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Database: UniProt
Entry: P50107
LinkDB: P50107
Original site: P50107 
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   26-NOV-2014, entry version 130.
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 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.,
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;
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
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       {ECO:0000269|PubMed:11050082, ECO:0000269|PubMed:8824231}.
CC   -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC       methylglyoxal.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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. {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   ProteinModelPortal; P50107; -.
DR   SMR; P50107; 18-165, 183-326.
DR   BioGrid; 35167; 12.
DR   MINT; MINT-4496565; -.
DR   BindingDB; P50107; -.
DR   ChEMBL; CHEMBL6057; -.
DR   MaxQB; P50107; -.
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   InParanoid; P50107; -.
DR   KO; K01759; -.
DR   OMA; TEGRMKN; -.
DR   OrthoDB; EOG7HXD33; -.
DR   BioCyc; MetaCyc:MONOMER-624; -.
DR   BioCyc; YEAST:YML004C-MONOMER; -.
DR   SABIO-RK; P50107; -.
DR   UniPathway; UPA00619; UER00675.
DR   NextBio; 978174; -.
DR   PRO; PR:P50107; -.
DR   Genevestigator; P50107; -.
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   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
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   SUPFAM; SSF54593; SSF54593; 2.
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   ACT_SITE    163    163       Proton donor/acceptor. {ECO:0000250}.
FT   METAL        25     25       Zinc; via tele nitrogen; shared with
FT                                dimeric partner. {ECO:0000250}.
FT   METAL        89     89       Zinc; shared with dimeric partner.
FT                                {ECO:0000250}.
FT   METAL       117    117       Zinc; via tele nitrogen. {ECO:0000250}.
FT   METAL       163    163       Zinc. {ECO:0000250}.
FT   BINDING      29     29       Substrate. {ECO:0000250}.
FT   BINDING      93     93       Substrate. {ECO:0000250}.
FT   BINDING     113    113       Substrate. {ECO:0000250}.
FT   BINDING     117    117       Substrate. {ECO:0000250}.
FT   CONFLICT     36     36       T -> A (in Ref. 2; CAC16163).
FT                                {ECO:0000305}.
FT   CONFLICT    156    156       G -> D (in Ref. 2; CAC16163 and 5; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    322    322       H -> Y (in Ref. 2; CAC16163).
FT                                {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
//
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