YAJL_SALTY
ID YAJL_SALTY Reviewed; 196 AA.
AC P55880;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein/nucleic acid deglycase YajL {ECO:0000250|UniProtKB:Q46948};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:Q46948};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q46948};
DE EC=3.5.1.124 {ECO:0000250|UniProtKB:Q46948};
DE AltName: Full=Chaperone protein YajL;
DE AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q46948};
GN Name=yajL; OrderedLocusNames=STM0433;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-196.
RA Metcalf W.W., Jiang W., Wanner B.L.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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. Thus,
CC functions as a protein deglycase that repairs methylglyoxal- and
CC glyoxal-glycated proteins, and releases repaired proteins and lactate
CC or glycolate, respectively. Deglycates cysteine, arginine and lysine
CC residues in proteins, and thus reactivates these proteins by reversing
CC glycation by glyoxals. Is able to repair glycated serum albumin,
CC collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose
CC 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. 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. Displays a covalent chaperone activity with
CC sulfenylated thiol proteins by forming mixed disulfides with members of
CC the thiol proteome, and preferentially with sulfenylated cellular
CC proteins, upon oxidative stress; these mixed disulfides can be
CC subsequently reduced by low-molecular-weight thiols to regenerate YajL
CC and reduced proteins. Involved in biogenesis of ribosomal proteins,
CC probably as a ribosomal protein-folding chaperone. Confers resistance
CC to oxidative stress. Plays an important role in protection against
CC electrophile/carbonyl stress. The chaperone activity reported for YajL
CC is probably recruited to execute its deglycase activity, to interact
CC with non-native glycated proteins and gain access to partially buried
CC glycated sites. Also displays an apparent glyoxalase activity that in
CC fact reflects its deglycase activity. {ECO:0000250|UniProtKB:Q46948}.
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
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:0000250|UniProtKB:Q46948};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q46948}.
CC -!- PTM: Cys-106 is easily oxidized to sulfinic acid.
CC {ECO:0000250|UniProtKB:Q46948}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
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DR EMBL; AE006468; AAL19387.1; -; Genomic_DNA.
DR EMBL; U69493; AAB39640.1; -; Genomic_DNA.
DR PIR; T46945; T46945.
DR RefSeq; NP_459428.1; NC_003197.2.
DR RefSeq; WP_001275806.1; NC_003197.2.
DR AlphaFoldDB; P55880; -.
DR SMR; P55880; -.
DR STRING; 99287.STM0433; -.
DR PaxDb; P55880; -.
DR EnsemblBacteria; AAL19387; AAL19387; STM0433.
DR GeneID; 1251952; -.
DR KEGG; stm:STM0433; -.
DR PATRIC; fig|99287.12.peg.462; -.
DR HOGENOM; CLU_000445_44_2_6; -.
DR OMA; TSYPAMK; -.
DR PhylomeDB; P55880; -.
DR BioCyc; SENT99287:STM0433-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Chaperone; DNA damage; DNA repair; Hydrolase; Oxidation;
KW Reference proteome; Stress response.
FT CHAIN 1..196
FT /note="Protein/nucleic acid deglycase YajL"
FT /id="PRO_0000157830"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q46948"
FT MOD_RES 106
FT /note="Cysteine sulfinic acid (-SO2H); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q46948"
SQ SEQUENCE 196 AA; 20767 MW; C4B239015257E176 CRC64;
MSAQALVCLA PGSEETEAVT TIDLLVRGGI HVTTASVASD GNLTIVCSRG VKLLADAPLV
EVADGDYDII VLPGGIKGAE CFRDSPLLVE TVKQFHRSGR IVAAICAAAA TVLVPHDIFP
IGNMTGFPAL KDKIPAEQWL DKRVVWDARV KLLTSQGPGT AIDFGLKIID LLAGREKAHE
VASQLVMAAG IYNYYE
