LGUL_SOLLC
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 03-AUG-2022, entry version 120.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. 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. {ECO:0000250}.
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;
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 degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: By stress conditions such as salt stress, water deficit, or
CC treatment with abscisic acid.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; Z48183; CAA88233.1; -; mRNA.
DR PIR; S62723; S62723.
DR RefSeq; NP_001234447.1; NM_001247518.3.
DR AlphaFoldDB; Q42891; -.
DR SMR; Q42891; -.
DR STRING; 4081.Solyc11g069040.2.1; -.
DR PaxDb; Q42891; -.
DR PRIDE; Q42891; -.
DR EnsemblPlants; Solyc11g069040.3.1; Solyc11g069040.3.1; Solyc11g069040.3.
DR GeneID; 544161; -.
DR Gramene; Solyc11g069040.3.1; Solyc11g069040.3.1; Solyc11g069040.3.
DR KEGG; sly:544161; -.
DR eggNOG; KOG2944; Eukaryota.
DR HOGENOM; CLU_046006_1_3_1; -.
DR InParanoid; Q42891; -.
DR OMA; FLQQTMF; -.
DR OrthoDB; 1513831at2759; -.
DR PhylomeDB; Q42891; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000004994; Chromosome 11.
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:0009651; P:response to salt stress; TAS:AgBase.
DR GO; GO:0009414; P:response to water deprivation; TAS:AgBase.
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 InterPro; IPR037523; VOC.
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.
DR PROSITE; PS51819; VOC; 1.
PE 2: Evidence at transcript level;
KW Lyase; Metal-binding; Reference proteome; Stress response; Zinc.
FT CHAIN 1..185
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000168084"
FT DOMAIN 27..174
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="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
