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NADPH-dependent thioredoxin reductase 3 (NTR3) (EC 1.8.1.9) (NADPH-dependent thioredoxin reductase C) (ANTR-C) (AtNTRC)

 TRXB3_ARATH             Reviewed;         529 AA.
O22229; Q0WM62; Q93ZQ1;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
25-OCT-2017, entry version 123.
RecName: Full=NADPH-dependent thioredoxin reductase 3;
Short=NTR3;
EC=1.8.1.9;
AltName: Full=NADPH-dependent thioredoxin reductase C;
Short=ANTR-C;
Short=AtNTRC;
Flags: Precursor;
Name=NTRC; OrderedLocusNames=At2g41680; ORFNames=T32G6.20;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-529.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BAS1.
PubMed=16884685; DOI=10.1016/j.bbrc.2006.07.088;
Moon J.C., Jang H.H., Chae H.B., Lee J.R., Lee S.Y., Jung Y.J.,
Shin M.R., Lim H.S., Chung W.S., Yun D.-J., Lee K.O., Lee S.Y.;
"The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an
electron donor to 2-Cys peroxiredoxins in chloroplasts.";
Biochem. Biophys. Res. Commun. 348:478-484(2006).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18625226; DOI=10.1016/j.febslet.2008.07.006;
Stenbaek A., Hansson A., Wulff R.P., Hansson M., Dietz K.J.,
Jensen P.E.;
"NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are
needed for the protection of Mg-protoporphyrin monomethyl ester
cyclase.";
FEBS Lett. 582:2773-2778(2008).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19470473; DOI=10.1073/pnas.0903559106;
Michalska J., Zauber H., Buchanan B.B., Cejudo F.J., Geigenberger P.;
"NTRC links built-in thioredoxin to light and sucrose in regulating
starch synthesis in chloroplasts and amyloplasts.";
Proc. Natl. Acad. Sci. U.S.A. 106:9908-9913(2009).
-!- FUNCTION: Thioredoxin reductase (TR) that exhibits both TR and
thioredoxin (Trx) activities. Contains a C-terminal functional Trx
domain. Functions as an electron donor for plastidial 2-Cys
peroxiredoxins and participates in a NADPH-dependent hydrogen
peroxide scavenging system in chloroplasts in the dark. Required
for chlorophyll biosynthesis and biogenesis of the photosynthetic
apparatus. Activates aerobic cyclase which converts Mg-
protoporhyrin monomethyl ester into protochlorophyllide. Involved
in a light-dependent regulation of starch biosynthesis by redox
activation of the ADP-glucose pyrophosphorylase (AGPase), a
central enzyme of starch synthesis. {ECO:0000269|PubMed:16884685,
ECO:0000269|PubMed:18625226, ECO:0000269|PubMed:19470473}.
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBUNIT: May homodimerize. Interacts with the 2-Cys peroxiredoxin
BAS1. {ECO:0000269|PubMed:16884685}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:16884685}.
-!- DISRUPTION PHENOTYPE: Dwarf plants with chlorotic leaves.
Accumulation of Mg-protoporhyrin after feeding with 5-
aminolevulinic acid. {ECO:0000269|PubMed:18625226,
ECO:0000269|PubMed:19470473}.
-!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC002510; AAB84351.2; -; Genomic_DNA.
EMBL; CP002685; AEC10015.1; -; Genomic_DNA.
EMBL; AY056394; AAL08250.1; -; mRNA.
EMBL; BT000516; AAN18085.1; -; mRNA.
EMBL; AK229969; BAF01794.1; -; mRNA.
PIR; T00824; T00824.
RefSeq; NP_565954.1; NM_129731.6.
UniGene; At.12409; -.
UniGene; At.42799; -.
ProteinModelPortal; O22229; -.
SMR; O22229; -.
BioGrid; 4103; 14.
IntAct; O22229; 10.
STRING; 3702.AT2G41680.1; -.
PaxDb; O22229; -.
EnsemblPlants; AT2G41680.1; AT2G41680.1; AT2G41680.
GeneID; 818766; -.
Gramene; AT2G41680.1; AT2G41680.1; AT2G41680.
KEGG; ath:AT2G41680; -.
Araport; AT2G41680; -.
TAIR; locus:2062683; AT2G41680.
eggNOG; KOG0404; Eukaryota.
eggNOG; KOG0907; Eukaryota.
eggNOG; COG0492; LUCA.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000072912; -.
InParanoid; O22229; -.
KO; K00384; -.
OMA; YQEDVEF; -.
OrthoDB; EOG09360E6S; -.
PhylomeDB; O22229; -.
PRO; PR:O22229; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O22229; baseline and differential.
Genevisible; O22229; AT.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:TAIR.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:UniProtKB.
GO; GO:0010581; P:regulation of starch biosynthetic process; IMP:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
InterPro; IPR005982; Thioredox_Rdtase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF00085; Thioredoxin; 1.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR01292; TRX_reduct; 1.
PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Disulfide bond; Electron transport;
FAD; Flavoprotein; NADP; Oxidoreductase; Plastid; Redox-active center;
Reference proteome; Transit peptide; Transport.
TRANSIT 1 67 Chloroplast. {ECO:0000255}.
CHAIN 68 529 NADPH-dependent thioredoxin reductase 3.
/FTId=PRO_0000394552.
DOMAIN 403 529 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
NP_BIND 91 94 FAD. {ECO:0000250}.
NP_BIND 112 113 FAD. {ECO:0000250}.
NP_BIND 120 124 FAD. {ECO:0000250}.
NP_BIND 371 373 FAD. {ECO:0000250}.
COMPBIAS 72 78 Poly-Ser.
ACT_SITE 454 454 Nucleophile. {ECO:0000250}.
ACT_SITE 457 457 Nucleophile. {ECO:0000250}.
BINDING 133 133 FAD. {ECO:0000250}.
BINDING 166 166 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 220 220 FAD. {ECO:0000250}.
BINDING 364 364 FAD. {ECO:0000250}.
SITE 241 241 Important for activity. {ECO:0000250}.
SITE 259 259 Important for activity. {ECO:0000250}.
SITE 260 260 Important for activity. {ECO:0000250}.
DISULFID 217 220 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 454 457 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
CONFLICT 399 399 E -> K (in Ref. 3; AAN18085/AAL08250).
{ECO:0000305}.
SEQUENCE 529 AA; 57950 MW; 53853134652D64AA CRC64;
MAASPKIGIG IASVSSPHRV SAASSALSPP PHLFFLTTTT TTRHGGSYLL RQPTRTRSSD
SLRLRVSATA NSPSSSSSGG EIIENVVIIG SGPAGYTAAI YAARANLKPV VFEGYQMGGV
PGGQLMTTTE VENFPGFPDG ITGPDLMEKM RKQAERWGAE LYPEDVESLS VTTAPFTVQT
SERKVKCHSI IYATGATARR LRLPREEEFW SRGISACAIC DGASPLFKGQ VLAVVGGGDT
ATEEALYLTK YARHVHLLVR RDQLRASKAM QDRVINNPNI TVHYNTETVD VLSNTKGQMS
GILLRRLDTG EETELEAKGL FYGIGHSPNS QLLEGQVELD SSGYVLVREG TSNTSVEGVF
AAGDVQDHEW RQAVTAAGSG CIAALSAERY LTSNNLLVEF HQPQTEEAKK EFTQRDVQEK
FDITLTKHKG QYALRKLYHE SPRVILVLYT SPTCGPCRTL KPILNKVVDE YNHDVHFVEI
DIEEDQEIAE AAGIMGTPCV QFFKNKEMLR TISGVKMKKE YREFIEANK


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