."
      Zhao Q., Su Y., Wang Z., Chen C., Wu T., Huang Y.
      BMC Evol. Biol. 14:86-86(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans."
      Hasim S., Hussin N.A., Alomar F., Bidasee K.R., Nickerson K.W., Wilson M.A.
      J. Biol. Chem. 289:1662-1674(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "Yeast DJ-1 superfamily members are required for diauxic-shift reprogramming and cell survival in stationary phase."
      Miller-Fleming L., Antas P., Pais T.F., Smalley J.L., Giorgini F., Outeiro T.F.
      Proc. Natl. Acad. Sci. U.S.A. 111:7012-7017(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
    10. "The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily."
      Wilson M.A., St Amour C.V., Collins J.L., Ringe D., Petsko G.A.
      Proc. Natl. Acad. Sci. U.S.A. 101:1531-1536(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), OXIDATION AT CYS-138, SUBUNIT, ACTIVE SITE.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiHSP31_YEAST
    AccessioniPrimary (citable) accession number: Q04432
    Secondary accession number(s): D6VTF4, E9P8V9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: November 1, 1996
    Last modified: May 11, 2016
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    No protease activity could be detected.1 Publication
    Present with 358 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.