ID   LGUL_SYNY3              Reviewed;         131 AA.
AC   Q55595;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Probable 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=gloA; OrderedLocusNames=slr0381;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC       Note=Binds 1 nickel 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; BA000022; BAA10101.1; -; Genomic_DNA.
DR   PIR; S76123; S76123.
DR   AlphaFoldDB; Q55595; -.
DR   SMR; Q55595; -.
DR   STRING; 1148.1001475; -.
DR   PaxDb; Q55595; -.
DR   EnsemblBacteria; BAA10101; BAA10101; BAA10101.
DR   KEGG; syn:slr0381; -.
DR   eggNOG; COG0346; Bacteria.
DR   InParanoid; Q55595; -.
DR   OMA; NWGTESY; -.
DR   PhylomeDB; Q55595; -.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IBA:GO_Central.
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   3: Inferred from homology;
KW   Lyase; Metal-binding; Nickel; Reference proteome.
FT   CHAIN           1..131
FT                   /note="Probable lactoylglutathione lyase"
FT                   /id="PRO_0000168096"
FT   DOMAIN          2..126
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        122
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         5
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   131 AA;  14665 MW;  7B65120783DE0F91 CRC64;
     MFLLHTMIRV GDLDKSLQFY CDILGMNLLR KKDYPSGEFT LAFVGYGKES ENAVIELTHN
     WGTDKYDLGN GFGHIALGVE DIYSTCDKIR DKGGKVVREP GPMKHGTTVI AFVEDPDGYK
     IELIQTSSKK D