YHBO_ECOLI
ID YHBO_ECOLI Reviewed; 172 AA.
AC P45470; Q2M957;
DT 01-NOV-1995, 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 2 {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=Maillard deglycase {ECO:0000303|PubMed:28596309};
GN Name=yhbO; OrderedLocusNames=b3153, JW5529;
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 / 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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-9, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16380269; DOI=10.1016/j.pep.2005.11.011;
RA Abdallah J., Kern R., Malki A., Eckey V., Richarme G.;
RT "Cloning, expression, and purification of the general stress protein YhbO
RT from Escherichia coli.";
RL Protein Expr. Purif. 47:455-460(2006).
RN [4]
RP FUNCTION IN STRESS RESISTANCE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-104.
RX PubMed=17933887; DOI=10.1128/jb.01208-07;
RA Abdallah J., Caldas T., Kthiri F., Kern R., Richarme G.;
RT "YhbO protects cells against multiple stresses.";
RL J. Bacteriol. 189:9140-9144(2007).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=27530919; DOI=10.1016/j.bbrc.2016.08.077;
RA Richarme G., Marguet E., Forterre P., Ishino S., Ishino Y.;
RT "DJ-1 family Maillard deglycases prevent acrylamide formation.";
RL Biochem. Biophys. Res. Commun. 478:1111-1116(2016).
RN [7]
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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-172.
RX PubMed=14649299; DOI=10.1023/a:1026177202925;
RA Abergel C., Coutard B., Byrne D., Chenivesse S., Claude J.-B.,
RA Deregnaucourt C., Fricaux T., Gianesini-Boutreux C., Jeudy S., Lebrun R.,
RA Maza C., Notredame C., Poirot O., Suhre K., Varagnol M., Claverie J.-M.;
RT "Structural genomics of highly conserved microbial genes of unknown
RT function in search of new antibacterial targets.";
RL J. Struct. Funct. Genomics 4:141-157(2003).
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 advanced glycation endproducts (AGE) that
CC cause irreversible damage (PubMed:26774339). Also functions as a
CC 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). In vitro, prevents acrylamide formation in
CC asparagine/glyoxal and asparagine/sugar mixtures at 55 degrees Celsius,
CC likely by degrading asparagine/glyoxal Maillard adducts formed at high
CC temperatures (PubMed:27530919). Also displays an apparent glyoxalase
CC activity that in fact reflects its deglycase activity (PubMed:26774339,
CC PubMed:26678554). Is a general stress protein; is required for the
CC protection of bacterial cells against many environmental stresses,
CC including oxidative, thermal, osmotic, UV, and pH stresses
CC (PubMed:17933887). And plays an important role in protection against
CC electrophile/carbonyl stress (PubMed:26774339).
CC {ECO:0000269|PubMed:17933887, ECO:0000269|PubMed:26678554,
CC ECO:0000269|PubMed:26774339, ECO:0000269|PubMed:27530919,
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 at
CC pH 7.0. {ECO:0000269|PubMed:26678554}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for glyoxal (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:26678554};
CC KM=0.06 mM for methylglyoxal (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:26678554};
CC Note=kcat is 118.44 min(-1) and 20.80 min (-1) for glyoxalase
CC activity with glyoxal (GO) and methylglyoxal (MGO) as substrate,
CC respectively (at pH 7.4 and 37 degrees Celsius) (PubMed:26678554).
CC The apparent kcat of MGO and GO degradation is 0.29 sec(-1), and 0.42
CC sec(-1), respectively (at 22 degrees Celsius) (PubMed:26774339).
CC {ECO:0000269|PubMed:26678554, ECO:0000269|PubMed:26774339};
CC -!- SUBUNIT: Exists in monomeric, trimeric, and hexameric forms.
CC {ECO:0000269|PubMed:16380269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16380269}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are highly sensitive to
CC oxidative, thermal, UV, and pH stresses, but only slightly sensitive to
CC salt stress and insensitive to cold stress (PubMed:17933887). They
CC display increased protein glycation levels, and decreased viability in
CC methylglyoxal- or glucose-containing media (PubMed:26774339). They also
CC show highly increased DNA and RNA glycation levels, and exhibit strong
CC mutator phenotypes (PubMed:28596309). Moreover, the double and triple
CC mutants lacking yhbO and yajL, and yhbO, yajL and hchA, respectively,
CC display impressive amounts of glycated proteins, suggesting that the
CC YhbO, YajL and Hsp31 deglycases display relatively redundant functions
CC (PubMed:26774339). The triple mutant displays higher glycation levels
CC of free nucleotides (GTP and dGTP) than the parental strain, and shows
CC higher glycation levels of DNA and RNA than those of single mutants
CC (PubMed:28596309). {ECO:0000269|PubMed:17933887,
CC ECO:0000269|PubMed:26774339}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {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=AAA57956.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57956.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76187.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77199.1; -; Genomic_DNA.
DR RefSeq; NP_417622.2; NC_000913.3.
DR RefSeq; WP_000037608.1; NZ_STEB01000012.1.
DR PDB; 1OI4; X-ray; 2.03 A; A/B=2-172.
DR PDBsum; 1OI4; -.
DR AlphaFoldDB; P45470; -.
DR SMR; P45470; -.
DR BioGRID; 4259270; 10.
DR DIP; DIP-12263N; -.
DR STRING; 511145.b3153; -.
DR MEROPS; C56.976; -.
DR jPOST; P45470; -.
DR PaxDb; P45470; -.
DR PRIDE; P45470; -.
DR EnsemblBacteria; AAC76187; AAC76187; b3153.
DR EnsemblBacteria; BAE77199; BAE77199; BAE77199.
DR GeneID; 66672946; -.
DR GeneID; 947666; -.
DR KEGG; ecj:JW5529; -.
DR KEGG; eco:b3153; -.
DR PATRIC; fig|1411691.4.peg.3577; -.
DR EchoBASE; EB2637; -.
DR eggNOG; COG0693; Bacteria.
DR HOGENOM; CLU_000445_44_4_6; -.
DR InParanoid; P45470; -.
DR OMA; YAWMREF; -.
DR PhylomeDB; P45470; -.
DR BioCyc; EcoCyc:G7647-MON; -.
DR BioCyc; MetaCyc:G7647-MON; -.
DR BRENDA; 3.5.1.124; 2026.
DR BRENDA; 4.2.1.130; 2026.
DR EvolutionaryTrace; P45470; -.
DR PRO; PR:P45470; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0019172; F:glyoxalase III activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0036524; F:protein deglycase activity; IDA:EcoCyc.
DR GO; GO:0006281; P:DNA repair; IMP:EcoCyc.
DR GO; GO:0106044; P:guanine deglycation; IDA:EcoCyc.
DR GO; GO:0036525; P:protein deglycation; IMP:EcoCyc.
DR GO; GO:0030091; P:protein repair; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR GO; GO:0009268; P:response to pH; IMP:EcoCyc.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR006286; C56_PfpI.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR PANTHER; PTHR42733; PTHR42733; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01382; PfpI; 1.
DR PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW Hydrolase; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16380269"
FT CHAIN 2..172
FT /note="Protein/nucleic acid deglycase 2"
FT /id="PRO_0000157831"
FT DOMAIN 3..171
FT /note="PfpI endopeptidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P31658"
FT MUTAGEN 104
FT /note="C->A: Unable to complement the gene deletion mutant,
FT in contrast to the wild-type allele that rescues the
FT oxidative-stress and thermal-stress sensitive phenotypes."
FT /evidence="ECO:0000269|PubMed:17933887"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1OI4"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1OI4"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1OI4"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1OI4"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1OI4"
SQ SEQUENCE 172 AA; 18858 MW; CF9E2E405788125E CRC64;
MSKKIAVLIT DEFEDSEFTS PADEFRKAGH EVITIEKQAG KTVKGKKGEA SVTIDKSIDE
VTPAEFDALL LPGGHSPDYL RGDNRFVTFT RDFVNSGKPV FAICHGPQLL ISADVIRGRK
LTAVKPIIID VKNAGAEFYD QEVVVDKDQL VTSRTPDDLP AFNREALRLL GA
