GLO22_ECOLI
ID GLO22_ECOLI Reviewed; 215 AA.
AC P75849;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Hydroxyacylglutathione hydrolase GloC {ECO:0000305|PubMed:25670698};
DE EC=3.1.2.6 {ECO:0000269|PubMed:25670698};
DE AltName: Full=Accessory type II glyoxalase {ECO:0000303|PubMed:25670698};
DE AltName: Full=Glyoxalase II 2 {ECO:0000303|PubMed:25670698};
DE Short=GlxII-2 {ECO:0000303|PubMed:25670698};
GN Name=gloC {ECO:0000303|PubMed:25670698}; Synonyms=ycbL;
GN OrderedLocusNames=b0927, JW0910;
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;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
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 [3]
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 [4]
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, isozyme of GloB, that hydrolyzes (R)-S-
CC lactoylglutathione to (R)-lactate and glutathione. Plays a minor
CC contribution to methylglyoxal (MG) detoxification in E.coli, compared
CC to GloB. The two isoenzymes have additive effects and ensure maximal MG
CC degradation. {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: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:25670698};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q16775, ECO:0000305|PubMed:25670698};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775};
CC -!- ACTIVITY REGULATION: Is inhibited by Cu(2+).
CC {ECO:0000269|PubMed:25670698}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for (R)-S-lactoylglutathione {ECO:0000269|PubMed:25670698};
CC Note=kcat is 0.9 sec(-1) for the hydrolysis of (R)-S-
CC lactoylglutathione. {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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene show decreased
CC methylglyoxal tolerance. A double deletion mutant lacking both gloC and
CC gloB 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; U00096; AAC74013.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35673.1; -; Genomic_DNA.
DR PIR; F64832; F64832.
DR RefSeq; NP_415447.1; NC_000913.3.
DR RefSeq; WP_001109486.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P75849; -.
DR SMR; P75849; -.
DR BioGRID; 4261607; 21.
DR BioGRID; 849925; 1.
DR DIP; DIP-11480N; -.
DR IntAct; P75849; 4.
DR STRING; 511145.b0927; -.
DR jPOST; P75849; -.
DR PaxDb; P75849; -.
DR PRIDE; P75849; -.
DR EnsemblBacteria; AAC74013; AAC74013; b0927.
DR EnsemblBacteria; BAA35673; BAA35673; BAA35673.
DR GeneID; 945551; -.
DR KEGG; ecj:JW0910; -.
DR KEGG; eco:b0927; -.
DR PATRIC; fig|1411691.4.peg.1349; -.
DR EchoBASE; EB3468; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_030571_5_0_6; -.
DR InParanoid; P75849; -.
DR OMA; GAWGTNC; -.
DR PhylomeDB; P75849; -.
DR BioCyc; EcoCyc:G6475-MON; -.
DR BioCyc; MetaCyc:G6475-MON; -.
DR UniPathway; UPA00619; UER00676.
DR PRO; PR:P75849; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Detoxification; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..215
FT /note="Hydroxyacylglutathione hydrolase GloC"
FT /id="PRO_0000192357"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
SQ SEQUENCE 215 AA; 23784 MW; C4233FF08308B18D CRC64;
MNYRIIPVTA FSQNCSLIWC EQTRLAALVD PGGDAEKIKQ EVDDSGLTLM QILLTHGHLD
HVGAAAELAQ HYGVPVFGPE KEDEFWLQGL PAQSRMFGLE ECQPLTPDRW LNEGDTISIG
NVTLQVLHCP GHTPGHVVFF DDRAKLLISG DVIFKGGVGR SDFPRGDHNQ LISSIKDKLL
PLGDDVIFIP GHGPLSTLGY ERLHNPFLQD EMPVW
