ID A0A0K1QSG3_PSEFL Unreviewed; 173 AA.
AC A0A0K1QSG3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081, ECO:0000256|RuleBase:RU361179};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081, ECO:0000256|RuleBase:RU361179};
DE AltName: Full=Glyoxalase I {ECO:0000256|RuleBase:RU361179};
GN ORFNames=B723_20265 {ECO:0000313|EMBL:AKV08597.1};
OS Pseudomonas fluorescens NCIMB 11764.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1221522 {ECO:0000313|EMBL:AKV08597.1, ECO:0000313|Proteomes:UP000017175};
RN [1] {ECO:0000313|EMBL:AKV08597.1, ECO:0000313|Proteomes:UP000017175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11764 {ECO:0000313|EMBL:AKV08597.1,
RC ECO:0000313|Proteomes:UP000017175};
RX PubMed=23144379; DOI=10.1128/JB.01670-12;
RA Vilo C.A., Benedik M.J., Kunz D.A., Dong Q.;
RT "Draft genome sequence of the cyanide-utilizing bacterium Pseudomonas
RT fluorescens strain NCIMB 11764.";
RL J. Bacteriol. 194:6618-6619(2012).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione.
CC {ECO:0000256|RuleBase:RU361179}.
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|RuleBase:RU361179};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|RuleBase:RU361179};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000256|RuleBase:RU361179};
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, ECO:0000256|RuleBase:RU361179}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC {ECO:0000256|ARBA:ARBA00010363, ECO:0000256|RuleBase:RU361179}.
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DR EMBL; CP010945; AKV08597.1; -; Genomic_DNA.
DR RefSeq; WP_017338616.1; NZ_CP010945.1.
DR AlphaFoldDB; A0A0K1QSG3; -.
DR eggNOG; COG0346; Bacteria.
DR OrthoDB; 9789841at2; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000017175; Chromosome.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd07233; GlxI_Zn; 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; PTHR10374:SF30; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR10374; LACTOYLGLUTATHIONE LYASE GLYOXALASE I; 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 {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361179};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3,
KW ECO:0000256|RuleBase:RU361179}; Nickel {ECO:0000256|RuleBase:RU361179};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 24..170
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 166
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 93
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 120
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 166
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 173 AA; 19570 MW; 6D0D8A7440855025 CRC64;
MSLHELNTFP GVTAQPDTAT QKFVFNHTML RVKDITKSLD FYTRILGFSL VEKRDFPEAE
FSLYFLALVD KDQIPADAAA RTEWMKSIPG ILELTHNHGT ENDADFAYHN GNTDPRGFGH
ICISVPDIVA ACERFEALGC DFQKRLNDGR MKSLAFIKDP DAYWVEIIQP APM
//
