SNO4_YEAST
ID SNO4_YEAST Reviewed; 237 AA.
AC Q04902; D6W0E9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable glutathione-independent glyoxalase SNO4 {ECO:0000250|UniProtKB:Q04432};
DE EC=4.2.1.130 {ECO:0000250|UniProtKB:Q04432};
DE AltName: Full=Glyoxalase 3 homolog 4 {ECO:0000250|UniProtKB:Q5AF03};
DE AltName: Full=Heat shock protein 34 {ECO:0000303|PubMed:14745011};
DE AltName: Full=SNZ proximal open reading frame 4 {ECO:0000303|PubMed:14566057};
GN Name=SNO4 {ECO:0000303|PubMed:14566057};
GN Synonyms=HSP34 {ECO:0000303|PubMed:14745011};
GN OrderedLocusNames=YMR322C {ECO:0000312|SGD:S000004941};
GN ORFNames=YM9924.14C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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=14566057; DOI=10.1073/pnas.2132527100;
RA Samanta M.P., Liang S.;
RT "Predicting protein functions from redundancies in large-scale protein
RT interaction networks.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12579-12583(2003).
RN [4]
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 [5]
RP 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).
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 -!- 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; Z54141; CAA90840.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10223.1; -; Genomic_DNA.
DR RefSeq; NP_014055.1; NM_001182835.1.
DR AlphaFoldDB; Q04902; -.
DR SMR; Q04902; -.
DR BioGRID; 35501; 88.
DR DIP; DIP-1968N; -.
DR IntAct; Q04902; 8.
DR MINT; Q04902; -.
DR STRING; 4932.YMR322C; -.
DR MEROPS; C56.A04; -.
DR MaxQB; Q04902; -.
DR PaxDb; Q04902; -.
DR PRIDE; Q04902; -.
DR EnsemblFungi; YMR322C_mRNA; YMR322C; YMR322C.
DR GeneID; 855372; -.
DR KEGG; sce:YMR322C; -.
DR SGD; S000004941; SNO4.
DR VEuPathDB; FungiDB:YMR322C; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR GeneTree; ENSGT00940000176307; -.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q04902; -.
DR OMA; DTIKSWN; -.
DR BioCyc; YEAST:G3O-32985-MON; -.
DR PRO; PR:Q04902; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04902; 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; IDA:SGD.
DR GO; GO:0031669; P:cellular response to nutrient levels; IMP: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 3: Inferred from homology;
KW Cytoplasm; Lyase; Reference proteome; Stress response.
FT CHAIN 1..237
FT /note="Probable glutathione-independent glyoxalase SNO4"
FT /id="PRO_0000157853"
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; 26040 MW; 004EA3E702332905 CRC64;
MTPKRALISL TSYHGPFYKD GAKTGVFVVE ILRSFDTFEK HGFEVDFVSE TGGFGWDEHY
LPKSFIGGED KMNFETKNSA FNKALARIKT ANEVNASDYK IFFASAGHGA LFDYPKAKNL
QDIASKIYAN GGVIAAICHG PLLFDGLIDI KTTRPLIEGK AITGFPLEGE IALGVDDILR
SRKLTTVERV ANKNRAKYLA PIHPWDDYSI TDGKLVTGVN ANSSYSTTIR AINALYS
