DEGLY_PYRFU
ID DEGLY_PYRFU Reviewed; 166 AA.
AC Q51732;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Deglycase PfpI {ECO:0000303|PubMed:27530919};
DE EC=3.5.1.124 {ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919};
DE AltName: Full=Intracellular protease I {ECO:0000303|PubMed:8626329};
DE EC=3.4.22.- {ECO:0000269|PubMed:16535492};
GN Name=pfpI {ECO:0000303|PubMed:8626329}; OrderedLocusNames=PF1719;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-28; 128-157 AND
RP 159-166, FUNCTION AS A PROTEASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8626329; DOI=10.1128/jb.178.9.2605-2612.1996;
RA Halio S.B., Blumentals I.I., Short S.A., Merrill B.M., Kelly R.M.;
RT "Sequence, expression in Escherichia coli, and analysis of the gene
RT encoding a novel intracellular protease (PfpI) from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 178:2605-2612(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP FUNCTION AS A PROTEASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=16535492; DOI=10.1128/aem.63.1.289-295.1997;
RA Halio S.B., Bauer M.W., Mukund S., Adams M., Kelly R.M.;
RT "Purification and characterization of two functional forms of intracellular
RT protease PfpI from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL Appl. Environ. Microbiol. 63:289-295(1997).
RN [4]
RP FUNCTION AS A DEGLYCASE, AND BIOTECHNOLOGY.
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).
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 (Probable). Thus, functions as a protein deglycase
CC that repairs methylglyoxal- and glyoxal-glycated proteins, and releases
CC repaired proteins and lactate or glycolate, respectively
CC (PubMed:27530919). Deglycates cysteine, arginine and lysine residues in
CC proteins, and thus reactivates these proteins by reversing glycation by
CC glyoxals (By similarity). Thus, was shown to afford full protection
CC against glycation of thioredoxin by glyoxal (PubMed:27530919). Acts on
CC early glycation intermediates (hemithioacetals and aminocarbinols),
CC preventing the formation of advanced glycation endproducts (AGE) that
CC cause irreversible damage (By similarity). Prevents acrylamide
CC formation in asparagine/glyoxal and asparagine/sugar mixtures, likely
CC by degrading asparagine/glyoxal Maillard adducts formed at high
CC temperatures (PubMed:27530919). Also displays proteolytic activity
CC (PubMed:8626329, PubMed:16535492). Cleaves at the carboxyl side of both
CC basic and hydrophobic residues in the P1 position, indicating
CC trypsin- and chymotrypsin-like specificities (PubMed:16535492).
CC {ECO:0000250|UniProtKB:P45470, ECO:0000269|PubMed:16535492,
CC ECO:0000269|PubMed:27530919, ECO:0000269|PubMed:8626329}.
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:P45470, ECO:0000305|PubMed:27530919};
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:P45470, ECO:0000305|PubMed:27530919};
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:P45470, ECO:0000305|PubMed:27530919};
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:P45470, ECO:0000305|PubMed:27530919};
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:P45470, ECO:0000305|PubMed:27530919};
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:P45470, ECO:0000305|PubMed:27530919};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.3 for proteolytic activity with AAF-MCA as substrate.
CC {ECO:0000269|PubMed:16535492};
CC Temperature dependence:
CC Optimum temperature is 84-97 degrees Celsius for proteolytic activity
CC (PubMed:8626329, PubMed:16535492). Thermostable. Displays a half-life
CC of 19 minutes at 95 degrees Celsius (PubMed:8626329).
CC {ECO:0000269|PubMed:16535492, ECO:0000269|PubMed:8626329};
CC -!- SUBUNIT: Homooligomer (PubMed:8626329). Exists in two functional
CC species: the predominant form is a homohexamer that comprises about 90%
CC of the total activity, and the minor form is trimeric
CC (PubMed:16535492). {ECO:0000269|PubMed:16535492,
CC ECO:0000269|PubMed:8626329}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8626329}.
CC -!- BIOTECHNOLOGY: Being able to prevent acrylamide formation at 100
CC degrees Celsius, this enzyme could constitute a viable and unique
CC enzymatic method to reduce acrylamide formation in food, whose presence
CC is a worldwide concern because it is carcinogenic, reprotoxic and
CC neurotoxic. The use of deglycases is not likely to affect the quality
CC parameters of foods, in contrast with methods which lead to depletion
CC of the components (asparagine and sugars) responsible for acrylamide
CC formation. Moreover, deglycases can be used directly during the thermal
CC process, which avoids a time consuming pre-incubation step.
CC Consequently, many foods whose heating processes occur at around 100
CC degrees Celsius, such as baby foods, evaporated milk, dry soups and
CC prune juices could be clients of the deglycase method.
CC {ECO:0000305|PubMed:27530919}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U57642; AAB04694.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81843.1; -; Genomic_DNA.
DR PIR; JC6003; JC6003.
DR RefSeq; WP_011012865.1; NC_018092.1.
DR AlphaFoldDB; Q51732; -.
DR SMR; Q51732; -.
DR STRING; 186497.PF1719; -.
DR MEROPS; C56.001; -.
DR EnsemblBacteria; AAL81843; AAL81843; PF1719.
DR GeneID; 41713550; -.
DR KEGG; pfu:PF1719; -.
DR PATRIC; fig|186497.12.peg.1787; -.
DR eggNOG; arCOG00769; Archaea.
DR HOGENOM; CLU_000445_44_4_2; -.
DR OMA; YAWMREF; -.
DR OrthoDB; 98884at2157; -.
DR PhylomeDB; Q51732; -.
DR BRENDA; 3.4.22.B20; 5243.
DR BRENDA; 3.5.1.124; 5243.
DR BRENDA; 4.2.1.130; 5243.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..166
FT /note="Deglycase PfpI"
FT /id="PRO_0000157826"
FT DOMAIN 1..166
FT /note="PfpI endopeptidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
SQ SEQUENCE 166 AA; 18791 MW; B4AA6FFB83FBE52F CRC64;
MKILFLSANE FEDVELIYPY HRLKEEGHEV YIASFEKGVI TGKHGYSVKV DLTFDEVNPD
EFDALVLPGG RAPERVRLNE KAVEIARKMF TEGKPVATIC HGPQILISAG VLKGRKGTSY
IGIRDDMINA GVEWIDREVV VDGNWVSSRH PGDLYAWMRE FVKLLK
