DJ12_CAEEL
ID DJ12_CAEEL Reviewed; 186 AA.
AC O16228;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glutathione-independent glyoxalase DJR-1.2 {ECO:0000303|PubMed:22523093};
DE EC=4.2.1.130 {ECO:0000269|PubMed:22523093};
DE AltName: Full=Protein DJ-1 homolog 2;
GN Name=djr-1.2 {ECO:0000312|WormBase:C49G7.11}; ORFNames=C49G7.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22523093; DOI=10.1093/hmg/dds155;
RA Lee J.Y., Song J., Kwon K., Jang S., Kim C., Baek K., Kim J., Park C.;
RT "Human DJ-1 and its homologs are novel glyoxalases.";
RL Hum. Mol. Genet. 21:3215-3225(2012).
RN [3]
RP INDUCTION.
RX PubMed=23624124; DOI=10.1016/j.gene.2013.04.032;
RA Lee J.Y., Kim C., Kim J., Park C.;
RT "DJR-1.2 of Caenorhabditis elegans is induced by DAF-16 in the dauer
RT state.";
RL Gene 524:373-376(2013).
CC -!- FUNCTION: Catalyzes the conversion of methylglyoxal (MG) or glyoxal
CC (GO) to D-lactate or glycolic acid respectively in a single glutathione
CC (GSH)-independent step. May play a role in detoxifying endogenously
CC produced glyoxals. Involved in protection against glyoxal-induced cell
CC death. Protects dopaminergic neurons from glyoxal-dependent neuronal
CC degeneration. {ECO:0000269|PubMed:22523093,
CC ECO:0000269|PubMed:23624124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC Evidence={ECO:0000269|PubMed:22523093};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 mM for methylglyoxal {ECO:0000269|PubMed:22523093};
CC KM=0.78 mM for glyoxal {ECO:0000269|PubMed:22523093};
CC Note=kcat is 60.0 min(-1) with methylglyoxal as substrate and 146.4
CC min(-1) with glyoxal as substrate. {ECO:0000269|PubMed:22523093};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22523093}.
CC -!- TISSUE SPECIFICITY: Expressed in various tissues, including pharyngeal
CC muscles, pharynx-intestinal valve, ventral nerve cord, spermatheca,
CC rectal gland, inner labial (IL) cells of head neurons, phasmid
CC (PHA/PHB) neurons in tail and supporting sheath/socket cells, as well
CC as in head mesodermal cells (HMC), excretory canals and coelomocytes.
CC {ECO:0000269|PubMed:22523093}.
CC -!- INDUCTION: Induced by DAF-16 during starvation as well as in the dauer
CC stage. {ECO:0000269|PubMed:23624124}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. DJ-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; FO080906; CCD67692.1; -; Genomic_DNA.
DR PIR; T03871; T03871.
DR RefSeq; NP_504132.1; NM_071731.1.
DR AlphaFoldDB; O16228; -.
DR SMR; O16228; -.
DR STRING; 6239.C49G7.11; -.
DR PaxDb; O16228; -.
DR PeptideAtlas; O16228; -.
DR EnsemblMetazoa; C49G7.11.1; C49G7.11.1; WBGene00016789.
DR GeneID; 183625; -.
DR KEGG; cel:CELE_C49G7.11; -.
DR UCSC; C49G7.11; c. elegans.
DR CTD; 183625; -.
DR WormBase; C49G7.11; CE08869; WBGene00016789; djr-1.2.
DR eggNOG; KOG2764; Eukaryota.
DR GeneTree; ENSGT00390000001231; -.
DR HOGENOM; CLU_000445_44_2_1; -.
DR InParanoid; O16228; -.
DR OMA; PVKCAKG; -.
DR OrthoDB; 1165707at2759; -.
DR PhylomeDB; O16228; -.
DR PRO; PR:O16228; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00016789; Expressed in larva and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019172; F:glyoxalase III activity; IEA:UniProtKB-EC.
DR GO; GO:0036471; P:cellular response to glyoxal; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097238; P:cellular response to methylglyoxal; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046295; P:glycolate biosynthetic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:1903189; P:glyoxal metabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019249; P:lactate biosynthetic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0009438; P:methylglyoxal metabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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 Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01383; not_thiJ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..186
FT /note="Glutathione-independent glyoxalase DJR-1.2"
FT /id="PRO_0000432109"
FT ACT_SITE 20
FT /evidence="ECO:0000250|UniProtKB:Q10356"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:Q10356"
FT ACT_SITE 124
FT /evidence="ECO:0000250|UniProtKB:Q10356"
SQ SEQUENCE 186 AA; 19556 MW; DE31E1AF30C011E3 CRC64;
MAAQKSALIL LPPEDAEEIE VIVTGDVLVR GGLQVLYAGS STEPVKCAKG ARIVPDVALK
DVKNKTFDII IIPGGPGCSK LAECPVIGEL LKTQVKSGGL IGAICAGPTV LLAHGIVAER
VTCHYTVKDK MTEGGYKYLD DNVVISDRVI TSKGPGTAFE FALKIVETLE GPEKTNSLLK
PLCLAK
