ID   LGUL_CICAR              Reviewed;         186 AA.
AC   O49818;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
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;
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Castellana;
RA   Romo S., Labrador E., Dopico B.;
RT   "Isolation and characterization of a cDNA encoding a glyoxalase-I from
RT   Cicer arietinum L. Epicotyls upregulated by stress.";
RL   (er) Plant Gene Register PGR98-074(1998).
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; AJ224520; CAA12028.1; -; mRNA.
DR   RefSeq; XP_004506056.1; XM_004505999.1.
DR   AlphaFoldDB; O49818; -.
DR   SMR; O49818; -.
DR   STRING; 3827.XP_004506055.1; -.
DR   KEGG; cam:101505694; -.
DR   eggNOG; KOG2944; Eukaryota.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000087171; Genome assembly.
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; -; 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; Zinc.
FT   CHAIN           1..186
FT                   /note="Lactoylglutathione lyase"
FT                   /id="PRO_0000168083"
FT   DOMAIN          28..175
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        171
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   186 AA;  21088 MW;  96F5C729AC3C2E5E CRC64;
     MAASESKESP ANNPGLHTTI DEATKGYFMQ QTMFRIKDPK VSLDFYSRVL GMSLLKRLDF
     PEMKFSLYFM GYEDTTEAPS NPVDRTVWTF AQKATIELTH NWGTESDPEF KGYHNGNSDP
     RGFGHIGITV DDTYKACERF QNLGVEFVKK PDDGKMKGIA FIKDPDGYWI ELFDRKTIGN
     VTEGNA