HCHA_ECOLI
ID HCHA_ECOLI Reviewed; 283 AA.
AC P31658; P76338;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein/nucleic acid deglycase 1 {ECO:0000305|PubMed:26774339, ECO:0000305|PubMed:28596309};
DE EC=3.1.2.- {ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
DE EC=3.5.1.- {ECO:0000269|PubMed:28596309};
DE EC=3.5.1.124 {ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
DE AltName: Full=Glyoxalase III {ECO:0000303|PubMed:21696459, ECO:0000303|PubMed:7848303};
DE EC=4.2.1.130 {ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:7848303};
DE AltName: Full=Holding molecular chaperone {ECO:0000303|PubMed:14731284};
DE AltName: Full=Hsp31 {ECO:0000303|PubMed:12235139};
DE AltName: Full=Maillard deglycase {ECO:0000303|PubMed:28596309};
GN Name=hchA; Synonyms=yedU, yzzC; OrderedLocusNames=b1967, JW1950;
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=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 PROTEIN SEQUENCE OF 2-21.
RC STRAIN=K12;
RX PubMed=8455549; DOI=10.1007/bf00282791;
RA Yoshida T., Ueguchi C., Yamada H., Mizuno T.;
RT "Function of the Escherichia coli nucleoid protein, H-NS: molecular
RT analysis of a subset of proteins whose expression is enhanced in a hns
RT deletion mutant.";
RL Mol. Gen. Genet. 237:113-122(1993).
RN [5]
RP FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=7848303; DOI=10.1042/bj3050999;
RA Misra K., Banerjee A.B., Ray S., Ray M.;
RT "Glyoxalase III from Escherichia coli: a single novel enzyme for the
RT conversion of methylglyoxal into D-lactate without reduced glutathione.";
RL Biochem. J. 305:999-1003(1995).
RN [6]
RP FUNCTION AS A CHAPERONE, SUBUNIT, AND ACTIVITY REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12235139; DOI=10.1074/jbc.m205800200;
RA Sastry M.S.R., Korotkov K., Brodsky Y., Baneyx F.;
RT "Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone
RT whose activity is inhibited by ATP at high temperatures.";
RL J. Biol. Chem. 277:46026-46034(2002).
RN [7]
RP FUNCTION AS A CHAPERONE, AND SUBUNIT.
RX PubMed=12565879; DOI=10.1016/s0006-291x(02)03053-x;
RA Malki A., Kern R., Abdallah J., Richarme G.;
RT "Characterization of the Escherichia coli YedU protein as a molecular
RT chaperone.";
RL Biochem. Biophys. Res. Commun. 301:430-436(2003).
RN [8]
RP FUNCTION AS A CHAPERONE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14731284; DOI=10.1046/j.1365-2958.2003.03871.x;
RA Mujacic M., Bader M.W., Baneyx F.;
RT "Escherichia coli Hsp31 functions as a holding chaperone that cooperates
RT with the DnaK-DnaJ-GrpE system in the management of protein misfolding
RT under severe stress conditions.";
RL Mol. Microbiol. 51:849-859(2004).
RN [9]
RP DOMAIN.
RX PubMed=15173574; DOI=10.1073/pnas.0403033101;
RA Sastry M.S.R., Quigley P.M., Hol W.G.J., Baneyx F.;
RT "The linker-loop region of Escherichia coli chaperone Hsp31 functions as a
RT gate that modulates high-affinity substrate binding at elevated
RT temperatures.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8587-8592(2004).
RN [10]
RP FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-185.
RX PubMed=15550391; DOI=10.1074/jbc.m408296200;
RA Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J., Cha S.S.,
RA Mori H., Richarme G.;
RT "Peptidase activity of the Escherichia coli Hsp31 chaperone.";
RL J. Biol. Chem. 280:14420-14426(2005).
RN [11]
RP FUNCTION IN STRESS RESISTANCE.
RX PubMed=16796689; DOI=10.1111/j.1365-2958.2006.05207.x;
RA Mujacic M., Baneyx F.;
RT "Regulation of Escherichia coli hchA, a stress-inducible gene encoding
RT molecular chaperone Hsp31.";
RL Mol. Microbiol. 60:1576-1589(2006).
RN [12]
RP FUNCTION IN ACID STRESS RESISTANCE.
RX PubMed=17158627; DOI=10.1128/aem.02429-06;
RA Mujacic M., Baneyx F.;
RT "Chaperone Hsp31 contributes to acid resistance in stationary-phase
RT Escherichia coli.";
RL Appl. Environ. Microbiol. 73:1014-1018(2007).
RN [13]
RP FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77;
RP CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21696459; DOI=10.1111/j.1365-2958.2011.07736.x;
RA Subedi K.P., Choi D., Kim I., Min B., Park C.;
RT "Hsp31 of Escherichia coli K-12 is glyoxalase III.";
RL Mol. Microbiol. 81:926-936(2011).
RN [14]
RP CRYSTALLIZATION.
RX PubMed=12077448; DOI=10.1107/s0907444902007369;
RA Kim O.-G., Kim I.-K., Kim G.-H., Ko J., Park C., Suh P.-G., Kang S.-O.,
RA Lee H.-S., Cha S.-S.;
RT "Crystallization and preliminary X-ray crystallographic analysis of a yedU
RT gene product from Escherichia coli.";
RL Acta Crystallogr. D 58:1217-1219(2002).
RN [15]
RP FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26102038; DOI=10.1016/j.bbrc.2015.06.111;
RA Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.;
RT "The DJ-1 superfamily member Hsp31 repairs proteins from glycation by
RT methylglyoxal and glyoxal.";
RL Biochem. Biophys. Res. Commun. 463:1305-1310(2015).
RN [16]
RP FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=26774339; DOI=10.1016/j.bbrc.2016.01.068;
RA Abdallah J., Mihoub M., Gautier V., Richarme G.;
RT "The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair
RT proteins from glycation by methylglyoxal and glyoxal.";
RL Biochem. Biophys. Res. Commun. 470:282-286(2016).
RN [17]
RP FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=28596309; DOI=10.1126/science.aag1095;
RA Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N.,
RA Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.;
RT "Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.";
RL Science 357:208-211(2017).
RN [18] {ECO:0007744|PDB:1IZY, ECO:0007744|PDB:1IZZ}
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), PROTEOLYTIC ACTIVITY, AND
RP MUTAGENESIS OF CYS-185.
RX PubMed=12939276; DOI=10.1074/jbc.m304517200;
RA Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C.,
RA Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.;
RT "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share
RT an evolutionarily conserved domain.";
RL J. Biol. Chem. 278:44552-44559(2003).
RN [19] {ECO:0007744|PDB:1N57}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-291.
RX PubMed=12621151; DOI=10.1073/pnas.0530312100;
RA Quigley P.M., Korotkov K., Baneyx F., Hol W.G.J.;
RT "The 1.6-A crystal structure of the class of chaperones represented by
RT Escherichia coli Hsp31 reveals a putative catalytic triad.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3137-3142(2003).
RN [20] {ECO:0007744|PDB:1ONS}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-283 IN COMPLEX WITH ZINC, AND
RP METAL-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14500888; DOI=10.1110/ps.03121403;
RA Zhao Y., Liu D., Kaluarachchi W.D., Bellamy H.D., White M.A., Fox R.O.;
RT "The crystal structure of Escherichia coli heat shock protein YedU reveals
RT three potential catalytic active sites.";
RL Protein Sci. 12:2303-2311(2003).
RN [21] {ECO:0007744|PDB:1PV2}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS).
RX PubMed=14691241; DOI=10.1110/ps.03399604;
RA Quigley P.M., Korotkov K., Baneyx F., Hol W.G.J.;
RT "A new native EcHsp31 structure suggests a key role of structural
RT flexibility for chaperone function.";
RL Protein Sci. 13:269-277(2004).
CC -!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
CC deglycation of the Maillard adducts formed between amino groups of
CC proteins or nucleotides and reactive carbonyl groups of glyoxals
CC (PubMed:26102038, PubMed:26774339, PubMed:28596309). Thus, functions as
CC a protein deglycase that repairs methylglyoxal- and glyoxal-glycated
CC proteins, and releases repaired proteins and lactate or glycolate,
CC respectively. Deglycates cysteine, arginine and lysine residues in
CC proteins, and thus reactivates these proteins by reversing glycation by
CC glyoxals. Is able to repair glycated serum albumin, aspartate
CC aminotransferase, glyceraldehyde-3-phosphate dehydrogenase, and
CC fructose biphosphate aldolase. Acts on early glycation intermediates
CC (hemithioacetals and aminocarbinols), preventing the formation of
CC Schiff bases and advanced glycation endproducts (AGE) that cause
CC irreversible damage (PubMed:26102038, PubMed:26774339). Also functions
CC as a nucleotide deglycase able to repair glycated guanine in the free
CC nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus
CC involved in a major nucleotide repair system named guanine glycation
CC repair (GG repair), dedicated to reversing methylglyoxal and glyoxal
CC damage via nucleotide sanitization and direct nucleic acid repair
CC (PubMed:28596309). Has been reported to display chaperone, peptidase
CC and glutathione-independent glyoxalase activities (PubMed:12235139,
CC PubMed:12565879, PubMed:14731284, PubMed:15550391, PubMed:7848303,
CC PubMed:21696459). However, these apparently disparate activities are
CC all recruited to execute its protein deglycase primary function
CC (PubMed:26102038, PubMed:26774339). Plays an important role in
CC protecting cells from carbonyl stress, severe heat shock and
CC starvation, as well as in acid resistance of stationary-phase cells
CC (PubMed:12235139, PubMed:16796689, PubMed:17158627).
CC {ECO:0000269|PubMed:12235139, ECO:0000269|PubMed:12565879,
CC ECO:0000269|PubMed:14731284, ECO:0000269|PubMed:15550391,
CC ECO:0000269|PubMed:16796689, ECO:0000269|PubMed:17158627,
CC ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:26102038,
CC ECO:0000269|PubMed:26774339, ECO:0000269|PubMed:28596309,
CC ECO:0000269|PubMed:7848303}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC Evidence={ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:7848303};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] =
CC H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:131708; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:26102038, ECO:0000305|PubMed:26774339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) +
CC L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131709; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) +
CC L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:131710; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] =
CC glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:141553; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
CC glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:141554; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
CC glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:141555; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:26102038, ECO:0000305|PubMed:26774339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
CC lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate;
CC Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570;
CC Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate;
CC Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate;
CC Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate +
CC H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
CC H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
CC H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
CC H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-
CC COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:141580; Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O
CC = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445,
CC ChEBI:CHEBI:141578; Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-
CC COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:141581; Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O
CC = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- ACTIVITY REGULATION: The glyoxalase activity is inhibited by copper and
CC zinc cations, activated by ferrous cations, and inactivated by thiol-
CC blocking reagents (PubMed:21696459, PubMed:7848303). The aminopeptidase
CC activity is inhibited by iodoacetamide, dithiothreitol, EDTA and 1, 10-
CC phenanthroline (PubMed:15550391). Binding of ATP at high temperatures
CC induces a conformational change that reduces HchA surface
CC hydrophobicity, interferes with its ability to capture substrate
CC proteins and inhibits chaperone activity (PubMed:12235139).
CC {ECO:0000269|PubMed:12235139, ECO:0000269|PubMed:15550391,
CC ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:7848303}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for Lys-AMC (at 37 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:15550391};
CC KM=95 uM for Arg-AMC (at 37 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:15550391};
CC KM=120 uM for Ala-AMC (at 37 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:15550391};
CC KM=1.43 mM for methylglyoxal {ECO:0000269|PubMed:21696459};
CC Note=kcat is 156.9 min(-1) for glyoxalase activity with methylglyoxal
CC as substrate (PubMed:21696459). kcat is 0.43 min(-1) for
CC aminopeptidase activity with Lys-AMC as substrate. kcat is 0.51 min(-
CC 1) for aminopeptidase activity with Arg-AMC as substrate. kcat is 1.1
CC min(-1) for aminopeptidase activity with Ala-AMC as substrate
CC (PubMed:15550391). {ECO:0000269|PubMed:15550391,
CC ECO:0000269|PubMed:21696459};
CC pH dependence:
CC Optimum pH is between 6 and 8 for glyoxalase activity
CC (PubMed:21696459, PubMed:7848303). Significant inhibition of
CC glyoxalase activity below pH 5 (PubMed:21696459). Optimum pH is 8 for
CC aminopeptidase activity (PubMed:15550391).
CC {ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:21696459,
CC ECO:0000269|PubMed:7848303};
CC Temperature dependence:
CC Optimum temperature for glyoxalase activity is around 37 degrees
CC Celsius (PubMed:21696459). Optimum temperature for aminopeptidase
CC activity is around 43 degrees Celsius (PubMed:15550391).
CC {ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:21696459};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12235139,
CC ECO:0000269|PubMed:12565879, ECO:0000269|PubMed:7848303}.
CC -!- INTERACTION:
CC P31658; P0ACI6: asnC; NbExp=2; IntAct=EBI-909144, EBI-1133670;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock.
CC -!- DOMAIN: Consists of a large A domain and a smaller P domain connected
CC by a linker. The thermally induced motion of the flexible linker-loop
CC region leads to the uncovering of a high-affinity substrate-binding
CC site that is essential to capture nonnative proteins at high
CC temperatures. {ECO:0000269|PubMed:15173574}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a loss of glyoxalase
CC and reduction in aminopeptidase activity (PubMed:15550391,
CC PubMed:21696459). They accumulate methylglyoxal and are more
CC susceptible to methylglyoxal than the parent strain (PubMed:21696459).
CC Cells exhibit growth defects above 48 degrees Celsius and accumulate
CC higher levels of peptides than wild-type (PubMed:14731284,
CC PubMed:15550391). They display increased protein and DNA/RNA glycation
CC levels, and exhibit strong mutator phenotypes (PubMed:26102038,
CC PubMed:28596309). Moreover, the double and triple mutants lacking yhbO
CC and yajL, and yhbO, yajL and hchA, respectively, display impressive
CC amounts of glycated proteins, suggesting that the YhbO, YajL and Hsp31
CC deglycases display relatively redundant functions (PubMed:26774339).
CC The triple mutant displays higher glycation levels of free nucleotides
CC (GTP and dGTP) than the parental strain, and shows higher glycation
CC levels of DNA and RNA than those of single mutants (PubMed:28596309).
CC The hchA mutant cells show decreased viability in methylglyoxal- or
CC glucose-containing media (PubMed:26774339).
CC {ECO:0000269|PubMed:14731284, ECO:0000269|PubMed:15550391,
CC ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:26102038,
CC ECO:0000269|PubMed:26774339, ECO:0000269|PubMed:28596309}.
CC -!- MISCELLANEOUS: According to some authors, HchA exhibits an exceedingly
CC weak proteolytic activity against bovine serum albumin (BSA) and some
CC peptidase activity against small single amino acids conjugated to a
CC fluorogenic reporter (PubMed:12939276). Another report showed that HchA
CC does not display any significant proteolytic activity but displays a
CC physiologically relevant aminopeptidase activity (PubMed:15550391).
CC {ECO:0000305|PubMed:12939276, ECO:0000305|PubMed:15550391}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HchA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01046}.
CC -!- CAUTION: The protein deglycation activity has been ascribed to a TRIS
CC buffer artifact by a publication (PubMed:27903648), which has then been
CC rebutted by clear biochemical experiments showing that DJ-1 family
CC deglycases are bona fide deglycases (PubMed:28013050). Deglycase
CC activity is even strengthened by a novel article that reports
CC nucleotide deglycation activity (PubMed:28596309). {ECO:0000305}.
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DR EMBL; U00096; AAC75033.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15794.1; -; Genomic_DNA.
DR PIR; C64961; C64961.
DR RefSeq; NP_416476.1; NC_000913.3.
DR RefSeq; WP_000218212.1; NZ_LN832404.1.
DR PDB; 1IZY; X-ray; 2.80 A; A/B=1-283.
DR PDB; 1IZZ; X-ray; 2.31 A; A=1-283.
DR PDB; 1N57; X-ray; 1.60 A; A=1-283.
DR PDB; 1ONS; X-ray; 2.20 A; A=2-283.
DR PDB; 1PV2; X-ray; 2.71 A; A/B/C/D/E/F/G/H=1-283.
DR PDBsum; 1IZY; -.
DR PDBsum; 1IZZ; -.
DR PDBsum; 1N57; -.
DR PDBsum; 1ONS; -.
DR PDBsum; 1PV2; -.
DR AlphaFoldDB; P31658; -.
DR SMR; P31658; -.
DR BioGRID; 4260394; 23.
DR BioGRID; 850832; 1.
DR DIP; DIP-11851N; -.
DR IntAct; P31658; 32.
DR STRING; 511145.b1967; -.
DR MEROPS; C56.006; -.
DR MoonProt; P31658; -.
DR SWISS-2DPAGE; P31658; -.
DR jPOST; P31658; -.
DR PaxDb; P31658; -.
DR PRIDE; P31658; -.
DR EnsemblBacteria; AAC75033; AAC75033; b1967.
DR EnsemblBacteria; BAA15794; BAA15794; BAA15794.
DR GeneID; 66674143; -.
DR GeneID; 946481; -.
DR KEGG; ecj:JW1950; -.
DR KEGG; eco:b1967; -.
DR PATRIC; fig|1411691.4.peg.283; -.
DR EchoBASE; EB1705; -.
DR eggNOG; COG0693; Bacteria.
DR InParanoid; P31658; -.
DR OMA; PMYHLDK; -.
DR PhylomeDB; P31658; -.
DR BioCyc; EcoCyc:G7055-MON; -.
DR BioCyc; MetaCyc:G7055-MON; -.
DR BRENDA; 3.5.1.124; 2026.
DR BRENDA; 4.2.1.130; 2026.
DR EvolutionaryTrace; P31658; -.
DR PRO; PR:P31658; -.
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:0019172; F:glyoxalase III activity; IDA:EcoCyc.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR GO; GO:0036524; F:protein deglycase activity; IDA:EcoCyc.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IMP:EcoCyc.
DR GO; GO:0106044; P:guanine deglycation; IDA:EcoCyc.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IMP:EcoCyc.
DR GO; GO:0036525; P:protein deglycation; IMP:EcoCyc.
DR GO; GO:0030091; P:protein repair; IDA:EcoCyc.
DR GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
DR GO; GO:0051595; P:response to methylglyoxal; IMP:EcoCyc.
DR GO; GO:0042245; P:RNA repair; IMP:EcoCyc.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01046; Deglycase_HchA; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017283; HchA.
DR PIRSF; PIRSF037798; Chaperone_HchA; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA repair; Hydrolase; Lyase; Metal-binding; Reference proteome;
KW Stress response; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8455549"
FT CHAIN 2..283
FT /note="Protein/nucleic acid deglycase 1"
FT /id="PRO_0000209412"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14500888"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14500888"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14500888"
FT MUTAGEN 77
FT /note="E->A: Loss of glyoxalase activity."
FT /evidence="ECO:0000269|PubMed:21696459"
FT MUTAGEN 185
FT /note="C->A: Loss of glyoxalase and aminopeptidase
FT activities."
FT /evidence="ECO:0000269|PubMed:12939276,
FT ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:21696459"
FT MUTAGEN 186
FT /note="H->A: Shows approximately 17% remaining glyoxalase
FT activity compared with that of the wild-type."
FT /evidence="ECO:0000269|PubMed:21696459"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1IZZ"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1ONS"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:1N57"
FT TURN 216..221
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1IZY"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1N57"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1N57"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:1N57"
SQ SEQUENCE 283 AA; 31190 MW; 5CA8A53843A83B72 CRC64;
MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY
LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF
EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF
VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM
NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG
