ID A2XHT7_ORYSI Unreviewed; 588 AA.
AC A2XHT7;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=OsI_11974 {ECO:0000313|EMBL:EAY90397.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EAY90397.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EAY90397.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 EMBL; CM000128; EAY90397.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XHT7; -.
DR STRING; 39946.A2XHT7; -.
DR EnsemblPlants; BGIOSGA012836-TA; BGIOSGA012836-PA; BGIOSGA012836.
DR Gramene; BGIOSGA012836-TA; BGIOSGA012836-PA; BGIOSGA012836.
DR HOGENOM; CLU_019626_1_0_1; -.
DR OMA; HELHGEH; -.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03009; TryX_like_TryX_NRX; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR004146; DC1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR PANTHER; PTHR13871:SF96; NUCLEOREDOXIN 1-RELATED; 1.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR Pfam; PF03107; C1_2; 1.
DR Pfam; PF13905; Thioredoxin_8; 3.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007015}.
FT DOMAIN 1..177
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 340..507
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 563..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 65357 MW; 49D47C79EA31A9D3 CRC64;
MADAAGIATV LAADGRDFLL RNSADQLPAT RAAVRCCAIE MSHEKVKISS IEASTVALYF
SASWCPPCRR FTPKLIEAYN ELVSQGKNFE VVFVSGDKDQ EAFDAYFAKM PWLAVPFSDS
ECRAKLNKRF KVRGIPHLVI LNATSGEVYT EDGVELVTVH GTEAYPFTTE RINELKEQEK
AAKDNQTVQS VLGTPTRDYL LSNKGDRVPI SDLEGKYVGL CFVVNGYGPV VQFTSLLAKF
YEKLKEVGEK FEVVAVSLDS DEELSNESFA GMPWLAIPQE DKMGEKLARY FELRGLPTLV
LIGPDGKTLN NNVADIIDEH GQDAWEGFPF TAEKMEILAE KAKAKAELQT LESLLVIGDL
DFVLGKDGAK VPVSELVGKT VLLYFSAKWC GPCRAFLPKL VDEYNKIKEK HNDFEIIFIS
SDRDQSSYDE FFSGMPWLAL PLGDERKQHL SKTFRVRGIP SLVAIGADGR TVARDAKTPL
TAHGADAFPF TEERLLEMER KIDEMAKGWP GKLKHELHDE HELVLTRCTT YGCDGCDEMG
SSWSYRCREC DFDLHPKCAL GKEEEKKGDD EAEAEADPAC EGGVCRKA
//
