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Database: UniProt
Entry: A0A0E0NG19_ORYRU
LinkDB: A0A0E0NG19_ORYRU
Original site: A0A0E0NG19_ORYRU 
ID   A0A0E0NG19_ORYRU        Unreviewed;       261 AA.
AC   A0A0E0NG19;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI02G20500.2, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI02G20500.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A0E0NG19; -.
DR   SMR; A0A0E0NG19; -.
DR   EnsemblPlants; ORUFI02G20500.2; ORUFI02G20500.2; ORUFI02G20500.
DR   Gramene; ORUFI02G20500.2; ORUFI02G20500.2; ORUFI02G20500.
DR   HOGENOM; CLU_042529_21_0_1; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF168; 2-CYS PEROXIREDOXIN BAS1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022}.
FT   DOMAIN          68..227
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   261 AA;  28097 MW;  5F0CA432FDA0007B CRC64;
     MAACCSSLAT AVSSSSAKPL AGIPPAAPHS LSLPRAPAAR PLRLSASSSR SARASSFVAR
     AGGVDDAPLV GNKAPDFDAE AVFDQEFINV KLSDYIGKKY VILFFYPLDF TFVCPTEITA
     FSDRYDEFEK LNTEILGVSI DSVFSHLAWV QTDRKSGGLG DLKYPLISDV TKSISKSFGV
     LIPDQGIALR GLFIIDKEGV IQHSTINNLA IGRSVDETMR TLQALQYVQD NPDEVCPAGW
     KPGDKSMKPD PKGSKEYFAA I
//
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