ID A0A0E1NVF0_YERPA Unreviewed; 135 AA.
AC A0A0E1NVF0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00018701};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081};
DE AltName: Full=Aldoketomutase {ECO:0000256|ARBA:ARBA00030892};
DE AltName: Full=Glyoxalase I {ECO:0000256|ARBA:ARBA00030537};
DE AltName: Full=Ketone-aldehyde mutase {ECO:0000256|ARBA:ARBA00030291};
DE AltName: Full=Methylglyoxalase {ECO:0000256|ARBA:ARBA00032460};
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase {ECO:0000256|ARBA:ARBA00033298};
GN OrderedLocusNames=YPA_1727 {ECO:0000313|EMBL:ABG13693.1};
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG13693.1, ECO:0000313|Proteomes:UP000001971};
RN [1] {ECO:0000313|EMBL:ABG13693.1, ECO:0000313|Proteomes:UP000001971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua {ECO:0000313|EMBL:ABG13693.1,
RC ECO:0000313|Proteomes:UP000001971};
RX PubMed=16740952; DOI=10.1128/JB.00124-06;
RA Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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:0000256|ARBA:ARBA00000817};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|ARBA:ARBA00001967};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR604361-3};
CC Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are
CC bound between subunits. {ECO:0000256|PIRSR:PIRSR604361-3};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005008}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC {ECO:0000256|ARBA:ARBA00010363}.
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DR EMBL; CP000308; ABG13693.1; -; Genomic_DNA.
DR RefSeq; WP_002210948.1; NZ_CP009906.1.
DR AlphaFoldDB; A0A0E1NVF0; -.
DR GeneID; 57976294; -.
DR KEGG; ypa:YPA_1727; -.
DR PATRIC; fig|360102.15.peg.325; -.
DR HOGENOM; CLU_046006_8_1_6; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000001971; Chromosome.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABG13693.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 2..126
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 122
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
SQ SEQUENCE 135 AA; 14834 MW; B11FAF23908BB8A4 CRC64;
MRLLHTMLRV GDLQRSIDFY TKVLGMRLLR TSENTEYKYS LAFVGYSDES KGSVIELTYN
WGVDQYDMGT AFGHLALGVD DVAATCDQIR QAGGKVTREA GPVKGGNTII AFVEDPDGYK
IELIENKSAG DCLGN
//
