PRDXL_DICDI
ID PRDXL_DICDI Reviewed; 241 AA.
AC Q54SE2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=1-Cys peroxiredoxin;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P34227};
DE AltName: Full=Thiol-specific antioxidant;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
GN ORFNames=DDB_G0282517;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {ECO:0000250|UniProtKB:P34227}.
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:P34227};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P34227}.
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 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC {ECO:0000250|UniProtKB:P34227}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66118.1; -; Genomic_DNA.
DR RefSeq; XP_640097.1; XM_635005.1.
DR AlphaFoldDB; Q54SE2; -.
DR SMR; Q54SE2; -.
DR STRING; 44689.DDB0238006; -.
DR PeroxiBase; 4099; Dd1CysPrx.
DR PaxDb; Q54SE2; -.
DR EnsemblProtists; EAL66118; EAL66118; DDB_G0282517.
DR GeneID; 8623628; -.
DR KEGG; ddi:DDB_G0282517; -.
DR dictyBase; DDB_G0282517; -.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_2_1; -.
DR InParanoid; Q54SE2; -.
DR OMA; MIDYQDT; -.
DR PhylomeDB; Q54SE2; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54SE2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR CDD; cd03016; PRX_1cys; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
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; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT CHAIN 1..241
FT /note="1-Cys peroxiredoxin"
FT /id="PRO_0000331376"
FT DOMAIN 33..189
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 75
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P34227"
SQ SEQUENCE 241 AA; 27301 MW; 55F7E52F3B4166F6 CRC64;
MSRIQQVNKS ILIRSFCTGA PSKSNFSPVG NFLRIGDVVP DFSQDSSVGQ INLYKTLGDS
WGLFVSHPKD FTPICTTELG RLAKLKPEFE KRNCKILALS VDSVKDHLEW MKDIEETQKV
KINYPIIADQ DRKVADLYGM IHPNADNTFT VRSVFFISPD KRLRAQITLP ASTGRNFNEI
IRILDSFQLT DKYKVATPAD WVDGDDCIIV PTVFDEDAKK LFPKGFPKIK SYLRVTPQPN
K
