Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable glutathione-independent glyoxalase HSP33

Gene

HSP33

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed:24706893).By similarity1 Publication

Catalytic activityi

(R)-lactate = methylglyoxal + H2O.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 13811 Publication
Active sitei139 – 13911 Publication
Active sitei170 – 17011 Publication

GO - Molecular functioni

  • cysteine-type peptidase activity Source: SGD
  • lyase activity Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • cellular response to nutrient levels Source: SGD
  • proteolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-33852-MONOMER.

Protein family/group databases

MEROPSiC56.A03.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glutathione-independent glyoxalase HSP33By similarity (EC:4.2.1.130By similarity)
Alternative name(s):
Glyoxalase 3 homolog 3By similarity
Heat shock protein 331 Publication
Gene namesi
Name:HSP331 Publication
Ordered Locus Names:YOR391CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR391C.
SGDiS000005918. HSP33.

Subcellular locationi

  • CytoplasmP-body By similarity

  • Note: Present in processing bodies (P-bodies) and stress granule (SG) foci upon glucose starvation and heat shock.By similarity

GO - Cellular componenti

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Probable glutathione-independent glyoxalase HSP33PRO_0000270556Add
BLAST

Expressioni

Inductioni

Induced during entry into stationary phase.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi34772. 4 interactions.
IntActiQ08914. 3 interactions.
MINTiMINT-1605011.

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi28 – 3912Combined sources
Turni40 – 423Combined sources
Beta strandi44 – 529Combined sources
Helixi58 – 603Combined sources
Helixi62 – 654Combined sources
Helixi69 – 757Combined sources
Helixi82 – 865Combined 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
Turni173 – 1753Combined sources
Helixi176 – 1816Combined sources
Helixi187 – 1926Combined sources
Turni193 – 1953Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2206Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 23512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KKLX-ray2.03A/B1-237[»]
3MIIX-ray2.40A/B1-237[»]
ProteinModelPortaliQ08914.
SMRiQ08914. Positions 4-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08914.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000181653.
InParanoidiQ08914.
OrthoDBiEOG73547H.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.

Sequencei

Sequence statusi: Complete.

Q08914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPKRALISL TSYHGPFYKD GAKTGVFVVE ILRSFDTFEK HGFEVDFVSE
60 70 80 90 100
TGGFGWDEHY LPKSFIGGED KMNFETKNSA FNKALARIKT ANEVNASDYK
110 120 130 140 150
VFFASAGHGA LFDYPKAKNL QDIASKIYAN GGVIAAICHG PLLFDGLIDI
160 170 180 190 200
KTTRPLIEGK AITGFPLEGE IALGVDDILR SRKLTTVERV ANKNGAKYLA
210 220 230
PIHPWDDYSI TDGKLVTGVN ANSSYSTTIR AINALYS
Length:237
Mass (Da):25,926
Last modified:November 1, 1996 - v1
Checksum:i0E817A44022231A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75299 Genomic DNA. Translation: CAA99723.1.
BK006948 Genomic DNA. Translation: DAA11150.1.
RefSeqiNP_015036.3. NM_001183811.3.

Genome annotation databases

EnsemblFungiiYOR391C; YOR391C; YOR391C.
GeneIDi854573.
KEGGisce:YOR391C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75299 Genomic DNA. Translation: CAA99723.1.
BK006948 Genomic DNA. Translation: DAA11150.1.
RefSeqiNP_015036.3. NM_001183811.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KKLX-ray2.03A/B1-237[»]
3MIIX-ray2.40A/B1-237[»]
ProteinModelPortaliQ08914.
SMRiQ08914. Positions 4-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34772. 4 interactions.
IntActiQ08914. 3 interactions.
MINTiMINT-1605011.

Protein family/group databases

MEROPSiC56.A03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR391C; YOR391C; YOR391C.
GeneIDi854573.
KEGGisce:YOR391C.

Organism-specific databases

EuPathDBiFungiDB:YOR391C.
SGDiS000005918. HSP33.

Phylogenomic databases

HOGENOMiHOG000181653.
InParanoidiQ08914.
OrthoDBiEOG73547H.

Enzyme and pathway databases

BioCyciYEAST:G3O-33852-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ08914.
NextBioi977030.
PROiQ08914.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(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. "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: GENE NAME.
  4. "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.
  5. "Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae."
    Guo P.C., Zhou Y.Y., Ma X.X., Li W.F.
    Acta Crystallogr. F 66:1557-1561(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ACTIVE SITE.
  6. "Crystal structure of functionally unknown HSP33 from Saccharomyces cerevisiae."
    Hwang K.Y., Sung M.W., Lee W.H.
    Submitted (MAR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).

Entry informationi

Entry nameiHSP33_YEAST
AccessioniPrimary (citable) accession number: Q08914
Secondary accession number(s): D6W384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.