HSP31_YEAST
ID HSP31_YEAST Reviewed; 237 AA.
AC Q04432; D6VTF4; E9P8V9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glutathione-independent glyoxalase HSP31 {ECO:0000303|PubMed:24302734};
DE EC=4.2.1.130 {ECO:0000269|PubMed:24302734, ECO:0000269|PubMed:24758716};
DE AltName: Full=Glyoxalase 3 homolog 1 {ECO:0000250|UniProtKB:Q5AF03};
DE AltName: Full=Heat shock protein 31 {ECO:0000303|PubMed:14745011};
GN Name=HSP31 {ECO:0000303|PubMed:14745011};
GN OrderedLocusNames=YDR533C {ECO:0000312|SGD:S000002941}; ORFNames=D9719.36;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP LACK OF PROTEASE ACTIVITY.
RX PubMed=12855764; DOI=10.1073/pnas.1133288100;
RA Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.;
RT "The 1.1-A resolution crystal structure of DJ-1, the protein mutated in
RT autosomal recessive early onset Parkinson's disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17395014; DOI=10.1016/j.freeradbiomed.2007.01.042;
RA Skoneczna A., Micialkiewicz A., Skoneczny M.;
RT "Saccharomyces cerevisiae Hsp31p, a stress response protein conferring
RT protection against reactive oxygen species.";
RL Free Radic. Biol. Med. 42:1409-1420(2007).
RN [7]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24758716; DOI=10.1186/1471-2148-14-86;
RA Zhao Q., Su Y., Wang Z., Chen C., Wu T., Huang Y.;
RT "Identification of glutathione (GSH)-independent glyoxalase III from
RT Schizosaccharomyces pombe.";
RL BMC Evol. Biol. 14:86-86(2014).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24302734; DOI=10.1074/jbc.m113.505784;
RA Hasim S., Hussin N.A., Alomar F., Bidasee K.R., Nickerson K.W.,
RA Wilson M.A.;
RT "A glutathione-independent glyoxalase of the DJ-1 superfamily plays an
RT important role in managing metabolically generated methylglyoxal in Candida
RT albicans.";
RL J. Biol. Chem. 289:1662-1674(2014).
RN [9]
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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), OXIDATION AT CYS-138, SUBUNIT, AND
RP ACTIVE SITE.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=15130476; DOI=10.1016/j.str.2004.02.030;
RA Graille M., Quevillon-Cheruel S., Leulliot N., Zhou C.-Z.,
RA de la Sierra Gallay I.L., Jacquamet L., Ferrer J.-L., Liger D., Poupon A.,
RA Janin J., van Tilbeurgh H.;
RT "Crystal structure of the YDR533c S. cerevisiae protein, a class II member
RT of the Hsp31 family.";
RL Structure 12:839-847(2004).
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 (PubMed:24302734). Involved
CC in protection against reactive oxygen species (ROS) (PubMed:17395014).
CC Important for viability in stationary phase. May negatively regulate
CC TORC1 in response to nutrient limitation (PubMed:24706893).
CC {ECO:0000269|PubMed:17395014, ECO:0000269|PubMed:24302734,
CC 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:0000269|PubMed:24302734, ECO:0000269|PubMed:24758716};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for methylglyoxal {ECO:0000269|PubMed:24758716};
CC Note=kcat is 75.0 min(-1) with methylglyoxal as substrate.
CC {ECO:0000269|PubMed:24758716};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14745011,
CC ECO:0000269|PubMed:15130476}.
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: Up-regulated 10- to 30-fold during entry into stationary
CC phase, by hydrogen peroxide or diamide stress, by heat stress, and by
CC growth in the presence of the proline analog azetidine-2-carboxylic
CC acid. {ECO:0000269|PubMed:17395014, ECO:0000269|PubMed:24706893}.
CC -!- PTM: Cys-138 is easily oxidized to sulfinic acid.
CC {ECO:0000269|PubMed:14745011}.
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:17395014, ECO:0000269|PubMed:24706893}.
CC -!- MISCELLANEOUS: No protease activity could be detected.
CC {ECO:0000269|PubMed:12855764}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
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DR EMBL; U33057; AAB64972.1; -; Genomic_DNA.
DR EMBL; AY558337; AAS56663.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12364.1; -; Genomic_DNA.
DR PIR; S69588; S69588.
DR RefSeq; NP_010822.1; NM_001180841.1.
DR PDB; 1QVV; X-ray; 2.35 A; A/B/C/D=1-237.
DR PDB; 1QVW; X-ray; 1.90 A; A/B=1-237.
DR PDB; 1QVZ; X-ray; 1.85 A; A/B=1-237.
DR PDB; 4QYX; X-ray; 1.69 A; A=1-237.
DR PDBsum; 1QVV; -.
DR PDBsum; 1QVW; -.
DR PDBsum; 1QVZ; -.
DR PDBsum; 4QYX; -.
DR AlphaFoldDB; Q04432; -.
DR SMR; Q04432; -.
DR BioGRID; 32582; 80.
DR DIP; DIP-4315N; -.
DR IntAct; Q04432; 2.
DR MINT; Q04432; -.
DR STRING; 4932.YDR533C; -.
DR MEROPS; C56.004; -.
DR MaxQB; Q04432; -.
DR PaxDb; Q04432; -.
DR PRIDE; Q04432; -.
DR TopDownProteomics; Q04432; -.
DR EnsemblFungi; YDR533C_mRNA; YDR533C; YDR533C.
DR GeneID; 852146; -.
DR KEGG; sce:YDR533C; -.
DR SGD; S000002941; HSP31.
DR VEuPathDB; FungiDB:YDR533C; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR GeneTree; ENSGT00940000176307; -.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q04432; -.
DR OMA; ALHPYNV; -.
DR BioCyc; YEAST:G3O-30044-MON; -.
DR BRENDA; 4.2.1.130; 984.
DR EvolutionaryTrace; Q04432; -.
DR PRO; PR:Q04432; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04432; 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; IDA:SGD.
DR GO; GO:0044183; F:protein folding chaperone; IDA:SGD.
DR GO; GO:0031669; P:cellular response to nutrient levels; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:SGD.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IDA:SGD.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Oxidation; Reference proteome;
KW Stress response.
FT CHAIN 1..237
FT /note="Glutathione-independent glyoxalase HSP31"
FT /id="PRO_0000157852"
FT ACT_SITE 138
FT /evidence="ECO:0000305|PubMed:14745011,
FT ECO:0000305|PubMed:15130476"
FT ACT_SITE 139
FT /evidence="ECO:0000305|PubMed:14745011,
FT ECO:0000305|PubMed:15130476"
FT ACT_SITE 170
FT /evidence="ECO:0000305|PubMed:14745011,
FT ECO:0000305|PubMed:15130476"
FT MOD_RES 138
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000269|PubMed:14745011"
FT CONFLICT 31
FT /note="A -> T (in Ref. 3; AAS56663)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1QVZ"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4QYX"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:4QYX"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4QYX"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:4QYX"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4QYX"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:4QYX"
SQ SEQUENCE 237 AA; 25670 MW; 088697FB888DF7D5 CRC64;
MAPKKVLLAL TSYNDVFYSD GAKTGVFVVE ALHPFNTFRK EGFEVDFVSE TGKFGWDEHS
LAKDFLNGQD ETDFKNKDSD FNKTLAKIKT PKEVNADDYQ IFFASAGHGT LFDYPKAKDL
QDIASEIYAN GGVVAAVCHG PAIFDGLTDK KTGRPLIEGK SITGFTDVGE TILGVDSILK
AKNLATVEDV AKKYGAKYLA PVGPWDDYSI TDGRLVTGVN PASAHSTAVR SIDALKN
