LGUL_PSEPU
ID LGUL_PSEPU Reviewed; 173 AA.
AC P16635; Q52084;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
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;
GN Name=gloA;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RC STRAIN=ATCC 8209 / DSM 1693 / JCM 20511 / NBRC 3738 / NCIMB 8296 / NRRL
RC B-1595 / NRS 77 / VKM B-899;
RA Rhee H., Sato N., Murata K., Kimura A.;
RT "Nucleotide sequence of the glyoxalase I gene of Pseudomonas putida.";
RL Agric. Biol. Chem. 52:2243-2246(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND SEQUENCE
RP REVISION.
RX PubMed=7959071; DOI=10.1016/0378-1119(94)90864-8;
RA Lu T., Creighton D.J., Antoine M., Fenselau C., Lovett P.S.;
RT "The gene encoding glyoxalase I from Pseudomonas putida: cloning,
RT overexpression, and sequence comparisons with human glyoxalase I.";
RL Gene 150:93-96(1994).
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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 nickel or zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; D00342; BAA00248.1; -; Genomic_DNA.
DR EMBL; L33880; AAA61758.1; -; Genomic_DNA.
DR PIR; JU0070; WZPSLP.
DR AlphaFoldDB; P16635; -.
DR SMR; P16635; -.
DR BioCyc; MetaCyc:MON-12895; -.
DR BRENDA; 4.4.1.5; 5092.
DR UniPathway; UPA00619; UER00675.
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 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Metal-binding; Nickel; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..173
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000168099"
FT DOMAIN 24..170
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 166
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT CONFLICT 11..54
FT /note="GVTAQADPATAQFVFNHTMLRVKDIEKSLDFYTRVLGFKLVDKR -> ALLP
FT KRTLPLRNSFQPHHRARQGHREVADSIPACLVSNWWTS (in Ref. 1;
FT BAA00248)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> D (in Ref. 1; BAA00248)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..173
FT /note="DGYWVEVIQPTPL -> MVTGSK (in Ref. 1; BAA00248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 173 AA; 19540 MW; DD3E559B4C261BB3 CRC64;
MSLNDLNTLP GVTAQADPAT AQFVFNHTML RVKDIEKSLD FYTRVLGFKL VDKRDFVEAK
FSLYFLALVD PATIPADDDA RHQWMKSIPG VLELTHNHGT ERDADFAYHH GNTDPRGFGH
ICVSVPDVVA ACERFEALQV PFQKRLSDGR MNHLAFIKDP DGYWVEVIQP TPL
