ID A0A0E0JPR0_ORYPU Unreviewed; 393 AA.
AC A0A0E0JPR0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC01G32800.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC01G32800.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC01G32800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001346};
CC -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC {ECO:0000256|ARBA:ARBA00025782}.
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DR AlphaFoldDB; A0A0E0JPR0; -.
DR STRING; 4537.A0A0E0JPR0; -.
DR EnsemblPlants; OPUNC01G32800.1; OPUNC01G32800.1; OPUNC01G32800.
DR Gramene; OPUNC01G32800.1; OPUNC01G32800.1; OPUNC01G32800.
DR eggNOG; KOG2501; Eukaryota.
DR HOGENOM; CLU_019626_0_2_1; -.
DR OMA; DIGCKKR; -.
DR Proteomes; UP000026962; Chromosome 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR004146; DC1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR PANTHER; PTHR13871:SF7; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03107; C1_2; 1.
DR Pfam; PF13905; Thioredoxin_8; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT DOMAIN 14..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 171..326
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 393 AA; 43871 MW; 7080B56AF318B014 CRC64;
MGREPEMEEA RENGGIGSVL PMSSLMSPSG NEVHISELEG KIVGLYFAAN WYPKCEAFTP
ALTAAYHRLK EHGACFEVVF VSCDENRTSF ERFHRAMPWP AVPFGDIGCK KRLSGRFQVE
GIPRLVVLAP NGEVVQHDAV ELVHRYGDRA FPFTSARVAE LEADEQRKFA SQTLEKIFSV
NGKDYVNGSQ EQVPISSLVG KTVGLYFSAH RCAPCIKFTA KLAAIYSNLK GKAEDFEIIY
IPMDKEEDGY LRSCSDMPWL ALPYDDGASS GELARYFDVR EIPTLVVVGP DGKTVTREGR
NLVNLYFDMA FPFTDEQIRL LQEMEDEDAK GYPPSLRHTG HRHELSIVSD KSGGGPYICC
ECDEQGLGWA YQCIACGYEI HLRCGRDMEG RST
//
