LGUL_YEAST
ID LGUL_YEAST Reviewed; 326 AA.
AC P50107; D6VZH1; Q9HFG0; Q9URB5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glyoxalase I {ECO:0000303|PubMed:8824231};
DE Short=Glx I {ECO:0000303|PubMed:8824231};
DE EC=4.4.1.5 {ECO:0000269|PubMed:11050082, ECO:0000269|PubMed:8824231};
DE AltName: Full=Aldoketomutase {ECO:0000305};
DE AltName: Full=Ketone-aldehyde mutase {ECO:0000305};
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
DE AltName: Full=actoylglutathione lyase;
GN Name=GLO1 {ECO:0000303|PubMed:8824231}; OrderedLocusNames=YML004C;
GN ORFNames=YM9571.15C;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8824231; DOI=10.1074/jbc.271.42.26194;
RA Inoue Y., Kimura A.;
RT "Identification of the structural gene for glyoxalase I from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 271:25958-25965(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, SUBUNIT, AND PATHWAY.
RX PubMed=11050082; DOI=10.1074/jbc.m005760200;
RA Frickel E.M., Jemth P., Widersten M., Mannervik B.;
RT "Yeast glyoxalase I is a monomeric enzyme with two active sites.";
RL J. Biol. Chem. 276:1845-1849(2001).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 310-326, AND PROTEIN SEQUENCE OF
RP 39-45; 150-165 AND 311-323.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=1777125;
RA Inoue Y., Yano H., Ginya H., Tsuchiyama H., Murata K., Kimura A.;
RT "Positive effect of GAC gene product on the mRNA level of glyoxalase I gene
RT in Saccharomyces cerevisiae.";
RL Biotechnol. Appl. Biochem. 14:391-394(1991).
RN [6]
RP DISCUSSION OF SEQUENCE.
RX PubMed=8670139; DOI=10.1042/bj3161005;
RA Ridderstroem M., Mannervik B.;
RT "The primary structure of monomeric yeast glyoxalase I indicates a gene
RT duplication resulting in two similar segments homologous with the subunit
RT of dimeric human glyoxalase I.";
RL Biochem. J. 316:1005-1006(1996).
RN [7]
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).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione
CC (PubMed:11050082, PubMed:8824231). Can use gamma-glutamylcysteine as a
CC substrate (PubMed:8824231). {ECO:0000269|PubMed:11050082,
CC ECO:0000269|PubMed:8824231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000269|PubMed:11050082,
CC ECO:0000269|PubMed:8824231};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04760};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q04760};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for glutathione {ECO:0000269|PubMed:8824231};
CC KM=1.2 mM for gamma-glutamylcysteine {ECO:0000269|PubMed:8824231};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2. {ECO:0000269|PubMed:11050082,
CC ECO:0000269|PubMed:8824231}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11050082}.
CC -!- MISCELLANEOUS: Present with 2570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; X99240; CAA67622.1; -; Genomic_DNA.
DR EMBL; AJ297938; CAC16163.1; -; Genomic_DNA.
DR EMBL; Z49810; CAA89948.1; -; Genomic_DNA.
DR EMBL; S80483; AAB21302.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09895.1; -; Genomic_DNA.
DR PIR; S55115; S55115.
DR RefSeq; NP_013710.1; NM_001182359.1.
DR AlphaFoldDB; P50107; -.
DR SMR; P50107; -.
DR BioGRID; 35167; 46.
DR STRING; 4932.YML004C; -.
DR BindingDB; P50107; -.
DR ChEMBL; CHEMBL6057; -.
DR iPTMnet; P50107; -.
DR MaxQB; P50107; -.
DR PaxDb; P50107; -.
DR PRIDE; P50107; -.
DR EnsemblFungi; YML004C_mRNA; YML004C; YML004C.
DR GeneID; 855009; -.
DR KEGG; sce:YML004C; -.
DR SGD; S000004463; GLO1.
DR VEuPathDB; FungiDB:YML004C; -.
DR eggNOG; KOG2944; Eukaryota.
DR GeneTree; ENSGT00390000012340; -.
DR HOGENOM; CLU_046006_0_1_1; -.
DR InParanoid; P50107; -.
DR OMA; MGDAWGH; -.
DR BioCyc; MetaCyc:YML004C-MON; -.
DR BioCyc; YEAST:YML004C-MON; -.
DR Reactome; R-SCE-70268; Pyruvate metabolism.
DR SABIO-RK; P50107; -.
DR UniPathway; UPA00619; UER00675.
DR PRO; PR:P50107; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50107; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:SGD.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IDA:SGD.
DR Gene3D; 3.10.180.10; -; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; SSF54593; 2.
DR TIGRFAMs; TIGR00068; glyox_I; 2.
DR PROSITE; PS00934; GLYOXALASE_I_1; 2.
DR PROSITE; PS00935; GLYOXALASE_I_2; 2.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Metal-binding; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..326
FT /note="Glyoxalase I"
FT /id="PRO_0000168087"
FT DOMAIN 22..167
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 182..322
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 163
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:11050082"
FT ACT_SITE 318
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:11050082"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 93
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 113
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 117
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 147..148
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT CONFLICT 36
FT /note="T -> A (in Ref. 2; CAC16163)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="G -> D (in Ref. 2; CAC16163 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="H -> Y (in Ref. 2; CAC16163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37209 MW; 9726A8253F53FB2B CRC64;
MSTDSTRYPI QIEKASNDPT LLLNHTCLRV KDPARTVKFY TEHFGMKLLS RKDFEEAKFS
LYFLSFPKDD IPKNKNGEPD VFSAHGVLEL THNWGTEKNP DYKINNGNEE PHRGFGHICF
SVSDINKTCE ELESQGVKFK KRLSEGRQKD IAFALGPDGY WIELITYSRE GQEYPKGSVG
NKFNHTMIRI KNPTRSLEFY QNVLGMKLLR TSEHESAKFT LYFLGYGVPK TDSVFSCESV
LELTHNWGTE NDPNFHYHNG NSEPQGYGHI CISCDDAGAL CKEIEVKYGD KIQWSPKFNQ
GRMKNIAFLK DPDGYSIEVV PHGLIA
