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Database: UniProt
Entry: Q42891
LinkDB: Q42891
Original site: Q42891 
ID   LGUL_SOLLC              Reviewed;         185 AA.
AC   Q42891;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   11-JUN-2014, entry version 82.
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=GLX1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Solaneae; Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Rutgers;
RX   PubMed=8616220; DOI=10.1007/BF00020464;
RA   Espartero J., Sanchez-Aguayo I., Pardo J.M.;
RT   "Molecular characterization of glyoxalase-I from a higher plant;
RT   upregulation by stress.";
RL   Plant Mol. Biol. 29:1223-1233(1995).
CC   -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC       methylglyoxal and glutathione, to S-lactoylglutathione (By
CC       similarity).
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   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: By stress conditions such as salt stress, water
CC       deficit, or treatment with abscisic acid.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family.
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DR   EMBL; Z48183; CAA88233.1; -; mRNA.
DR   PIR; S62723; S62723.
DR   RefSeq; NP_001234447.1; NM_001247518.2.
DR   UniGene; Les.40; -.
DR   ProteinModelPortal; Q42891; -.
DR   SMR; Q42891; 17-177.
DR   EnsemblPlants; Solyc11g069040.2.1; Solyc11g069040.2.1; Solyc11g069040.2.
DR   GeneID; 544161; -.
DR   KEGG; sly:544161; -.
DR   KO; K01759; -.
DR   OMA; WALSRKA; -.
DR   UniPathway; UPA00619; UER00675.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.180.10; -; 1.
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   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   TIGRFAMs; TIGR00068; glyox_I; 1.
DR   PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR   PROSITE; PS00935; GLYOXALASE_I_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Lyase; Metal-binding; Reference proteome;
KW   Stress response; Zinc.
FT   CHAIN         1    185       Lactoylglutathione lyase.
FT                                /FTId=PRO_0000168084.
FT   REGION      154    155       Substrate binding (By similarity).
FT   ACT_SITE    170    170       Proton donor/acceptor (By similarity).
FT   METAL        30     30       Zinc (By similarity).
FT   METAL        96     96       Zinc (By similarity).
FT   METAL       124    124       Zinc; via tele nitrogen (By similarity).
FT   METAL       170    170       Zinc (By similarity).
FT   BINDING      30     30       Substrate (By similarity).
FT   BINDING      34     34       Substrate (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     120    120       Substrate (By similarity).
FT   BINDING     124    124       Substrate (By similarity).
SQ   SEQUENCE   185 AA;  20717 MW;  0D16247209138CA1 CRC64;
     MASESKDSPS NNPGLHATPD EATKGYFLQQ TMFRIKDPKV SLEFYSKVLG MSLLKRLDFP
     EMKFSLYFMG YEDTASAPSD PVERTAWTFS QKSTLELTHN WGTESDPNFT GYHNGNSEPR
     GFGHIGVTVD DVYKACERFE SLGVEFVKKP LDGKMKGIAF IKDPDGYWIE IFDTKIIKDA
     AGSAS
//
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