ID I1JSZ5_SOYBN Unreviewed; 423 AA.
AC I1JSZ5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=GLYMA_04G021000 {ECO:0000313|EMBL:KRH60996.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH60996.1};
RN [1] {ECO:0000313|EMBL:KRH60996.1, ECO:0000313|EnsemblPlants:KRH60996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH60996};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH60996.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH60996}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH60996};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH60996.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH60996.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000837; KRH60996.1; -; Genomic_DNA.
DR AlphaFoldDB; I1JSZ5; -.
DR SMR; I1JSZ5; -.
DR STRING; 3847.I1JSZ5; -.
DR PaxDb; 3847-GLYMA04G02330-1; -.
DR EnsemblPlants; KRH60996; KRH60996; GLYMA_04G021000.
DR Gramene; KRH60996; KRH60996; GLYMA_04G021000.
DR eggNOG; KOG2501; Eukaryota.
DR HOGENOM; CLU_019626_0_2_1; -.
DR InParanoid; I1JSZ5; -.
DR OMA; HACMPWL; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000008827; Chromosome 4.
DR ExpressionAtlas; I1JSZ5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR004146; DC1.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 157..351
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 361..413
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
SQ SEQUENCE 423 AA; 47766 MW; 12D9B005CA97AD29 CRC64;
MKAEMKDGAP QVVMNHNGNH GKFSHLLASQ DRDYLLSPTG AQVKVSDLEG KVVGLLFAAN
WYPPCRGFTQ VLAGIYEELK SRVPQFEIVY VSSDEDLNAF NSFYGSMPWI AIPFSDLETK
KSLTRKFDVE AVPCLILLQP DDRKEHATVR DGVELIYRYG IQAYPFSKDR LEQLQKEDKV
KRDNQTLTNL LANHHRDYVL SHTHTGLKKV PVASLVGKTI GLYFSAEWCV PCAKFTPKLI
SVYEKIKHEL AEKGEEDFEV VLISSDRDQA SFDSYYSTMP WLALPFGDPE IKNLVRHYNV
QGIPWLVIIG PDGKTITVHG RSLINLYQEN AYPFTKAKVE ELEKQLEEEA KGLPALVYHQ
GHRHDLNLVS DGNGGGPFIC CVCDEQGSSW AYQCLQCGYE VHPKCVRTVE RDDNVLVDTT
GCF
//
