YAJL_ECOLI
ID YAJL_ECOLI Reviewed; 196 AA.
AC Q46948; Q2MC02;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein/nucleic acid deglycase 3 {ECO:0000305|PubMed:26774339, ECO:0000305|PubMed:28596309};
DE EC=3.1.2.- {ECO:0000269|PubMed:26774339};
DE EC=3.5.1.- {ECO:0000269|PubMed:28596309};
DE EC=3.5.1.124 {ECO:0000269|PubMed:26774339};
DE AltName: Full=Chaperone protein YajL;
DE AltName: Full=Maillard deglycase {ECO:0000303|PubMed:28596309};
GN Name=yajL; Synonyms=thiJ; OrderedLocusNames=b0424, JW5057;
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;
RA Backstrom A.D.;
RT "The biosynthesis of thiamin in Escherichia coli K-12: structural genes for
RT thiamin biosynthetic enzymes (thiCEFGH and thiJ) and function of the thiE
RT gene product (thiamin phosphate synthase [E.C. 2.5.1.3]).";
RL Thesis (1996), Cornell University, United States.
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 ABSENCE OF FUNCTION IN THIAMINE BIOSYNTHESIS.
RX PubMed=9592144; DOI=10.1093/nar/26.11.2606;
RA Mueller E.G., Buck C.J., Palenchar P.M., Barnhart L.E., Paulson J.L.;
RT "Identification of a gene involved in the generation of 4-thiouridine in
RT tRNA.";
RL Nucleic Acids Res. 26:2606-2610(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=20889753; DOI=10.1128/jb.01077-10;
RA Kthiri F., Gautier V., Le H.T., Prere M.F., Fayet O., Malki A.,
RA Landoulsi A., Richarme G.;
RT "Translational defects in a mutant deficient in YajL, the bacterial homolog
RT of the parkinsonism-associated protein DJ-1.";
RL J. Bacteriol. 192:6302-6306(2010).
RN [7]
RP FUNCTION AS A CHAPERONE, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-106.
RC STRAIN=K12 / BW25113;
RX PubMed=20124404; DOI=10.1074/jbc.m109.077529;
RA Kthiri F., Le H.T., Gautier V., Caldas T., Malki A., Landoulsi A., Bohn C.,
RA Bouloc P., Richarme G.;
RT "Protein aggregation in a mutant deficient in yajL, the bacterial homolog
RT of the Parkinsonism-associated protein DJ-1.";
RL J. Biol. Chem. 285:10328-10336(2010).
RN [8]
RP FUNCTION AS A CHAPERONE, SUBUNIT, AND MUTAGENESIS OF CYS-47 AND CYS-106.
RX PubMed=22157000; DOI=10.1074/jbc.m111.299198;
RA Le H.T., Gautier V., Kthiri F., Malki A., Messaoudi N., Mihoub M.,
RA Landoulsi A., An Y.J., Cha S.S., Richarme G.;
RT "YajL, prokaryotic homolog of parkinsonism-associated protein DJ-1,
RT functions as a covalent chaperone for thiol proteome.";
RL J. Biol. Chem. 287:5861-5870(2012).
RN [9]
RP FUNCTION AS A CHAPERONE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-47
RP AND CYS-106.
RX PubMed=22321799; DOI=10.1016/j.jmb.2012.01.047;
RA Gautier V., Le H.T., Malki A., Messaoudi N., Caldas T., Kthiri F.,
RA Landoulsi A., Richarme G.;
RT "YajL, the prokaryotic homolog of the Parkinsonism-associated protein DJ-1,
RT protects cells against protein sulfenylation.";
RL J. Mol. Biol. 421:662-670(2012).
RN [10]
RP FUNCTION IN DEGLYCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25416785; DOI=10.1074/jbc.m114.597815;
RA Richarme G., Mihoub M., Dairou J., Bui L.C., Leger T., Lamouri A.;
RT "Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase
RT that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine and
RT lysine residues.";
RL J. Biol. Chem. 290:1885-1897(2015).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=26377309; DOI=10.1099/mic.0.000181;
RA Messaoudi N., Gautier V., Dairou J., Mihoub M., Lelandais G., Bouloc P.,
RA Landoulsi A., Richarme G.;
RT "Fermentation and alternative respiration compensate for NADH dehydrogenase
RT deficiency in a prokaryotic model of DJ-1 associated parkinsonism.";
RL Microbiology 161:2220-2231(2015).
RN [12]
RP FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION 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 [13]
RP FUNCTION AS A GLYOXALASE, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=26678554; DOI=10.1093/femsle/fnv239;
RA Lee C., Lee J., Lee J.Y., Park C.;
RT "Characterization of the Escherichia coli YajL, YhbO and ElbB
RT glyoxalases.";
RL FEMS Microbiol. Lett. 363:0-0(2016).
RN [14]
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 [15] {ECO:0007744|PDB:2AB0}
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), OXIDATION AT CYS-106, AND SUBUNIT.
RX PubMed=16181642; DOI=10.1016/j.jmb.2005.08.033;
RA Wilson M.A., Ringe D., Petsko G.A.;
RT "The atomic resolution crystal structure of the YajL (ThiJ) protein from
RT Escherichia coli: a close prokaryotic homologue of the Parkinsonism-
RT associated protein DJ-1.";
RL J. Mol. Biol. 353:678-691(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS).
RX PubMed=27989121; DOI=10.1021/acs.biochem.6b00906;
RA Lin J., Pozharski E., Wilson M.A.;
RT "Short carboxylic acid-carboxylate hydrogen bonds can have fully localized
RT protons.";
RL Biochemistry 56:391-402(2017).
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:26774339, PubMed:28596309). Thus, functions as a protein
CC deglycase that repairs methylglyoxal- and glyoxal-glycated proteins,
CC and releases repaired proteins and lactate or glycolate, respectively.
CC Deglycates cysteine, arginine and lysine residues in proteins, and thus
CC reactivates these proteins by reversing glycation by glyoxals. Is able
CC to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate
CC dehydrogenase, and fructose biphosphate aldolase. Acts on early
CC glycation intermediates (hemithioacetals and aminocarbinols),
CC preventing the formation of Schiff bases and advanced glycation
CC endproducts (AGE) that cause irreversible damage (PubMed:25416785,
CC PubMed:26774339). Also functions as a nucleotide deglycase able to
CC repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP,
CC dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair
CC system named guanine glycation repair (GG repair), dedicated to
CC reversing methylglyoxal and glyoxal damage via nucleotide sanitization
CC and direct nucleic acid repair. However, is less efficient than Hsp31
CC and YhbO, suggesting that YajL might be preferentially dedicated to
CC protein repair (PubMed:28596309). Displays a covalent chaperone
CC activity with sulfenylated thiol proteins by forming mixed disulfides
CC with members of the thiol proteome, and preferentially with
CC sulfenylated cellular proteins, upon oxidative stress; these mixed
CC disulfides can be subsequently reduced by low-molecular-weight thiols
CC to regenerate YajL and reduced proteins (PubMed:22157000,
CC PubMed:22321799). Involved in biogenesis of ribosomal proteins,
CC probably as a ribosomal protein-folding chaperone (PubMed:20889753).
CC Confers resistance to oxidative stress (PubMed:20124404,
CC PubMed:22157000, PubMed:22321799). Plays an important role in
CC protection against electrophile/carbonyl stress (PubMed:26774339). The
CC chaperone activity reported for YajL is probably recruited to execute
CC its deglycase activity, to interact with non-native glycated proteins
CC and gain access to partially buried glycated sites (PubMed:25416785,
CC PubMed:26774339). Also displays an apparent glyoxalase activity that in
CC fact reflects its deglycase activity (PubMed:26774339,
CC PubMed:26678554). {ECO:0000269|PubMed:20124404,
CC ECO:0000269|PubMed:20889753, ECO:0000269|PubMed:22157000,
CC ECO:0000269|PubMed:22321799, ECO:0000269|PubMed:25416785,
CC ECO:0000269|PubMed:26678554, ECO:0000269|PubMed:26774339,
CC ECO:0000269|PubMed:28596309}.
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: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: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: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: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: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: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: Glyoxalase activity is inhibited by zinc ions
CC (PubMed:26678554). Active as a chaperone in both its reduced and
CC oxidized states, and is more active in its oxidized form
CC (PubMed:20124404). {ECO:0000269|PubMed:20124404,
CC ECO:0000269|PubMed:26678554}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.97 mM for glyoxal (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:26678554};
CC Note=kcat is 70.32 min(-1) for glyoxalase activity with glyoxal as
CC substrate (at pH 7.4 and 37 degrees Celsius) (PubMed:26678554). The
CC apparent kcat of methylglyoxal and glyoxal degradation is 0.08 sec(-
CC 1), and 0.15 sec(-1), respectively (at 22 degrees Celsius)
CC (PubMed:26774339). {ECO:0000269|PubMed:26678554,
CC ECO:0000269|PubMed:26774339};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16181642,
CC ECO:0000269|PubMed:22157000}.
CC -!- PTM: Cys-106 is easily oxidized to sulfinic acid.
CC {ECO:0000269|PubMed:16181642}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display highest
CC sensitivity to carbonyl stress. The yajL mutant (but not the parental
CC strain) suffers from a 100-fold decrease in viability after incubation
CC for 48 h in LB medium containing 0.6% glucose, and the mutant is
CC rescued by YajL- and DJ-1-overproducing plasmids. The wild-type strain
CC displays a small quantity of glycated proteins after overnight culture
CC in LB medium supplemented with 0.6% glucose, whereas the yajL mutant
CC displays much higher levels of glycated proteins (PubMed:25416785,
CC PubMed:26774339), and also higher DNA and RNA glycation levels
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 yajL mutant cells display decreased viability in methylglyoxal- or
CC glucose-containing media (PubMed:26774339). They also display increased
CC protein sulfenic acids levels, both before and after oxidative stress,
CC but similar protein disulfides levels (PubMed:22321799). In aerobiosis,
CC mutants show a protein aggregation phenotype, which is increased by
CC oxidative stress (PubMed:20124404). Mutants show also altered gene
CC expression and display decreased translation accuracy
CC (PubMed:20889753). The yajL deletion mutant shows a negligible NADH
CC dehydrogenase 1 activity and compensates for this low activity by
CC utilizing NADH-independent alternative dehydrogenases, including
CC pyruvate oxidase PoxB and D-aminoacid dehydrogenase DadA, and mixed
CC acid aerobic fermentations characterized by acetate, lactate, succinate
CC and ethanol excretion (PubMed:26377309). It shows up-regulation of
CC genes involved in glycolytic and pentose phosphate pathways and
CC alternative respiratory pathways (PubMed:26377309). Moreover, the yajL
CC mutant preferentially catabolizes pyruvate-forming amino acids over
CC Krebs cycle-related ones, and thus it utilizes pyruvate-centred
CC respiro-fermentative metabolism to compensate for the NADH
CC dehydrogenase 1 defect (PubMed:26377309). {ECO:0000269|PubMed:20124404,
CC ECO:0000269|PubMed:20889753, ECO:0000269|PubMed:22321799,
CC ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:26377309,
CC ECO:0000269|PubMed:26774339, ECO:0000269|PubMed:28596309}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC -!- CAUTION: Was originally (Ref.1) thought to be involved in thiamine
CC biosynthesis. However, this phenotype was probably due to an
CC artifactual recombination event involving a portion of the adjacent
CC thiI gene. {ECO:0000305}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA82704.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB40180.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U34923; AAA82704.1; ALT_INIT; Genomic_DNA.
DR EMBL; U82664; AAB40180.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73527.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76204.1; -; Genomic_DNA.
DR PIR; H64771; H64771.
DR RefSeq; NP_414958.4; NC_000913.3.
DR RefSeq; WP_001276305.1; NZ_LN832404.1.
DR PDB; 2AB0; X-ray; 1.10 A; A/B=1-196.
DR PDB; 5SY4; X-ray; 0.98 A; A/B=1-196.
DR PDBsum; 2AB0; -.
DR PDBsum; 5SY4; -.
DR AlphaFoldDB; Q46948; -.
DR SMR; Q46948; -.
DR BioGRID; 4263345; 17.
DR BioGRID; 849455; 59.
DR IntAct; Q46948; 17.
DR STRING; 511145.b0424; -.
DR jPOST; Q46948; -.
DR PaxDb; Q46948; -.
DR PRIDE; Q46948; -.
DR EnsemblBacteria; AAC73527; AAC73527; b0424.
DR EnsemblBacteria; BAE76204; BAE76204; BAE76204.
DR GeneID; 945066; -.
DR KEGG; ecj:JW5057; -.
DR KEGG; eco:b0424; -.
DR PATRIC; fig|1411691.4.peg.1853; -.
DR EchoBASE; EB3057; -.
DR eggNOG; COG0693; Bacteria.
DR HOGENOM; CLU_000445_44_2_6; -.
DR InParanoid; Q46948; -.
DR OMA; TSYPAMK; -.
DR PhylomeDB; Q46948; -.
DR BioCyc; EcoCyc:HMP-KIN-MON; -.
DR BioCyc; MetaCyc:HMP-KIN-MON; -.
DR BRENDA; 3.5.1.124; 2026.
DR BRENDA; 4.2.1.130; 2026.
DR EvolutionaryTrace; Q46948; -.
DR PRO; PR:Q46948; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0036524; F:protein deglycase activity; IDA:EcoCyc.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0036525; P:protein deglycation; IMP:EcoCyc.
DR GO; GO:0042026; P:protein refolding; IDA:EcoCyc.
DR GO; GO:0030091; P:protein repair; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR006287; DJ-1.
DR InterPro; IPR002818; DJ-1/PfpI.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01383; not_thiJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; DNA damage; DNA repair; Hydrolase; Oxidation;
KW Reference proteome; Stress response.
FT CHAIN 1..196
FT /note="Protein/nucleic acid deglycase 3"
FT /id="PRO_0000157829"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT MOD_RES 106
FT /note="Cysteine sulfinic acid (-SO2H); alternate"
FT /evidence="ECO:0000269|PubMed:16181642"
FT MUTAGEN 47
FT /note="C->A: Is not impaired in the formation of mixed
FT disulfide with a sulfenylated protein. Has a monomeric
FT quaternary structure."
FT /evidence="ECO:0000269|PubMed:22157000,
FT ECO:0000269|PubMed:22321799"
FT MUTAGEN 106
FT /note="C->A: Is impaired in the formation of mixed
FT disulfide with cytoplasmic and sulfenylated proteins. Does
FT not complement a disruption mutant."
FT /evidence="ECO:0000269|PubMed:20124404,
FT ECO:0000269|PubMed:22157000, ECO:0000269|PubMed:22321799"
FT MUTAGEN 106
FT /note="C->D: Does not complement a disruption mutant."
FT /evidence="ECO:0000269|PubMed:20124404"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:5SY4"
FT TURN 113..117
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2AB0"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:5SY4"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5SY4"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5SY4"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:5SY4"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:5SY4"
SQ SEQUENCE 196 AA; 20777 MW; 15282395CCF2CE75 CRC64;
MSASALVCLA PGSEETEAVT TIDLLVRGGI KVTTASVASD GNLAITCSRG VKLLADAPLV
EVADGEYDVI VLPGGIKGAE CFRDSTLLVE TVKQFHRSGR IVAAICAAPA TVLVPHDIFP
IGNMTGFPTL KDKIPAEQWL DKRVVWDARV KLLTSQGPGT AIDFGLKIID LLVGREKAHE
VASQLVMAAG IYNYYE
