LGUL_ECOLI
ID LGUL_ECOLI Reviewed; 135 AA.
AC P0AC81; P77036; Q2MB62; Q59384;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I {ECO:0000303|PubMed:25670698};
DE Short=Glx I {ECO:0000303|PubMed:25670698};
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=gloA; OrderedLocusNames=b1651, JW1643;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9047352; DOI=10.1016/s0378-1119(96)00691-9;
RA Clugston S.L., Daub E., Kinach R., Miedema D., Barnard J.F.J., Honek J.F.;
RT "Isolation and sequencing of a gene coding for glyoxalase I activity from
RT Salmonella typhimurium and comparison with other glyoxalase I sequences.";
RL Gene 186:103-111(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11,
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RX PubMed=9628737; DOI=10.1021/bi972791w;
RA Clugston S.L., Barnard J.F.J., Kinach R., Miedema D., Ruman R., Daub E.,
RA Honek J.F.;
RT "Overproduction and characterization of a dimeric non-zinc glyoxalase I
RT from Escherichia coli: evidence for optimal activation by nickel ions.";
RL Biochemistry 37:8754-8763(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Mizugaki M., Miura K., Yonezawa M., Hishinuma T., Tomioka Y.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=23506073; DOI=10.1111/mmi.12192;
RA Lee C., Shin J., Park C.;
RT "Novel regulatory system nemRA-gloA for electrophile reduction in
RT Escherichia coli K-12.";
RL Mol. Microbiol. 88:395-412(2013).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23536188; DOI=10.1074/jbc.m113.454421;
RA Gray M.J., Wholey W.Y., Parker B.W., Kim M., Jakob U.;
RT "NemR is a bleach-sensing transcription factor.";
RL J. Biol. Chem. 288:13789-13798(2013).
RN [8]
RP INDUCTION.
RX PubMed=23646895; DOI=10.1111/mmi.12234;
RA Ozyamak E., de Almeida C., de Moura A.P., Miller S., Booth I.R.;
RT "Integrated stress response of Escherichia coli to methylglyoxal:
RT transcriptional readthrough from the nemRA operon enhances protection
RT through increased expression of glyoxalase I.";
RL Mol. Microbiol. 88:936-950(2013).
RN [9]
RP FUNCTION, AND PATHWAY.
RX PubMed=25670698; DOI=10.1093/femsle/fnu014;
RA Reiger M., Lassak J., Jung K.;
RT "Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 362:1-7(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH ZINC; NICKEL;
RP COBALT AND CADMIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX PubMed=10913283; DOI=10.1021/bi000856g;
RA He M.M., Clugston S.L., Honek J.F., Matthews B.W.;
RT "Determination of the structure of Escherichia coli glyoxalase I suggests a
RT structural basis for differential metal activation.";
RL Biochemistry 39:8719-8727(2000).
CC -!- FUNCTION: Catalyzes the isomerization of the hemithioacetal formed
CC spontaneously from methylglyoxal and glutathione, to S-
CC lactoylglutathione, which is then hydrolyzed by a type II glyoxalase
CC (GloB or GloC). Is involved in methylglyoxal (MG) detoxification
CC (PubMed:10913283) (Probable). Involved in resistance to hypochlorous
CC acid (HOCl), which is the active component of household bleach and a
CC powerful antimicrobial during the innate immune response
CC (PubMed:23536188). {ECO:0000269|PubMed:10913283,
CC ECO:0000269|PubMed:23536188, ECO:0000305|PubMed:25670698}.
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:0000269|PubMed:10913283};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:10913283};
CC Note=Binds 1 nickel ion per subunit. In the homodimer, two nickel ions
CC are bound between subunits. Is not active with zinc ions.
CC {ECO:0000269|PubMed:10913283};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000269|PubMed:25670698}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10913283}.
CC -!- INTERACTION:
CC P0AC81; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-551143, EBI-542092;
CC -!- INDUCTION: Repressed by NemR. Induced by reactive electrophilic species
CC (RES) such as quinones, glyoxals and methylglyoxal (PubMed:23506073,
CC PubMed:23646895). Up-regulated by HOCl (PubMed:23536188).
CC {ECO:0000269|PubMed:23506073, ECO:0000269|PubMed:23536188,
CC ECO:0000269|PubMed:23646895}.
CC -!- MASS SPECTROMETRY: Mass=14919; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9628737};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases the HOCl
CC sensitivity. Mutant is more sensitive to methylglyoxal treatment.
CC {ECO:0000269|PubMed:23536188}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; U57363; AAC27133.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74723.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76494.1; -; Genomic_DNA.
DR EMBL; D86931; BAA13187.1; -; Genomic_DNA.
DR PIR; E64922; E64922.
DR RefSeq; NP_416168.1; NC_000913.3.
DR RefSeq; WP_001237796.1; NZ_STEB01000003.1.
DR PDB; 1F9Z; X-ray; 1.50 A; A/B=1-135.
DR PDB; 1FA5; X-ray; 1.80 A; A/B=1-135.
DR PDB; 1FA6; X-ray; 1.90 A; A/B=1-135.
DR PDB; 1FA7; X-ray; 1.90 A; A/B=1-135.
DR PDB; 1FA8; X-ray; 1.70 A; A/B=1-135.
DR PDBsum; 1F9Z; -.
DR PDBsum; 1FA5; -.
DR PDBsum; 1FA6; -.
DR PDBsum; 1FA7; -.
DR PDBsum; 1FA8; -.
DR AlphaFoldDB; P0AC81; -.
DR SMR; P0AC81; -.
DR BioGRID; 4259387; 22.
DR BioGRID; 850521; 1.
DR DIP; DIP-47995N; -.
DR IntAct; P0AC81; 7.
DR STRING; 511145.b1651; -.
DR jPOST; P0AC81; -.
DR PaxDb; P0AC81; -.
DR PRIDE; P0AC81; -.
DR EnsemblBacteria; AAC74723; AAC74723; b1651.
DR EnsemblBacteria; BAE76494; BAE76494; BAE76494.
DR GeneID; 66674457; -.
DR GeneID; 946161; -.
DR KEGG; ecj:JW1643; -.
DR KEGG; eco:b1651; -.
DR PATRIC; fig|1411691.4.peg.608; -.
DR EchoBASE; EB3197; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_046006_8_1_6; -.
DR InParanoid; P0AC81; -.
DR OMA; NWGTESY; -.
DR PhylomeDB; P0AC81; -.
DR BioCyc; EcoCyc:GLYOXI-MON; -.
DR BioCyc; MetaCyc:GLYOXI-MON; -.
DR BRENDA; 4.4.1.5; 2026.
DR SABIO-RK; P0AC81; -.
DR UniPathway; UPA00619; UER00675.
DR EvolutionaryTrace; P0AC81; -.
DR PRO; PR:P0AC81; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:EcoCyc.
DR GO; GO:0016151; F:nickel cation binding; IDA:EcoCyc.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; 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 3D-structure; Detoxification; Direct protein sequencing; Lyase;
KW Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..135
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000168088"
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 /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:10913283"
FT BINDING 9
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:10913283"
FT BINDING 60
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:10913283"
FT BINDING 74
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:10913283"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1F9Z"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:1F9Z"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1F9Z"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:1F9Z"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1F9Z"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1F9Z"
SQ SEQUENCE 135 AA; 14920 MW; A53FC5412B9A6CE3 CRC64;
MRLLHTMLRV GDLQRSIDFY TKVLGMKLLR TSENPEYKYS LAFVGYGPET EEAVIELTYN
WGVDKYELGT AYGHIALSVD NAAEACEKIR QNGGNVTREA GPVKGGTTVI AFVEDPDGYK
IELIEEKDAG RGLGN
