ID A0A0A0AGI6_CHAVO Unreviewed; 189 AA.
AC A0A0A0AGI6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=protein deglycase {ECO:0000256|ARBA:ARBA00012719};
DE EC=3.5.1.124 {ECO:0000256|ARBA:ARBA00012719};
DE AltName: Full=Maillard deglycase {ECO:0000256|ARBA:ARBA00030958};
DE AltName: Full=Parkinsonism-associated deglycase {ECO:0000256|ARBA:ARBA00031312};
GN ORFNames=N301_15298 {ECO:0000313|EMBL:KGL92543.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL92543.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL92543.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL92543.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000867};
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:0000256|ARBA:ARBA00000833};
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:0000256|ARBA:ARBA00000164};
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:0000256|ARBA:ARBA00000484};
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:0000256|ARBA:ARBA00001318};
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:0000256|ARBA:ARBA00000480};
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:0000256|ARBA:ARBA00001515};
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:0000256|ARBA:ARBA00000267};
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:0000256|ARBA:ARBA00000247};
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:0000256|ARBA:ARBA00001233};
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:0000256|ARBA:ARBA00000302};
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:0000256|ARBA:ARBA00001300};
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:0000256|ARBA:ARBA00001659};
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:0000256|ARBA:ARBA00000760};
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:0000256|ARBA:ARBA00000456};
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:0000256|ARBA:ARBA00000739};
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:0000256|ARBA:ARBA00001733};
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:0000256|ARBA:ARBA00001123};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family.
CC {ECO:0000256|ARBA:ARBA00008542}.
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DR EMBL; KL871566; KGL92543.1; -; Genomic_DNA.
DR RefSeq; XP_009882375.1; XM_009884073.1.
DR AlphaFoldDB; A0A0A0AGI6; -.
DR STRING; 50402.A0A0A0AGI6; -.
DR GeneID; 104285607; -.
DR KEGG; cvf:104285607; -.
DR CTD; 11315; -.
DR OrthoDB; 1117759at2759; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036524; F:protein deglycase activity; IEA:UniProtKB-EC.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd03135; GATase1_DJ-1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR006287; DJ-1.
DR InterPro; IPR002818; DJ-1/PfpI.
DR NCBIfam; TIGR01383; not_thiJ; 1.
DR PANTHER; PTHR48094:SF12; PARKINSON DISEASE PROTEIN 7 HOMOLOG; 1.
DR PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Fertilization {ECO:0000256|ARBA:ARBA00023279};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 4..170
FT /note="DJ-1/PfpI"
FT /evidence="ECO:0000259|Pfam:PF01965"
SQ SEQUENCE 189 AA; 20011 MW; 2E21CBCC7D803353 CRC64;
MASKRALVIL AKGAEEMETV IPTDVMRRAG IKVTVAGLTG KEPVQCSRDV FICPDASLED
ARKEGPYDVV VLPGGNLGAQ NLSESSAVKD ILKDQESRKG LIAAICAGPT ALLAHGIGFG
SKVTTHPLAK DKMMNGAHYC YSESRVEKDG NILTSRGPGT SFEFGLAIVE TLMGKEVAEQ
VKAPLILKE
//
