HSP31_CANAL
ID HSP31_CANAL Reviewed; 236 AA.
AC Q5AF03; A0A1D8PJH1; Q5AEL7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glyoxalase 3 {ECO:0000303|PubMed:24302734};
DE EC=4.2.1.130 {ECO:0000269|PubMed:24302734};
DE AltName: Full=Glutathione-independent glyoxalase {ECO:0000303|PubMed:24302734};
GN Name=GLX3 {ECO:0000303|PubMed:24302734};
GN OrderedLocusNames=CAALFM_C302610CA;
GN ORFNames=CaO19.251, CaO19.7882, orf19.251, orf19.7882;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF CYS-136
RP AND HIS-137, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Catalyzes the conversion of methylglyoxal (MG) to D-lactate
CC in a single glutathione (GSH)-independent step. Selective for MG, does
CC not use glyoxal as substrate. Plays a role in detoxifying endogenously
CC produced MG, particularly when glycerol is the principal carbon source
CC (PubMed:24302734). Important for viability in stationary phase (By
CC similarity). {ECO:0000250|UniProtKB:Q04432,
CC ECO:0000269|PubMed:24302734}.
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};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 mM for methylglyoxal {ECO:0000269|PubMed:24302734};
CC Note=kcat is 7.8 sec(-1) with methylglyoxal as substrate.
CC {ECO:0000269|PubMed:24302734};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24302734}.
CC -!- DISRUPTION PHENOTYPE: Has a 3- to 5-fold increase in levels of
CC intracellular methylglyoxal compared with wild-type cells grown in the
CC same media. {ECO:0000269|PubMed:24302734}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017625; AOW28295.1; -; Genomic_DNA.
DR RefSeq; XP_719950.2; XM_714857.2.
DR PDB; 4LRU; X-ray; 1.60 A; A=1-236.
DR PDBsum; 4LRU; -.
DR AlphaFoldDB; Q5AF03; -.
DR SMR; Q5AF03; -.
DR STRING; 237561.Q5AF03; -.
DR GeneID; 3638325; -.
DR KEGG; cal:CAALFM_C302610CA; -.
DR CGD; CAL0000194072; GLX3.
DR VEuPathDB; FungiDB:C3_02610C_A; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q5AF03; -.
DR OrthoDB; 1305649at2759; -.
DR PHI-base; PHI:8693; -.
DR PRO; PR:Q5AF03; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0019172; F:glyoxalase III activity; IDA:CGD.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IDA:CGD.
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; Lyase; Oxidation; Reference proteome; Stress response.
FT CHAIN 1..236
FT /note="Glyoxalase 3"
FT /id="PRO_0000432110"
FT ACT_SITE 136
FT /evidence="ECO:0000305|PubMed:24302734"
FT ACT_SITE 137
FT /evidence="ECO:0000305|PubMed:24302734"
FT ACT_SITE 168
FT /evidence="ECO:0000305|PubMed:24302734"
FT MOD_RES 136
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT MUTAGEN 136
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:24302734"
FT MUTAGEN 137
FT /note="H->F: Reduces catalytic activity by 75%."
FT /evidence="ECO:0000269|PubMed:24302734"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 26..39
FT /evidence="ECO:0007829|PDB:4LRU"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4LRU"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4LRU"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:4LRU"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:4LRU"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4LRU"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4LRU"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:4LRU"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:4LRU"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4LRU"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:4LRU"
SQ SEQUENCE 236 AA; 25812 MW; 4C77E841710C4542 CRC64;
MVKVLLALTS YNETFYSDGK KTGVFVVEAL HPFEVFRKKG YEIQLASETG TFGWDDHSVV
PDFLNGEDKE IFDNVNSEFN VALKNLKKAS DLDPNDYDIF FGSAGHGTLF DYPNAKDLQK
IATTVYDKGG VVSAVCHGPA IFENLNDPKT GEPLIKGKKI TGFTDIGEDI LGVTDIMKKG
NLLTIKQVAE KEGATYIEPE GPWDNFTVTD GRIVTGVNPQ SAVKTAEDVI AAFECN
