DEGLY_PYRHO
ID DEGLY_PYRHO Reviewed; 166 AA.
AC O59413;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Deglycase PH1704 {ECO:0000250|UniProtKB:Q51732};
DE EC=3.5.1.124 {ECO:0000250|UniProtKB:Q51732};
DE AltName: Full=Intracellular protease PH1704 {ECO:0000303|PubMed:11114201};
DE EC=3.4.22.- {ECO:0000305|PubMed:11114201};
GN OrderedLocusNames=PH1704;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS),
RP FUNCTION, SUBUNIT, AND ACTIVE SITE.
RX PubMed=11114201; DOI=10.1073/pnas.260503597;
RA Du X., Choi I.-G., Kim R., Wang W., Jancarik J., Yokota H., Kim S.-H.;
RT "Crystal structure of an intracellular protease from Pyrococcus horikoshii
RT at 2-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14079-14084(2000).
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 (By similarity). Also displays proteolytic activity
CC (PubMed:11114201). {ECO:0000250|UniProtKB:Q51732,
CC ECO:0000269|PubMed:11114201}.
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:0000269|PubMed:11114201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q51732}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30818.1; -; Genomic_DNA.
DR PIR; C71178; C71178.
DR RefSeq; WP_010885770.1; NC_000961.1.
DR PDB; 1G2I; X-ray; 2.00 A; A/B/C=1-166.
DR PDB; 6F2F; X-ray; 1.65 A; A/B/C=1-166.
DR PDB; 6F2H; X-ray; 2.19 A; A/B/C/D/E/F/G/H/I/J/K/L=1-166.
DR PDB; 6HF6; X-ray; 2.00 A; A/B/C=1-166.
DR PDB; 6Q3T; X-ray; 2.15 A; A/B/C=1-166.
DR PDB; 7QO8; X-ray; 1.95 A; A/B/C/D/E/F=1-166.
DR PDBsum; 1G2I; -.
DR PDBsum; 6F2F; -.
DR PDBsum; 6F2H; -.
DR PDBsum; 6HF6; -.
DR PDBsum; 6Q3T; -.
DR PDBsum; 7QO8; -.
DR AlphaFoldDB; O59413; -.
DR SMR; O59413; -.
DR STRING; 70601.3258135; -.
DR MEROPS; C56.001; -.
DR EnsemblBacteria; BAA30818; BAA30818; BAA30818.
DR GeneID; 1442551; -.
DR KEGG; pho:PH1704; -.
DR eggNOG; arCOG00769; Archaea.
DR OMA; YAWMREF; -.
DR OrthoDB; 98884at2157; -.
DR BRENDA; 3.4.11.B7; 5244.
DR BRENDA; 3.4.22.B78; 5244.
DR EvolutionaryTrace; O59413; -.
DR Proteomes; UP000000752; 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 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Protease.
FT CHAIN 1..166
FT /note="Deglycase PH1704"
FT /id="PRO_0000157827"
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:0000305|PubMed:11114201"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:6F2F"
FT STRAND 29..41
FT /evidence="ECO:0007829|PDB:6F2F"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6F2F"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:6F2F"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6F2F"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6F2F"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6F2F"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6F2F"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:6F2F"
SQ SEQUENCE 166 AA; 18624 MW; CED046ED1789808C CRC64;
MKVLFLTANE FEDVELIYPY HRLKEEGHEV YIASFERGTI TGKHGYSVKV DLTFDKVNPE
EFDALVLPGG RAPERVRLNE KAVSIARKMF SEGKPVASIC HGPQILISAG VLRGRKGTSY
PGIKDDMINA GVEWVDAEVV VDGNWVSSRV PADLYAWMRE FVKLLK
