HSP33_YEAST
ID HSP33_YEAST Reviewed; 237 AA.
AC Q08914; D6W384;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable glutathione-independent glyoxalase HSP33 {ECO:0000250|UniProtKB:Q04432};
DE EC=4.2.1.130 {ECO:0000250|UniProtKB:Q04432};
DE AltName: Full=Glyoxalase 3 homolog 3 {ECO:0000250|UniProtKB:Q5AF03};
DE AltName: Full=Heat shock protein 33 {ECO:0000303|PubMed:14745011};
GN Name=HSP33 {ECO:0000303|PubMed:14745011};
GN OrderedLocusNames=YOR391C {ECO:0000312|SGD:S000005918};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP GENE NAME.
RX PubMed=14745011; DOI=10.1073/pnas.0308089100;
RA Wilson M.A., St Amour C.V., Collins J.L., Ringe D., Petsko G.A.;
RT "The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces
RT cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1531-1536(2004).
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24706893; DOI=10.1073/pnas.1319221111;
RA Miller-Fleming L., Antas P., Pais T.F., Smalley J.L., Giorgini F.,
RA Outeiro T.F.;
RT "Yeast DJ-1 superfamily members are required for diauxic-shift
RT reprogramming and cell survival in stationary phase.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7012-7017(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=21139195; DOI=10.1107/s1744309110039965;
RA Guo P.C., Zhou Y.Y., Ma X.X., Li W.F.;
RT "Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.";
RL Acta Crystallogr. F 66:1557-1561(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
RA Hwang K.Y., Sung M.W., Lee W.H.;
RT "Crystal structure of functionally unknown HSP33 from Saccharomyces
RT cerevisiae.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of methylglyoxal (MG) to D-lactate
CC in a single glutathione (GSH)-independent step. May play a role in
CC detoxifying endogenously produced glyoxals. Involved in protection
CC against reactive oxygen species (ROS) (By similarity). Important for
CC viability in stationary phase. May negatively regulate TORC1 in
CC response to nutrient limitation (PubMed:24706893).
CC {ECO:0000250|UniProtKB:Q04432, ECO:0000269|PubMed:24706893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC Evidence={ECO:0000250|UniProtKB:Q04432};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q04432}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q04432}.
CC Note=Present in processing bodies (P-bodies) and stress granule (SG)
CC foci upon glucose starvation and heat shock.
CC {ECO:0000250|UniProtKB:Q04432}.
CC -!- INDUCTION: Induced during entry into stationary phase.
CC {ECO:0000269|PubMed:24706893}.
CC -!- DISRUPTION PHENOTYPE: Results in higher sensitivity to oxidative
CC stress, reduced thermotolerance, accumulation of higher levels of
CC reactive oxygen species, and reduced chronological life span.
CC {ECO:0000269|PubMed:24706893}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
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DR EMBL; Z75299; CAA99723.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11150.1; -; Genomic_DNA.
DR RefSeq; NP_015036.3; NM_001183811.3.
DR PDB; 3KKL; X-ray; 2.03 A; A/B=1-237.
DR PDB; 3MII; X-ray; 2.40 A; A/B=1-237.
DR PDBsum; 3KKL; -.
DR PDBsum; 3MII; -.
DR AlphaFoldDB; Q08914; -.
DR SMR; Q08914; -.
DR BioGRID; 34772; 27.
DR IntAct; Q08914; 3.
DR MINT; Q08914; -.
DR STRING; 4932.YOR391C; -.
DR MEROPS; C56.A03; -.
DR MEROPS; C56.A04; -.
DR MaxQB; Q08914; -.
DR PaxDb; Q08914; -.
DR EnsemblFungi; YOR391C_mRNA; YOR391C; YOR391C.
DR GeneID; 854573; -.
DR KEGG; sce:YOR391C; -.
DR SGD; S000005918; HSP33.
DR VEuPathDB; FungiDB:YOR391C; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR GeneTree; ENSGT00940000176307; -.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q08914; -.
DR OMA; ASDYKVF; -.
DR BioCyc; YEAST:G3O-33852-MON; -.
DR EvolutionaryTrace; Q08914; -.
DR PRO; PR:Q08914; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08914; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0019172; F:glyoxalase III activity; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; ISA:SGD.
DR GO; GO:0031669; P:cellular response to nutrient levels; IMP:SGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISA:SGD.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IBA:GO_Central.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Reference proteome; Stress response.
FT CHAIN 1..237
FT /note="Probable glutathione-independent glyoxalase HSP33"
FT /id="PRO_0000270556"
FT ACT_SITE 138
FT /evidence="ECO:0000305|PubMed:21139195"
FT ACT_SITE 139
FT /evidence="ECO:0000305|PubMed:21139195"
FT ACT_SITE 170
FT /evidence="ECO:0000305|PubMed:21139195"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:3KKL"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3KKL"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3MII"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3MII"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3MII"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3KKL"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:3KKL"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:3KKL"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3KKL"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3KKL"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3KKL"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:3KKL"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3KKL"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:3KKL"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3KKL"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:3KKL"
SQ SEQUENCE 237 AA; 25926 MW; 0E817A44022231A6 CRC64;
MTPKRALISL TSYHGPFYKD GAKTGVFVVE ILRSFDTFEK HGFEVDFVSE TGGFGWDEHY
LPKSFIGGED KMNFETKNSA FNKALARIKT ANEVNASDYK VFFASAGHGA LFDYPKAKNL
QDIASKIYAN GGVIAAICHG PLLFDGLIDI KTTRPLIEGK AITGFPLEGE IALGVDDILR
SRKLTTVERV ANKNGAKYLA PIHPWDDYSI TDGKLVTGVN ANSSYSTTIR AINALYS
