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Protein/nucleic acid deglycase 1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Glyoxalase III) (EC 4.2.1.130) (Holding molecular chaperone) (Hsp31) (Maillard deglycase)

 HCHA_ECOLI              Reviewed;         283 AA.
P31658; P76338;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 148.
RecName: Full=Protein/nucleic acid deglycase 1 {ECO:0000305|PubMed:26774339, ECO:0000305|PubMed:28596309};
EC=3.1.2.- {ECO:0000305|PubMed:26102038, ECO:0000305|PubMed:26774339};
EC=3.5.1.- {ECO:0000269|PubMed:28596309};
EC=3.5.1.124 {ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339};
AltName: Full=Glyoxalase III {ECO:0000303|PubMed:21696459, ECO:0000303|PubMed:7848303};
EC=4.2.1.130 {ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:7848303};
AltName: Full=Holding molecular chaperone {ECO:0000303|PubMed:14731284};
AltName: Full=Hsp31 {ECO:0000303|PubMed:12235139};
AltName: Full=Maillard deglycase {ECO:0000303|PubMed:28596309};
Name=hchA; Synonyms=yedU, yzzC; OrderedLocusNames=b1967, JW1950;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097040; DOI=10.1093/dnares/3.6.379;
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 2-21.
STRAIN=K12;
PubMed=8455549; DOI=10.1007/BF00282791;
Yoshida T., Ueguchi C., Yamada H., Mizuno T.;
"Function of the Escherichia coli nucleoid protein, H-NS: molecular
analysis of a subset of proteins whose expression is enhanced in a hns
deletion mutant.";
Mol. Gen. Genet. 237:113-122(1993).
[5]
FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=7848303; DOI=10.1042/bj3050999;
Misra K., Banerjee A.B., Ray S., Ray M.;
"Glyoxalase III from Escherichia coli: a single novel enzyme for the
conversion of methylglyoxal into D-lactate without reduced
glutathione.";
Biochem. J. 305:999-1003(1995).
[6]
FUNCTION AS A CHAPERONE, SUBUNIT, AND ENZYME REGULATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12235139; DOI=10.1074/jbc.M205800200;
Sastry M.S.R., Korotkov K., Brodsky Y., Baneyx F.;
"Hsp31, the Escherichia coli yedU gene product, is a molecular
chaperone whose activity is inhibited by ATP at high temperatures.";
J. Biol. Chem. 277:46026-46034(2002).
[7]
FUNCTION AS A CHAPERONE, AND SUBUNIT.
PubMed=12565879; DOI=10.1016/S0006-291X(02)03053-X;
Malki A., Kern R., Abdallah J., Richarme G.;
"Characterization of the Escherichia coli YedU protein as a molecular
chaperone.";
Biochem. Biophys. Res. Commun. 301:430-436(2003).
[8]
FUNCTION AS A CHAPERONE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=14731284; DOI=10.1046/j.1365-2958.2003.03871.x;
Mujacic M., Bader M.W., Baneyx F.;
"Escherichia coli Hsp31 functions as a holding chaperone that
cooperates with the DnaK-DnaJ-GrpE system in the management of protein
misfolding under severe stress conditions.";
Mol. Microbiol. 51:849-859(2004).
[9]
DOMAIN.
PubMed=15173574; DOI=10.1073/pnas.0403033101;
Sastry M.S.R., Quigley P.M., Hol W.G.J., Baneyx F.;
"The linker-loop region of Escherichia coli chaperone Hsp31 functions
as a gate that modulates high-affinity substrate binding at elevated
temperatures.";
Proc. Natl. Acad. Sci. U.S.A. 101:8587-8592(2004).
[10]
FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-185.
PubMed=15550391; DOI=10.1074/jbc.M408296200;
Malki A., Caldas T., Abdallah J., Kern R., Eckey V., Kim S.J.,
Cha S.S., Mori H., Richarme G.;
"Peptidase activity of the Escherichia coli Hsp31 chaperone.";
J. Biol. Chem. 280:14420-14426(2005).
[11]
FUNCTION IN STRESS RESISTANCE.
PubMed=16796689; DOI=10.1111/j.1365-2958.2006.05207.x;
Mujacic M., Baneyx F.;
"Regulation of Escherichia coli hchA, a stress-inducible gene encoding
molecular chaperone Hsp31.";
Mol. Microbiol. 60:1576-1589(2006).
[12]
FUNCTION IN ACID STRESS RESISTANCE.
PubMed=17158627; DOI=10.1128/AEM.02429-06;
Mujacic M., Baneyx F.;
"Chaperone Hsp31 contributes to acid resistance in stationary-phase
Escherichia coli.";
Appl. Environ. Microbiol. 73:1014-1018(2007).
[13]
FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77;
CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=21696459; DOI=10.1111/j.1365-2958.2011.07736.x;
Subedi K.P., Choi D., Kim I., Min B., Park C.;
"Hsp31 of Escherichia coli K-12 is glyoxalase III.";
Mol. Microbiol. 81:926-936(2011).
[14]
CRYSTALLIZATION.
PubMed=12077448; DOI=10.1107/S0907444902007369;
Kim O.-G., Kim I.-K., Kim G.-H., Ko J., Park C., Suh P.-G.,
Kang S.-O., Lee H.-S., Cha S.-S.;
"Crystallization and preliminary X-ray crystallographic analysis of a
yedU gene product from Escherichia coli.";
Acta Crystallogr. D 58:1217-1219(2002).
[15]
FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, AND DISRUPTION
PHENOTYPE.
PubMed=26102038; DOI=10.1016/j.bbrc.2015.06.111;
Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.;
"The DJ-1 superfamily member Hsp31 repairs proteins from glycation by
methylglyoxal and glyoxal.";
Biochem. Biophys. Res. Commun. 463:1305-1310(2015).
[16]
FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, AND DISRUPTION
PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=26774339; DOI=10.1016/j.bbrc.2016.01.068;
Abdallah J., Mihoub M., Gautier V., Richarme G.;
"The DJ-1 superfamily members YhbO and YajL from Escherichia coli
repair proteins from glycation by methylglyoxal and glyoxal.";
Biochem. Biophys. Res. Commun. 470:282-286(2016).
[17]
FUNCTION AS A NUCLEOTIDE DEGLYCASE, CATALYTIC ACTIVITY, AND DISRUPTION
PHENOTYPE.
STRAIN=K12 / BW25113;
PubMed=28596309; DOI=10.1126/science.aag1095;
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N.,
Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J.,
Lamouri A.;
"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.";
Science 357:208-211(2017).
[18] {ECO:0000244|PDB:1IZY, ECO:0000244|PDB:1IZZ}
X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), PROTEOLYTIC ACTIVITY, AND
MUTAGENESIS OF CYS-185.
PubMed=12939276; DOI=10.1074/jbc.M304517200;
Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H.,
Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.;
"Crystal structures of human DJ-1 and Escherichia coli Hsp31, which
share an evolutionarily conserved domain.";
J. Biol. Chem. 278:44552-44559(2003).
[19] {ECO:0000244|PDB:1N57}
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-291.
PubMed=12621151; DOI=10.1073/pnas.0530312100;
Quigley P.M., Korotkov K., Baneyx F., Hol W.G.J.;
"The 1.6-A crystal structure of the class of chaperones represented by
Escherichia coli Hsp31 reveals a putative catalytic triad.";
Proc. Natl. Acad. Sci. U.S.A. 100:3137-3142(2003).
[20] {ECO:0000244|PDB:1ONS}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-283 IN COMPLEX WITH ZINC,
AND METAL-BINDING.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=14500888; DOI=10.1110/ps.03121403;
Zhao Y., Liu D., Kaluarachchi W.D., Bellamy H.D., White M.A.,
Fox R.O.;
"The crystal structure of Escherichia coli heat shock protein YedU
reveals three potential catalytic active sites.";
Protein Sci. 12:2303-2311(2003).
[21] {ECO:0000244|PDB:1PV2}
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS).
PubMed=14691241; DOI=10.1110/ps.03399604;
Quigley P.M., Korotkov K., Baneyx F., Hol W.G.J.;
"A new native EcHsp31 structure suggests a key role of structural
flexibility for chaperone function.";
Protein Sci. 13:269-277(2004).
-!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
deglycation of the Maillard adducts formed between amino groups of
proteins or nucleotides and reactive carbonyl groups of glyoxals
(PubMed:26102038, PubMed:26774339, PubMed:28596309). Thus,
functions as a protein deglycase that repairs methylglyoxal- and
glyoxal-glycated proteins, and releases repaired proteins and
lactate or glycolate, respectively. Deglycates cysteine, arginine
and lysine residues in proteins, and thus reactivates these
proteins by reversing glycation by glyoxals. Is able to repair
glycated serum albumin, aspartate aminotransferase,
glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate
aldolase. Acts on early glycation intermediates (hemithioacetals
and aminocarbinols), preventing the formation of Schiff bases and
advanced glycation endproducts (AGE) that cause irreversible
damage (PubMed:26102038, PubMed:26774339). Also functions as a
nucleotide deglycase able to repair glycated guanine in the free
nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus
involved in a major nucleotide repair system named guanine
glycation repair (GG repair), dedicated to reversing methylglyoxal
and glyoxal damage via nucleotide sanitization and direct nucleic
acid repair (PubMed:28596309). Has been reported to display
chaperone, peptidase and glutathione-independent glyoxalase
activities (PubMed:12235139, PubMed:12565879, PubMed:14731284,
PubMed:15550391, PubMed:7848303, PubMed:21696459). However, these
apparently disparate activities are all recruited to execute its
protein deglycase primary function (PubMed:26102038,
PubMed:26774339). Plays an important role in protecting cells from
carbonyl stress, severe heat shock and starvation, as well as in
acid resistance of stationary-phase cells (PubMed:12235139,
PubMed:16796689, PubMed:17158627). {ECO:0000269|PubMed:12235139,
ECO:0000269|PubMed:12565879, ECO:0000269|PubMed:14731284,
ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:16796689,
ECO:0000269|PubMed:17158627, ECO:0000269|PubMed:21696459,
ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339,
ECO:0000269|PubMed:28596309, ECO:0000269|PubMed:7848303}.
-!- CATALYTIC ACTIVITY: (R)-lactate = methylglyoxal + H(2)O.
{ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:7848303}.
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + (R)-lactate.
{ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339}.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + (R)-lactate.
{ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339}.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate.
{ECO:0000269|PubMed:26102038, ECO:0000269|PubMed:26774339}.
-!- ENZYME REGULATION: The glyoxalase activity is inhibited by copper
and zinc cations, activated by ferrous cations, and inactivated by
thiol-blocking reagents (PubMed:21696459, PubMed:7848303). The
aminopeptidase activity is inhibited by iodoacetamide,
dithiothreitol, EDTA and 1, 10-phenanthroline (PubMed:15550391).
Binding of ATP at high temperatures induces a conformational
change that reduces HchA surface hydrophobicity, interferes with
its ability to capture substrate proteins and inhibits chaperone
activity (PubMed:12235139). {ECO:0000269|PubMed:12235139,
ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:21696459,
ECO:0000269|PubMed:7848303}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=55 uM for Lys-AMC (at 37 degrees Celsius and pH 8.5)
{ECO:0000269|PubMed:15550391};
KM=95 uM for Arg-AMC (at 37 degrees Celsius and pH 8.5)
{ECO:0000269|PubMed:15550391};
KM=120 uM for Ala-AMC (at 37 degrees Celsius and pH 8.5)
{ECO:0000269|PubMed:15550391};
KM=1.43 mM for methylglyoxal {ECO:0000269|PubMed:21696459};
Note=kcat is 156.9 min(-1) for glyoxalase activity with
methylglyoxal as substrate (PubMed:21696459). kcat is 0.43 min(-
1) for aminopeptidase activity with Lys-AMC as substrate. kcat
is 0.51 min(-1) for aminopeptidase activity with Arg-AMC as
substrate. kcat is 1.1 min(-1) for aminopeptidase activity with
Ala-AMC as substrate (PubMed:15550391).
{ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:21696459};
pH dependence:
Optimum pH is between 6 and 8 for glyoxalase activity
(PubMed:21696459, PubMed:7848303). Significant inhibition of
glyoxalase activity below pH 5 (PubMed:21696459). Optimum pH is
8 for aminopeptidase activity (PubMed:15550391).
{ECO:0000269|PubMed:15550391, ECO:0000269|PubMed:21696459,
ECO:0000269|PubMed:7848303};
Temperature dependence:
Optimum temperature for glyoxalase activity is around 37 degrees
Celsius (PubMed:21696459). Optimum temperature for
aminopeptidase activity is around 43 degrees Celsius
(PubMed:15550391). {ECO:0000269|PubMed:15550391,
ECO:0000269|PubMed:21696459};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12235139,
ECO:0000269|PubMed:12565879, ECO:0000269|PubMed:7848303}.
-!- INTERACTION:
P0ACI6:asnC; NbExp=2; IntAct=EBI-909144, EBI-1133670;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: By heat shock.
-!- DOMAIN: Consists of a large A domain and a smaller P domain
connected by a linker. The thermally induced motion of the
flexible linker-loop region leads to the uncovering of a high-
affinity substrate-binding site that is essential to capture
nonnative proteins at high temperatures.
{ECO:0000269|PubMed:15173574}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show a loss of
glyoxalase and reduction in aminopeptidase activity
(PubMed:15550391, PubMed:21696459). They accumulate methylglyoxal
and are more susceptible to methylglyoxal than the parent strain
(PubMed:21696459). Cells exhibit growth defects above 48 degrees
Celsius and accumulate higher levels of peptides than wild-type
(PubMed:14731284, PubMed:15550391). They display increased protein
and DNA/RNA glycation levels, and exhibit strong mutator
phenotypes (PubMed:26102038, PubMed:28596309). Moreover, the
double and triple mutants lacking yhbO and yajL, and yhbO, yajL
and hchA, respectively, display impressive amounts of glycated
proteins, suggesting that the YhbO, YajL and Hsp31 deglycases
display relatively redundant functions (PubMed:26774339). The
triple mutant displays higher glycation levels of free nucleotides
(GTP and dGTP) than the parental strain, and shows higher
glycation levels of DNA and RNA than those of single mutants
(PubMed:28596309). The hchA mutant cells show decreased viability
in methylglyoxal- or glucose-containing media (PubMed:26774339).
{ECO:0000269|PubMed:14731284, ECO:0000269|PubMed:15550391,
ECO:0000269|PubMed:21696459, ECO:0000269|PubMed:26102038,
ECO:0000269|PubMed:26774339, ECO:0000269|PubMed:28596309}.
-!- MISCELLANEOUS: According to some authors, HchA exhibits an
exceedingly weak proteolytic activity against bovine serum albumin
(BSA) and some peptidase activity against small single amino acids
conjugated to a fluorogenic reporter (PubMed:12939276). Another
report showed that HchA does not display any significant
proteolytic activity but displays a physiologically relevant
aminopeptidase activity (PubMed:15550391).
{ECO:0000305|PubMed:12939276, ECO:0000305|PubMed:15550391}.
-!- SIMILARITY: Belongs to the peptidase C56 family. HchA subfamily.
{ECO:0000255|HAMAP-Rule:MF_01046}.
-!- CAUTION: The protein deglycation activity has been ascribed to a
TRIS buffer artifact by a publication (PubMed:27903648), which has
then been rebutted by clear biochemical experiments showing that
DJ-1 family deglycases are bona fide deglycases (PubMed:28013050).
Deglycase activity is even strengthened by a novel article that
reports nucleotide deglycation activity (PubMed:28596309).
{ECO:0000305}.
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EMBL; U00096; AAC75033.1; -; Genomic_DNA.
EMBL; AP009048; BAA15794.1; -; Genomic_DNA.
PIR; C64961; C64961.
RefSeq; NP_416476.1; NC_000913.3.
RefSeq; WP_000218212.1; NZ_LN832404.1.
PDB; 1IZY; X-ray; 2.80 A; A/B=1-283.
PDB; 1IZZ; X-ray; 2.31 A; A=1-283.
PDB; 1N57; X-ray; 1.60 A; A=1-283.
PDB; 1ONS; X-ray; 2.20 A; A=2-283.
PDB; 1PV2; X-ray; 2.71 A; A/B/C/D/E/F/G/H=1-283.
PDBsum; 1IZY; -.
PDBsum; 1IZZ; -.
PDBsum; 1N57; -.
PDBsum; 1ONS; -.
PDBsum; 1PV2; -.
ProteinModelPortal; P31658; -.
SMR; P31658; -.
BioGrid; 4260394; 20.
DIP; DIP-11851N; -.
IntAct; P31658; 32.
STRING; 316385.ECDH10B_2110; -.
SWISS-2DPAGE; P31658; -.
PaxDb; P31658; -.
PRIDE; P31658; -.
EnsemblBacteria; AAC75033; AAC75033; b1967.
EnsemblBacteria; BAA15794; BAA15794; BAA15794.
GeneID; 946481; -.
KEGG; ecj:JW1950; -.
KEGG; eco:b1967; -.
PATRIC; fig|1411691.4.peg.283; -.
EchoBASE; EB1705; -.
EcoGene; EG11755; hchA.
eggNOG; ENOG4105TMR; Bacteria.
eggNOG; COG0693; LUCA.
HOGENOM; HOG000221774; -.
InParanoid; P31658; -.
KO; K05523; -.
BioCyc; EcoCyc:G7055-MONOMER; -.
BioCyc; MetaCyc:G7055-MONOMER; -.
EvolutionaryTrace; P31658; -.
PRO; PR:P31658; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0019172; F:glyoxalase III activity; IDA:EcoCyc.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0036524; F:protein deglycase activity; IDA:EcoCyc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IMP:EcoCyc.
GO; GO:0006517; P:protein deglycosylation; IMP:EcoCyc.
GO; GO:0030091; P:protein repair; IDA:EcoCyc.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
GO; GO:0051595; P:response to methylglyoxal; IMP:EcoCyc.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_01046; Deglycase_HchA; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR017283; HchA.
PANTHER; PTHR11019:SF109; PTHR11019:SF109; 1.
PIRSF; PIRSF037798; Chaperone_HchA; 1.
SUPFAM; SSF52317; SSF52317; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair; Hydrolase; Lyase;
Metal-binding; Reference proteome; Stress response; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8455549}.
CHAIN 2 283 Protein/nucleic acid deglycase 1.
/FTId=PRO_0000209412.
ACT_SITE 185 185 Nucleophile. {ECO:0000305}.
METAL 86 86 Zinc. {ECO:0000269|PubMed:14500888}.
METAL 91 91 Zinc. {ECO:0000269|PubMed:14500888}.
METAL 123 123 Zinc. {ECO:0000269|PubMed:14500888}.
MUTAGEN 77 77 E->A: Loss of glyoxalase activity.
{ECO:0000269|PubMed:21696459}.
MUTAGEN 185 185 C->A: Loss of glyoxalase and
aminopeptidase activities.
{ECO:0000269|PubMed:12939276,
ECO:0000269|PubMed:15550391,
ECO:0000269|PubMed:21696459}.
MUTAGEN 186 186 H->A: Shows approximately 17% remaining
glyoxalase activity compared with that of
the wild-type.
{ECO:0000269|PubMed:21696459}.
STRAND 8 11 {ECO:0000244|PDB:1IZZ}.
STRAND 18 20 {ECO:0000244|PDB:1N57}.
HELIX 23 29 {ECO:0000244|PDB:1N57}.
STRAND 50 54 {ECO:0000244|PDB:1N57}.
STRAND 60 62 {ECO:0000244|PDB:1N57}.
STRAND 68 70 {ECO:0000244|PDB:1N57}.
HELIX 75 87 {ECO:0000244|PDB:1N57}.
STRAND 92 99 {ECO:0000244|PDB:1N57}.
HELIX 106 108 {ECO:0000244|PDB:1N57}.
HELIX 116 128 {ECO:0000244|PDB:1N57}.
HELIX 133 138 {ECO:0000244|PDB:1N57}.
STRAND 145 151 {ECO:0000244|PDB:1N57}.
HELIX 155 158 {ECO:0000244|PDB:1N57}.
HELIX 161 163 {ECO:0000244|PDB:1N57}.
HELIX 165 176 {ECO:0000244|PDB:1N57}.
STRAND 180 184 {ECO:0000244|PDB:1N57}.
HELIX 187 194 {ECO:0000244|PDB:1N57}.
STRAND 195 197 {ECO:0000244|PDB:1ONS}.
TURN 200 203 {ECO:0000244|PDB:1N57}.
HELIX 211 215 {ECO:0000244|PDB:1N57}.
TURN 216 221 {ECO:0000244|PDB:1N57}.
STRAND 222 225 {ECO:0000244|PDB:1N57}.
STRAND 227 229 {ECO:0000244|PDB:1IZY}.
HELIX 231 237 {ECO:0000244|PDB:1N57}.
STRAND 251 254 {ECO:0000244|PDB:1N57}.
STRAND 257 262 {ECO:0000244|PDB:1N57}.
HELIX 263 265 {ECO:0000244|PDB:1N57}.
HELIX 266 281 {ECO:0000244|PDB:1N57}.
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


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