ID K3ZS44_SETIT Unreviewed; 544 AA.
AC K3ZS44;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881};
GN ORFNames=SETIT_2G417000v2 {ECO:0000313|EMBL:RCV14331.1};
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:RCV14331.1};
RN [1] {ECO:0000313|EMBL:RCV14331.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL26991,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV14331.1};
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:RCV14331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV14331.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL26991}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL26991};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|RuleBase:RU003881};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003881};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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DR EMBL; AGNK02001357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003529; RCV14331.1; -; Genomic_DNA.
DR AlphaFoldDB; K3ZS44; -.
DR STRING; 4555.K3ZS44; -.
DR EnsemblPlants; KQL26991; KQL26991; SETIT_029424mg.
DR Gramene; KQL26991; KQL26991; SETIT_029424mg.
DR eggNOG; KOG0404; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_031864_5_4_1; -.
DR InParanoid; K3ZS44; -.
DR OMA; QPHTEEV; -.
DR OrthoDB; 1125295at2759; -.
DR Proteomes; UP000004995; Chromosome II.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:EnsemblPlants.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:EnsemblPlants.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR CDD; cd02949; TRX_NTR; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF26; NADPH-DEPENDENT THIOREDOXIN REDUCTASE 3; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|RuleBase:RU003881};
KW Flavoprotein {ECO:0000256|RuleBase:RU003881};
KW NADP {ECO:0000256|RuleBase:RU003881};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003881};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003881};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 406..544
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 59366 MW; 5B36519F505CA9D6 CRC64;
MIHPLHTLRH QRSSQQPSRP PHPTSPLAMA VTRVAVAAAL SVAPPSSRRR RVALPSSCRP
LPTARPSKAL HAAAAPAAGA VDEETPAASP PSDPSKVVEN LVIIGSGPAG YTAAIYAARA
NLKPVVFEGY QAGGVPGGQL MTTTEVENFP GFPEGITGPD LMDRMRKQAE RWGAELHQED
VEFVNVKSSP FVIRSSDREV KCHSVIIATG ATAKRLRLPR EDEFWSRGIS ACAICDGASP
LFKGQVLAVV GGGDTATEEA IYLTKYARHV HLLVRKEQLR ASKAMQDRVL NNPNITVHFN
TEAVDVVSND KGQMSGIQLK RTDTGEESVL EVKGLFYGIG HTPNSQLLQG QIELDSTGYI
LVKEGSAKTS VDGVFAAGDV QDHEWRQAIT AAGSGCIAAL SVERYLVAND LLVEFHQPVQ
EETKKEITDK DVEMGFDISR TKHKGQYALR KIYHESPRLI CVLYTSPTCG PCRTLKPILS
KVIDEYGKYV HFVEIDIEED PEIAEAAGIM GTPCVQFFKN KEMLRTVSGV KMKKEYREFI
ESHK
//
