DEGLY_THEKO
ID DEGLY_THEKO Reviewed; 166 AA.
AC Q5JGM7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Deglycase TK1284 {ECO:0000250|UniProtKB:Q51732};
DE EC=3.5.1.124 {ECO:0000250|UniProtKB:Q51732};
DE AltName: Full=Intracellular protease TK1284 {ECO:0000250|UniProtKB:Q51732};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q51732};
GN OrderedLocusNames=TK1284;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Deglycase that catalyzes the deglycation of the Maillard
CC adducts formed between amino groups of proteins and reactive carbonyl
CC groups of glyoxals. Thus, functions as a protein deglycase that repairs
CC methylglyoxal- and glyoxal-glycated proteins, and releases repaired
CC proteins and lactate or glycolate, respectively. Deglycates cysteine,
CC arginine and lysine residues in proteins, and thus reactivates these
CC proteins by reversing glycation by glyoxals. Acts on early glycation
CC intermediates (hemithioacetals and aminocarbinols), preventing the
CC formation of advanced glycation endproducts (AGE) that cause
CC irreversible damage. Also displays proteolytic activity.
CC {ECO:0000250|UniProtKB:Q51732}.
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:Q51732};
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:Q51732};
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:Q51732};
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:Q51732};
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:Q51732};
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:Q51732};
CC -!- SUBUNIT: Homohexamer formed by a dimer of trimers that assemble into a
CC hollow ring structure. {ECO:0000250|UniProtKB:O59413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q51732}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
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DR EMBL; AP006878; BAD85473.1; -; Genomic_DNA.
DR RefSeq; WP_011250235.1; NC_006624.1.
DR AlphaFoldDB; Q5JGM7; -.
DR SMR; Q5JGM7; -.
DR STRING; 69014.TK1284; -.
DR MEROPS; C56.001; -.
DR EnsemblBacteria; BAD85473; BAD85473; TK1284.
DR GeneID; 3235476; -.
DR KEGG; tko:TK1284; -.
DR PATRIC; fig|69014.16.peg.1256; -.
DR eggNOG; arCOG00769; Archaea.
DR HOGENOM; CLU_000445_44_4_2; -.
DR InParanoid; Q5JGM7; -.
DR OMA; YAWMREF; -.
DR OrthoDB; 98884at2157; -.
DR PhylomeDB; Q5JGM7; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..166
FT /note="Deglycase TK1284"
FT /id="PRO_0000157828"
FT DOMAIN 1..166
FT /note="PfpI endopeptidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
SQ SEQUENCE 166 AA; 18415 MW; F6FC25F20B228316 CRC64;
MKVLILSADG FEDLELIYPL HRIKEEGHEV YVASFQRGKI TGKHGYTVNV DLAFDEVDPD
EFDALVLPGG RAPEIVRLNE KAVAITKKMF EDGKPVASIC HGPQILISAG VLKGRKGTST
VTIRDDVKNA GAEWIDAEVV VDGNWVSSRH PGDLYAWMRE FVKLLR
