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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)DescriptionActionsGraphical viewLength
Active sitei1381 Publication1
Active sitei1391 Publication1
Active sitei1701 Publication1

GO - Molecular functioni

  • cysteine-type peptidase activity Source: SGD
  • glyoxalase III activity Source: GO_Central
  • unfolded protein binding Source: SGD

GO - Biological processi

  • cellular response to nutrient levels Source: SGD
  • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: GO_Central
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)DescriptionActionsGraphical viewLength
ChainiPRO_00002705561 – 237Probable glutathione-independent glyoxalase HSP33Add BLAST237

Proteomic databases

MaxQBiQ08914.

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 interactors.
IntActiQ08914. 3 interactors.
MINTiMINT-1605011.

Structurei

Secondary structure

1237
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi28 – 39Combined sources12
Turni40 – 42Combined sources3
Beta strandi44 – 52Combined sources9
Helixi58 – 60Combined sources3
Helixi62 – 65Combined sources4
Helixi69 – 75Combined sources7
Helixi82 – 86Combined sources5
Helixi91 – 93Combined sources3
Helixi96 – 98Combined sources3
Beta strandi100 – 104Combined sources5
Helixi110 – 113Combined sources4
Helixi114 – 116Combined sources3
Helixi118 – 129Combined sources12
Beta strandi133 – 137Combined sources5
Helixi140 – 144Combined sources5
Turni150 – 152Combined sources3
Beta strandi153 – 155Combined sources3
Turni156 – 159Combined sources4
Helixi167 – 172Combined sources6
Turni173 – 175Combined sources3
Helixi176 – 181Combined sources6
Helixi187 – 192Combined sources6
Turni193 – 195Combined sources3
Beta strandi209 – 212Combined sources4
Beta strandi215 – 220Combined sources6
Helixi221 – 223Combined sources3
Helixi224 – 235Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ08914.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000181653.
InParanoidiQ08914.
OrthoDBiEOG092C4O4J.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KKLX-ray2.03A/B1-237[»]
3MIIX-ray2.40A/B1-237[»]
ProteinModelPortaliQ08914.
SMRiQ08914.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiC56.A03.

Proteomic databases

MaxQBiQ08914.

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.
OrthoDBiEOG092C4O4J.

Enzyme and pathway databases

BioCyciYEAST:G3O-33852-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ08914.
PROiQ08914.

Family and domain databases

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

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: November 2, 2016
This is version 93 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.