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Thioredoxin reductase NTRC (EC 1.8.1.9) (NADPH-dependent thioredoxin reductase C) (OsNTRC)

 NTRC_ORYSJ              Reviewed;         515 AA.
Q70G58; B9FUN1;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
15-JUN-2010, sequence version 2.
25-OCT-2017, entry version 104.
RecName: Full=Thioredoxin reductase NTRC;
EC=1.8.1.9;
AltName: Full=NADPH-dependent thioredoxin reductase C;
Short=OsNTRC;
Flags: Precursor;
OrderedLocusNames=Os07g0657900, LOC_Os07g46410; ORFNames=OsJ_25429;
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=cv. Nipponbare; TISSUE=Leaf;
PubMed=15292215; DOI=10.1074/jbc.M404696200;
Serrato A.J., Perez-Ruiz J.M., Spinola M.C., Cejudo F.J.;
"A novel NADPH thioredoxin reductase, localized in the chloroplast,
which deficiency causes hypersensitivity to abiotic stress in
Arabidopsis thaliana.";
J. Biol. Chem. 279:43821-43827(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[4]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[6]
FUNCTION, AND MUTAGENESIS OF CYS-203; CYS-206; CYS-440 AND CYS-443.
PubMed=16891402; DOI=10.1105/tpc.106.041541;
Perez-Ruiz J.M., Spinola M.C., Kirchsteiger K., Moreno J., Sahrawy M.,
Cejudo F.J.;
"Rice NTRC is a high-efficiency redox system for chloroplast
protection against oxidative damage.";
Plant Cell 18:2356-2368(2006).
[7]
FUNCTION, SUBUNIT, AND INTERACTION WITH BAS1.
PubMed=19345687; DOI=10.1016/j.febslet.2009.03.067;
Perez-Ruiz J.M., Cejudo F.J.;
"A proposed reaction mechanism for rice NADPH thioredoxin reductase C,
an enzyme with protein disulfide reductase activity.";
FEBS Lett. 583:1399-1402(2009).
[8]
FUNCTION, AND MUTAGENESIS OF ALA-227; VAL-245 AND ARG-246.
PubMed=19825629; DOI=10.1093/mp/ssp011;
Perez-Ruiz J.M., Gonzalez M., Spinola M.C., Sandalio L.M.,
Cejudo F.J.;
"The quaternary structure of NADPH thioredoxin reductase C is redox-
sensitive.";
Mol. Plant 2:457-467(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 the plastidial 2-Cys
peroxiredoxin BAS1 and participates in a NADPH-dependent hydrogen
peroxide scavenging system in chloroplasts in the dark.
{ECO:0000269|PubMed:15292215, ECO:0000269|PubMed:16891402,
ECO:0000269|PubMed:19345687, ECO:0000269|PubMed:19825629}.
-!- 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: Homodimerizes under reducing conditions. Interacts (via
thioredoxin domain) with the plastidial 2-Cys peroxiredoxin BAS1.
{ECO:0000269|PubMed:19345687}.
-!- INTERACTION:
Q6ER94:BAS1; NbExp=5; IntAct=EBI-6956411, EBI-6956385;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:15292215}.
-!- TISSUE SPECIFICITY: Expressed in roots and shoots.
{ECO:0000269|PubMed:15292215}.
-!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAF22429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAE46765.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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EMBL; AJ582621; CAE46765.1; ALT_SEQ; mRNA.
EMBL; AP008213; BAF22429.1; ALT_SEQ; Genomic_DNA.
EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CM000144; EEE67738.1; -; Genomic_DNA.
RefSeq; XP_015646853.1; XM_015791367.1.
UniGene; Os.7284; -.
ProteinModelPortal; Q70G58; -.
SMR; Q70G58; -.
DIP; DIP-57118N; -.
IntAct; Q70G58; 3.
MINT; MINT-7017090; -.
STRING; 39947.LOC_Os07g46410.1; -.
PaxDb; Q70G58; -.
PRIDE; Q70G58; -.
GeneID; 4344159; -.
KEGG; osa:4344159; -.
eggNOG; KOG0404; Eukaryota.
eggNOG; KOG0907; Eukaryota.
eggNOG; COG0492; LUCA.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000072912; -.
InParanoid; Q70G58; -.
KO; K00384; -.
OrthoDB; EOG09360E6S; -.
BRENDA; 1.8.1.9; 4460.
Proteomes; UP000059680; Chromosome 7.
Genevisible; Q70G58; OS.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI: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; IEA:InterPro.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
Gene3D; 3.50.50.60; -; 1.
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; 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; 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 45 Chloroplast. {ECO:0000255}.
CHAIN 46 515 Thioredoxin reductase NTRC.
/FTId=PRO_0000394859.
DOMAIN 377 515 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
NP_BIND 77 80 FAD. {ECO:0000250}.
NP_BIND 98 99 FAD. {ECO:0000250}.
NP_BIND 106 110 FAD. {ECO:0000250}.
NP_BIND 357 359 FAD. {ECO:0000250}.
ACT_SITE 440 440 Nucleophile. {ECO:0000250}.
ACT_SITE 443 443 Nucleophile. {ECO:0000250}.
BINDING 119 119 FAD. {ECO:0000250}.
BINDING 152 152 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 206 206 FAD. {ECO:0000250}.
BINDING 350 350 FAD. {ECO:0000250}.
SITE 227 227 Important for activity. {ECO:0000250}.
SITE 245 245 Important for activity. {ECO:0000250}.
SITE 246 246 Important for activity. {ECO:0000250}.
DISULFID 203 206 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 440 443 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MUTAGEN 203 203 C->S: Loss of thioredoxin reductase
activity. {ECO:0000269|PubMed:16891402}.
MUTAGEN 206 206 C->S: Loss of thioredoxin reductase
activity. {ECO:0000269|PubMed:16891402}.
MUTAGEN 227 227 A->G: Reduces activity 30-fold; when
associated with E-245 and F-246.
{ECO:0000269|PubMed:19825629}.
MUTAGEN 245 245 V->E: Reduces activity 30-fold; when
associated with G-227 and F-246.
{ECO:0000269|PubMed:19825629}.
MUTAGEN 246 246 R->F: Reduces activity 30-fold; when
associated with G-227 and E-245.
{ECO:0000269|PubMed:19825629}.
MUTAGEN 440 440 C->S: Loss of thioredoxin activity.
{ECO:0000269|PubMed:16891402}.
MUTAGEN 443 443 C->S: Loss of thioredoxin activity.
{ECO:0000269|PubMed:16891402}.
SEQUENCE 515 AA; 56151 MW; C10BF4681B135DA3 CRC64;
MAVTRLAVAA ALSAAPPSSR RRRAFFHHSC RPLPSSAAAA AKALRASAAP AVDEEAPASP
PPSDLGKGVE NLVIIGSGPA GYTAAIYAAR ANLKPVVFEG YQVGGVPGGQ LMTTTEVENF
PGFPDGVTGP DLMDKMRKQA ERWGAELHQE DVEFVNVKSR PFVIRSSDRE VKCHSVIIAT
GAAAKRLRLP REDEFWSRGI SACAICDGAS PLFKGQVLAV VGGGDTATEE AIYLTKYARH
VHLLVRKDQL RASKAMQDRV LNNPNITVHF NTEAVDVVSN PKGQMSGIQL KRTDTGEESV
LEVKGLFYGI GHTPNSQLLQ GQIDLDDAGY ILVEEGTAKT SVDGVFAAGD VQDHEWRQAV
TAAGSGCVAA LSVERYLVAN DLLVEFHQPV REEKEKEITD RDVEMGFDIS HTKHRGQYAL
RKVYHESPRL VCVLYTSPTC GPCRTLKPIL SKVIDEYNEH VHFVEIDIEE DPEIAEAAGI
MGTPCVQFFK NKEMLRTVSG VKMKKEYREF IESNK


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