HSP32_YEAST
ID HSP32_YEAST Reviewed; 237 AA.
AC Q08992; D6W392;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable glutathione-independent glyoxalase HSP32 {ECO:0000250|UniProtKB:Q04432};
DE EC=4.2.1.130 {ECO:0000250|UniProtKB:Q04432};
DE AltName: Full=Glyoxalase 3 homolog 2 {ECO:0000250|UniProtKB:Q5AF03};
DE AltName: Full=Heat shock protein 32 {ECO:0000303|PubMed:14745011};
GN Name=HSP32 {ECO:0000303|PubMed:14745011};
GN OrderedLocusNames=YPL280W {ECO:0000312|SGD:S000006201};
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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).
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:0000269|PubMed:24706893}.
CC Note=Present in processing bodies (P-bodies) and stress granule (SG)
CC foci upon glucose starvation and heat shock.
CC {ECO:0000269|PubMed:24706893}.
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; Z73636; CAA98017.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11158.1; -; Genomic_DNA.
DR PIR; S65313; S65313.
DR RefSeq; NP_015043.1; NM_001184094.1.
DR AlphaFoldDB; Q08992; -.
DR SMR; Q08992; -.
DR BioGRID; 35935; 155.
DR DIP; DIP-3919N; -.
DR IntAct; Q08992; 3.
DR MINT; Q08992; -.
DR STRING; 4932.YPL280W; -.
DR MEROPS; C56.A03; -.
DR MEROPS; C56.A04; -.
DR MaxQB; Q08992; -.
DR PaxDb; Q08992; -.
DR EnsemblFungi; YPL280W_mRNA; YPL280W; YPL280W.
DR GeneID; 855849; -.
DR KEGG; sce:YPL280W; -.
DR SGD; S000006201; HSP32.
DR VEuPathDB; FungiDB:YPL280W; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR GeneTree; ENSGT00940000176307; -.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q08992; -.
DR OMA; NSAYNIA; -.
DR BioCyc; YEAST:G3O-34161-MON; -.
DR PRO; PR:Q08992; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08992; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
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:0051596; P:methylglyoxal catabolic process; IGI: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 2: Evidence at transcript level;
KW Cytoplasm; Lyase; Reference proteome; Stress response.
FT CHAIN 1..237
FT /note="Probable glutathione-independent glyoxalase HSP32"
FT /id="PRO_0000270555"
FT ACT_SITE 138
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 170
FT /evidence="ECO:0000250|UniProtKB:Q04432"
SQ SEQUENCE 237 AA; 25940 MW; 004EB2E702222905 CRC64;
MTPKRALISL TSYHGPFYKD GAKTGVFVVE ILRSFDTFEK HGFEVDFVSE TGGFGWDEHY
LPKSFIGGED KMNFETKNSA FNKALARIKT ANEVNASDYK IFFASAGHGA LFDYPKAKNL
QDIASKIYAN GGVIAAICHG PLLFDGLIDI KTTRPLIEGK AITGFPLEGE IALGVDDILR
SRKLTTVERV ANKNGAKYLA PIHPWDDYSI TDGKLVTGVN ANSSYSTTIR AINALYS
