ID   LGUL_VIBCH              Reviewed;         138 AA.
AC   Q9KT93;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   27-MAR-2024, entry version 122.
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=VC_1010;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF94171.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF94171.1; ALT_INIT; Genomic_DNA.
DR   PIR; H82251; H82251.
DR   RefSeq; NP_230656.2; NC_002505.1.
DR   RefSeq; WP_000064966.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KT93; -.
DR   SMR; Q9KT93; -.
DR   STRING; 243277.VC_1010; -.
DR   DNASU; 2614263; -.
DR   EnsemblBacteria; AAF94171; AAF94171; VC_1010.
DR   GeneID; 69720292; -.
DR   KEGG; vch:VC_1010; -.
DR   PATRIC; fig|243277.26.peg.964; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_046006_8_1_6; -.
DR   UniPathway; UPA00619; UER00675.
DR   PRO; PR:Q9KT93; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   CDD; cd16358; GlxI_Ni; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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   NCBIfam; TIGR00068; glyox_I; 1.
DR   PANTHER; PTHR46036; LACTOYLGLUTATHIONE LYASE; 1.
DR   PANTHER; PTHR46036:SF5; LACTOYLGLUTATHIONE LYASE; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 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..138
FT                   /note="Probable lactoylglutathione lyase"
FT                   /id="PRO_0000168097"
FT   DOMAIN          5..129
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        125
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15176 MW;  21427CF9AA2E51BD CRC64;
     MSNHRILHTM LRVGDLDKSI EFYTQVMGMS LLRKNENTEY KYTLAFLGYG DESQGAVIEL
     TYNWGVADYE KGNAYGHIAI GVDDIYATCD TIKAAGGIVT REPGPVKGGT THIAFVKDPD
     GYMIELIQNK QAHAGLEG
//