ID K4A7K9_SETIT Unreviewed; 580 AA.
AC K4A7K9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN Name=101776072 {ECO:0000313|EnsemblPlants:KQK90477};
GN ORFNames=SETIT_9G370000v2 {ECO:0000313|EMBL:RCV44391.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV44391.1};
RN [1] {ECO:0000313|EMBL:RCV44391.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK90477,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV44391.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV44391.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV44391.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK90477}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK90477};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; AGNK02005938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003536; RCV44391.1; -; Genomic_DNA.
DR RefSeq; XP_004984067.1; XM_004984010.3.
DR AlphaFoldDB; K4A7K9; -.
DR SMR; K4A7K9; -.
DR EnsemblPlants; KQK90477; KQK90477; SETIT_034860mg.
DR GeneID; 101776072; -.
DR Gramene; KQK90477; KQK90477; SETIT_034860mg.
DR KEGG; sita:101776072; -.
DR HOGENOM; CLU_019626_1_0_1; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000004995; Chromosome IX.
DR ExpressionAtlas; K4A7K9; baseline.
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:UP000004995}.
FT DOMAIN 1..176
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 329..489
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 580 AA; 64178 MW; 6A0184DC7F7E43F7 CRC64;
MAEAAPTTNG GGGGIGTILA AGDRDFLVRN SGEQVKISSI EASPVALYFS ASWCPPCRRF
TPKLIEAYKE LASQGKSFEV VFVSGDQDEE AFNEYFAKMP WLAVPFSDSE GREALDGRFK
VSGIPHLVIL DAKTGEVYTE DGVGLVSEYG VEAYPFTPER INELKEQEKA AKENQTIKSV
LGTSTRDYLI TSKGDKVPIS ELEGKYVGLC FVVPGYGPVD EFISVLAKIY EKLKEVGEKF
EVVAVSLDSD ESSFNESLAK MPWLAIPQGD KMCEKLVRYF ELRTLPTLVL IGTDGKTLNT
NVADIIEEHG FEAWEGFPFS AEKLETLAEK AKAKAASQTL ESLLISGDLD FVIGKGGAKV
PVSELVGKTV LLYFSAKWCG PCRAFLPMLV KEYNKIKEKH SDFEIVFISS DSDQSSFDEF
FTEMPWLALP LEDERKAFLE KTFRIRGIPS LVAIGPNGQT VSRDAKAQLM IHGAEAFPFT
EERLEELQKE LDEMAKGWPE KLKHELHEEH ELVLERRGTF CCDGCEEMGN TWSYSCNKCD
FDLHPKCALA EEEKKGEEDG KAAEETPAGY VCEGGVCRKA
//
