GenomeNet

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   29-OCT-2014, entry version 84.
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.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC       methylglyoxal.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. {ECO:0000250}.
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. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   InParanoid; Q42891; -.
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:0006094; P:gluconeogenesis; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006096; P:glycolytic process; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants/Gramene.
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. {ECO:0000250}.
FT   ACT_SITE    170    170       Proton donor/acceptor. {ECO:0000250}.
FT   METAL        30     30       Zinc. {ECO:0000250}.
FT   METAL        96     96       Zinc. {ECO:0000250}.
FT   METAL       124    124       Zinc; via tele nitrogen. {ECO:0000250}.
FT   METAL       170    170       Zinc. {ECO:0000250}.
FT   BINDING      30     30       Substrate. {ECO:0000250}.
FT   BINDING      34     34       Substrate. {ECO:0000250}.
FT   BINDING     100    100       Substrate. {ECO:0000250}.
FT   BINDING     120    120       Substrate. {ECO:0000250}.
FT   BINDING     124    124       Substrate. {ECO:0000250}.
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
//
DBGET integrated database retrieval system