DEGLY_PYRAB
ID DEGLY_PYRAB Reviewed; 166 AA.
AC Q9V1F8; G8ZGH3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Deglycase PYRAB04690 {ECO:0000250|UniProtKB:Q51732};
DE EC=3.5.1.124 {ECO:0000250|UniProtKB:Q51732};
DE AltName: Full=Intracellular protease PYRAB04690 {ECO:0000250|UniProtKB:Q51732};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q51732};
GN OrderedLocusNames=PYRAB04690; ORFNames=PAB0311;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49391.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69852.1; -; Genomic_DNA.
DR PIR; H75163; H75163.
DR RefSeq; WP_010867593.1; NC_000868.1.
DR AlphaFoldDB; Q9V1F8; -.
DR SMR; Q9V1F8; -.
DR STRING; 272844.PAB0311; -.
DR MEROPS; C56.001; -.
DR EnsemblBacteria; CAB49391; CAB49391; PAB0311.
DR GeneID; 1495365; -.
DR KEGG; pab:PAB0311; -.
DR PATRIC; fig|272844.11.peg.496; -.
DR eggNOG; arCOG00769; Archaea.
DR HOGENOM; CLU_000445_44_4_2; -.
DR OMA; YAWMREF; -.
DR OrthoDB; 98884at2157; -.
DR PhylomeDB; Q9V1F8; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..166
FT /note="Deglycase PYRAB04690"
FT /id="PRO_0000157825"
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; 18522 MW; C38832E1C1DC0718 CRC64;
MRVLILSADQ FEDVELIYPY HRLKEEGHEV LVASFKRGVI TGKHGYTVNV DLAFEEVNPD
EFDALVLPGG RAPERVRLNE KAVEIAKKMF SEGKPVASIC HGPQILISAG VLRGRRGTSY
PGIKDDMINA GVDWVDAEVV VDGNWVSSRV PGDLYAWMRE FVKLLK
