TDX1_CAEEL
ID TDX1_CAEEL Reviewed; 226 AA.
AC Q21824;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable peroxiredoxin prdx-3;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=Thiol-specific antioxidant protein;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxide reductase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 1 {ECO:0000305};
GN Name=prdx-3; ORFNames=R07E5.2;
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).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000250|UniProtKB:Q06830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:Q06830};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC {ECO:0000250|UniProtKB:Q06830}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:Q06830}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z32683; CAA83619.1; -; Genomic_DNA.
DR PIR; S43598; S43598.
DR RefSeq; NP_497892.1; NM_065491.4.
DR AlphaFoldDB; Q21824; -.
DR SMR; Q21824; -.
DR BioGRID; 40809; 24.
DR STRING; 6239.R07E5.2; -.
DR World-2DPAGE; 0020:Q21824; -.
DR EPD; Q21824; -.
DR PaxDb; Q21824; -.
DR PeptideAtlas; Q21824; -.
DR EnsemblMetazoa; R07E5.2.1; R07E5.2.1; WBGene00011110.
DR GeneID; 175573; -.
DR KEGG; cel:CELE_R07E5.2; -.
DR UCSC; R07E5.2.1; c. elegans.
DR CTD; 175573; -.
DR WormBase; R07E5.2; CE00657; WBGene00011110; prdx-3.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000153430; -.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; Q21824; -.
DR OMA; VRHTTCN; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; Q21824; -.
DR BRENDA; 1.11.1.24; 1045.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q21824; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011110; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..226
FT /note="Probable peroxiredoxin prdx-3"
FT /id="PRO_0000135088"
FT DOMAIN 33..191
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 78
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 78
FT /note="Interchain (with C-199); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 199
FT /note="Interchain (with C-78); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
SQ SEQUENCE 226 AA; 24932 MW; 7BEC3DE46516C615 CRC64;
MFSSAVRALC RTVPTVATRQ LSTSRALLSL RPLGPKNTVP AFKGTAVVDG DFKVISDQDY
KGKWLVMFFY PLDFTFVCPT EIIAYGDRAN EFRSLGAEVV ACSCDSHFSH LAWVNTPRKD
GGLGDMDIPL LADFNKKIAD SFGVLDKESG LSYRGLFLID PSGTVRHTTC NDLPVGRSVD
ETLRVLKAFQ FSDKHGEVCP ADWHEDSPTI KPGVATSKEY FNKVNK
