ID   LGUL_BRAOG              Reviewed;         282 AA.
AC   Q39366; Q39365;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=S-D-lactoylglutathione methylglyoxal lyase;
OS   Brassica oleracea var. gemmifera (Brussel sprouts).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=178616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Booker J.P.;
RL   Thesis (1996), University of Durham, United Kingdom.
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   -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR   EMBL; Z74962; CAA99248.1; -; Genomic_DNA.
DR   EMBL; Z74950; CAA99233.1; -; mRNA.
DR   PIR; T14440; T14440.
DR   AlphaFoldDB; Q39366; -.
DR   SMR; Q39366; -.
DR   PRIDE; Q39366; -.
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.
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; IPR004361; Glyoxalase_1.
DR   InterPro; IPR018146; Glyoxalase_1_CS.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   SUPFAM; SSF54593; SSF54593; 2.
DR   TIGRFAMs; TIGR00068; glyox_I; 1.
DR   PROSITE; PS00934; GLYOXALASE_I_1; 2.
DR   PROSITE; PS00935; GLYOXALASE_I_2; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Lyase; Metal-binding; Repeat; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O65398"
FT   CHAIN           2..282
FT                   /note="Putative lactoylglutathione lyase"
FT                   /id="PRO_0000168081"
FT   DOMAIN          17..141
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          147..274
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O65398"
FT   VARIANT         41
FT                   /note="M -> L"
FT   VARIANT         162
FT                   /note="V -> I"
FT   VARIANT         165
FT                   /note="M -> Y"
FT   VARIANT         183
FT                   /note="N -> KY"
FT   VARIANT         236
FT                   /note="V -> A"
FT   VARIANT         269
FT                   /note="Q -> T"
SQ   SEQUENCE   282 AA;  31646 MW;  2BBB0F14BD52101C CRC64;
     MAENADLVEW PKKDKRRFLH VVYRVGDLDR TIQFYTECFG MKVLRKRDVP EEKYSNAFLG
     FGPETSNFVV ELTYNYGVSS YDIGTGFGHF AISTQDVSKM VEAVRAKGGN VTREPGPVKG
     GGSVIAFVKD PDGYTFELIQ RGPTPEPLCQ VMLRVGDLDR AVKFMEKALG MRLLRRIERP
     EYNTIGMMGY AEEYESIVLE LTYNYGVTEY TKGNAYAQIA IGTDDVYKSA EVVKIVNQEL
     GGKITREAGP LPGLGTKIVS FLDPDGWKQV LVDNEDFLKE LE