GLO2_ECOLI
ID GLO2_ECOLI Reviewed; 251 AA.
AC P0AC84; Q47677;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Hydroxyacylglutathione hydrolase GloB {ECO:0000305|PubMed:17196158, ECO:0000305|PubMed:25670698};
DE EC=3.1.2.6 {ECO:0000269|PubMed:17196158, ECO:0000269|PubMed:25670698};
DE AltName: Full=Glyoxalase II {ECO:0000303|PubMed:17196158, ECO:0000303|PubMed:25670698};
DE Short=Glx II {ECO:0000303|PubMed:17196158, ECO:0000303|PubMed:25670698};
GN Name=gloB {ECO:0000303|PubMed:25670698}; Synonyms=yafR;
GN OrderedLocusNames=b0212, JW0202;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17196158; DOI=10.1016/j.abb.2006.11.024;
RA O'Young J., Sukdeo N., Honek J.F.;
RT "Escherichia coli glyoxalase II is a binuclear zinc-dependent
RT metalloenzyme.";
RL Arch. Biochem. Biophys. 459:20-26(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, DISRUPTION PHENOTYPE, 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).
CC -!- FUNCTION: Type II glyoxalase that catalyzes the hydrolysis of (R)-S-
CC lactoylglutathione to (R)-lactate and glutathione (PubMed:25670698,
CC PubMed:17196158). Is more efficient than the isozyme GloC, and plays a
CC major contribution to methylglyoxal (MG) detoxification in E.coli
CC (PubMed:25670698). The two isoenzymes have additive effects and ensure
CC maximal MG degradation (PubMed:25670698). {ECO:0000269|PubMed:17196158,
CC ECO:0000269|PubMed:25670698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC Evidence={ECO:0000269|PubMed:17196158, ECO:0000269|PubMed:25670698};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione +
CC H(+); Xref=Rhea:RHEA:25245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=3.1.2.6;
CC Evidence={ECO:0000269|PubMed:17196158, ECO:0000269|PubMed:25670698};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17196158, ECO:0000305|PubMed:25670698};
CC Note=Binds 2 Zn(2+) ions per subunit. Mn(2+) and Co(2+) can substitute
CC for zinc in reconstitution experiments. {ECO:0000269|PubMed:17196158};
CC -!- ACTIVITY REGULATION: Is inhibited by Cu(2+).
CC {ECO:0000269|PubMed:25670698}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=184 uM for (R)-S-lactoylglutathione {ECO:0000269|PubMed:17196158};
CC KM=0.5 mM for (R)-S-lactoylglutathione {ECO:0000269|PubMed:25670698};
CC Vmax=112 umol/min/mg enzyme for the hydrolysis of (R)-S-
CC lactoylglutathione {ECO:0000269|PubMed:17196158};
CC Note=kcat is 53 sec(-1) for the hydrolysis of (R)-S-
CC lactoylglutathione (PubMed:17196158). kcat is 15.6 sec(-1) for the
CC hydrolysis of (R)-S-lactoylglutathione (PubMed:25670698).
CC {ECO:0000269|PubMed:17196158, ECO:0000269|PubMed:25670698};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC {ECO:0000269|PubMed:25670698}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17196158}.
CC -!- MASS SPECTROMETRY: Mass=28432; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17196158};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show decreased
CC methylglyoxal tolerance. A double deletion mutant lacking both gloB and
CC gloC exhibits almost no resistance to exogenously supplied
CC methylglyoxal, and is unable to grow at MG concentrations as low as 0.1
CC mM. {ECO:0000269|PubMed:25670698}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; U70214; AAB08634.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73317.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77883.1; -; Genomic_DNA.
DR PIR; F64745; F64745.
DR RefSeq; NP_414748.1; NC_000913.3.
DR RefSeq; WP_001052715.1; NZ_SSZK01000029.1.
DR PDB; 6RZ0; X-ray; 1.10 A; A=1-251.
DR PDB; 6S0I; X-ray; 1.80 A; A=1-251.
DR PDBsum; 6RZ0; -.
DR PDBsum; 6S0I; -.
DR AlphaFoldDB; P0AC84; -.
DR SMR; P0AC84; -.
DR BioGRID; 4262005; 24.
DR DIP; DIP-48248N; -.
DR IntAct; P0AC84; 1.
DR STRING; 511145.b0212; -.
DR jPOST; P0AC84; -.
DR PaxDb; P0AC84; -.
DR PRIDE; P0AC84; -.
DR EnsemblBacteria; AAC73317; AAC73317; b0212.
DR EnsemblBacteria; BAA77883; BAA77883; BAA77883.
DR GeneID; 944902; -.
DR KEGG; ecj:JW0202; -.
DR KEGG; eco:b0212; -.
DR PATRIC; fig|1411691.4.peg.2072; -.
DR EchoBASE; EB3114; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_030571_4_1_6; -.
DR InParanoid; P0AC84; -.
DR OMA; NYIWLLQ; -.
DR PhylomeDB; P0AC84; -.
DR BioCyc; EcoCyc:GLYOXII-MON; -.
DR BioCyc; MetaCyc:GLYOXII-MON; -.
DR BRENDA; 3.1.2.6; 2026.
DR SABIO-RK; P0AC84; -.
DR UniPathway; UPA00619; UER00676.
DR PRO; PR:P0AC84; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Hydrolase; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..251
FT /note="Hydroxyacylglutathione hydrolase GloB"
FT /id="PRO_0000192351"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 165..167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 245..248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:6RZ0"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:6RZ0"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:6RZ0"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:6RZ0"
SQ SEQUENCE 251 AA; 28434 MW; D59948B6E12809F5 CRC64;
MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIA ANNWQPEAIF LTHHHHDHVG
GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK
PYLFCGDTLF SGGCGRLFEG TASQMYQSLK KLSALPDDTL VCCAHEYTLS NMKFALSILP
HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER
FAWLRSKKDR F
