ID A0A078GRY6_BRANA Unreviewed; 390 AA.
AC A0A078GRY6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN Name=BnaA01g05980D {ECO:0000313|EMBL:CDY28251.1};
GN ORFNames=GSBRNA2T00039986001 {ECO:0000313|EMBL:CDY28251.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY28251.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY28251.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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; LK032216; CDY28251.1; -; Genomic_DNA.
DR RefSeq; XP_013650181.1; XM_013794727.1.
DR RefSeq; XP_013650182.1; XM_013794728.1.
DR RefSeq; XP_013650184.1; XM_013794730.1.
DR RefSeq; XP_013650185.1; XM_013794731.1.
DR RefSeq; XP_013650186.1; XM_013794732.1.
DR RefSeq; XP_013650187.1; XM_013794733.1.
DR AlphaFoldDB; A0A078GRY6; -.
DR STRING; 3708.A0A078GRY6; -.
DR PaxDb; 3708-A0A078GRY6; -.
DR EnsemblPlants; CDY28251; CDY28251; GSBRNA2T00039986001.
DR Gramene; CDY28251; CDY28251; GSBRNA2T00039986001.
DR OMA; NAPCRQF; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
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; 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 InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR PANTHER; PTHR13871:SF81; NUCLEOREDOXIN 3-RELATED; 1.
DR PANTHER; PTHR13871; THIOREDOXIN; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028999}.
FT DOMAIN 17..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 390 AA; 44927 MW; 1FAB40B63FC35CD0 CRC64;
MAVTADYQVQ FPENDDIYSI LAAEGIEFLL SHSGEVPLEY IHGKTICLFF SANWCRPCKD
FTPELVKLYE SLQKRGEELE IIFVSFDHDM TLFYEHFWSM PWLAVPFSLS LRNKLTDKYR
VARIPSLVPL YPDEISVADD VIGLIEDYGP EAFPFTKKRK EELKAIDESK RVGGQLEKLL
THETRSYVVS RNGSKVLVSD LVGKTIGLYF GAHWCPPFRS FTSQLIDVYN ELTISTKGSF
EVILVSTDRD AREFNINMTN MPWLAIPYED RTRQDLCRIF NIKLIPALVI IGPEEKTVCT
NAREMVSLYG SRSYPFTESR VAELEACLKK EGDSFPRKVK DKKHEHELKL DMAKGYVCDF
CKKQGKFWAF SCDACDYDLH PTCVEEQEEQ
//
