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 01-MAY-2013, entry version 118.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=GLO1; OrderedLocusNames=YML004C; ORFNames=YM9571.15C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:25958-25965(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 204511 / S288c / AB972;
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.,
RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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
RT gene in Saccharomyces cerevisiae.";
RL Biotechnol. Appl. Biochem. 14:391-394(1991).
RN [6]
RP DISCUSSION OF SEQUENCE.
RX PubMed=8670139;
RA Ridderstroem M., Mannervik B.;
RT "The primary structure of monomeric yeast glyoxalase I indicates a
RT gene duplication resulting in two similar segments homologous with the
RT subunit 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.,
RA Dephoure N., 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 -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC methylglyoxal.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC degradation; (R)-lactate from methylglyoxal: step 1/2.
CC -!- SUBUNIT: Monomer.
CC -!- MISCELLANEOUS: Present with 2570 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
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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 ProteinModelPortal; P50107; -.
DR SMR; P50107; 18-165, 183-326.
DR PaxDb; P50107; -.
DR PeptideAtlas; P50107; -.
DR EnsemblFungi; YML004C; YML004C; YML004C.
DR GeneID; 855009; -.
DR KEGG; sce:YML004C; -.
DR CYGD; YML004c; -.
DR SGD; S000004463; GLO1.
DR eggNOG; COG0346; -.
DR GeneTree; ENSGT00390000009312; -.
DR HOGENOM; HOG000215632; -.
DR KO; K01759; -.
DR OMA; GYADEDK; -.
DR OrthoDB; EOG4GXJWH; -.
DR BioCyc; MetaCyc:MONOMER-624; -.
DR SABIO-RK; P50107; -.
DR UniPathway; UPA00619; UER00675.
DR BindingDB; P50107; -.
DR ChEMBL; CHEMBL6057; -.
DR NextBio; 978174; -.
DR Genevestigator; P50107; -.
DR GermOnline; YML004C; Saccharomyces cerevisiae.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IGI:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IGI:SGD.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate; IDA:SGD.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR025870; Glyoxalase-like_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR Pfam; PF00903; Glyoxalase; 1.
DR Pfam; PF12681; Glyoxalase_2; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 2.
DR PROSITE; PS00934; GLYOXALASE_I_1; 2.
DR PROSITE; PS00935; GLYOXALASE_I_2; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Lyase; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1 326 Lactoylglutathione lyase.
FT /FTId=PRO_0000168087.
FT METAL 242 242 Zinc (Potential).
FT METAL 245 245 Zinc (Potential).
FT METAL 258 258 Zinc (Potential).
FT METAL 269 269 Zinc (Potential).
FT CONFLICT 36 36 T -> A (in Ref. 2; CAC16163).
FT CONFLICT 156 156 G -> D (in Ref. 2; CAC16163 and 5; AA
FT sequence).
FT CONFLICT 322 322 H -> Y (in Ref. 2; CAC16163).
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
//
