ID   LGUL_PINST              Reviewed;          22 AA.
AC   P84719;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Putative 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=PS3;
DE   AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
DE   Flags: Fragments;
OS   Pinus strobus (Eastern white pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=3348;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|PubMed:16529377};
RX   PubMed=16529377; DOI=10.1094/mpmi-19-0150;
RA   Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
RA   Witthuhn B.A., David A.J., Gillman J.H.;
RT   "Proteomic comparison of needles from blister rust-resistant and
RT   susceptible Pinus strobus seedlings reveals upregulation of putative
RT   disease resistance proteins.";
RL   Mol. Plant Microbe Interact. 19:150-160(2006).
CC   -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC       methylglyoxal and glutathione, to S-lactoylglutathione.
CC       {ECO:0000250|UniProtKB:Q09751}.
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         Evidence={ECO:0000250|UniProtKB:Q09751};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q09751};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q09751};
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC       (R)-lactate from methylglyoxal: step 1/2.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.7,
CC       its MW is: 35.1 kDa. {ECO:0000269|PubMed:16529377}.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:16529377}.
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DR   AlphaFoldDB; P84719; -.
DR   UniPathway; UPA00619; UER00675.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Metal-binding; Zinc.
FT   CHAIN           <1..>22
FT                   /note="Putative lactoylglutathione lyase"
FT                   /id="PRO_0000240626"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        12
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         22
FT                   /evidence="ECO:0000303|PubMed:16529377"
SQ   SEQUENCE   22 AA;  2296 MW;  5E312E7F47F4B4D6 CRC64;
     ITACLDPDGW KEPGPLPGIS TK