ID R4G853_RHOPR Unreviewed; 195 AA.
AC R4G853;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA75938.1};
RN [1] {ECO:0000313|EMBL:JAA75938.1}
RP NUCLEOTIDE SEQUENCE.
RA Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA Azambuja P., Braz G.R.C., Oliveira P.L.;
RT "An insight into the transcriptome of the digestive tract of the blood
RT sucking bug, Rhodnius prolixus.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:RPRC007595-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. {ECO:0000256|PIRNR:PIRNR000239}.
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:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACPB03016202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GAHY01001572; JAA75938.1; -; mRNA.
DR AlphaFoldDB; R4G853; -.
DR STRING; 13249.R4G853; -.
DR EnsemblMetazoa; RPRC007595-RA; RPRC007595-PA; RPRC007595.
DR VEuPathDB; VectorBase:RPRC007595; -.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; R4G853; -.
DR OMA; HYAFGDV; -.
DR OrthoDB; 47465at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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 PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT DOMAIN 3..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 195 AA; 21779 MW; D5AB1C1C27DDC92A CRC64;
MTPKLQKPAP AFTTVAVVND DFKEISLSDY KGKYVVLFFY PLDFTFVCPT EIVAFSDRAE
DFRKIDCEVL AASCDSQYSH LAWINTPRNQ GGLGKMDIPI LADKSGKIAK EYGIFDEDSG
IPFRGLFIID KKQNLRQITV NDLPVGRSVD ETLRLVQAFQ YTDQHGEVCP ANWHPGKKGM
KADPAGAAEY FKAES
//
