NTRC_ORYSJ
ID NTRC_ORYSJ Reviewed; 515 AA.
AC Q70G58; B9FUN1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Thioredoxin reductase NTRC {ECO:0000305};
DE EC=1.8.1.9 {ECO:0000269|PubMed:15292215};
DE AltName: Full=NADPH-dependent thioredoxin reductase C {ECO:0000303|PubMed:15292215};
DE Short=OsNTRC {ECO:0000303|PubMed:15292215};
DE Flags: Precursor;
GN OrderedLocusNames=Os07g0657900 {ECO:0000312|EMBL:AP014963},
GN LOC_Os07g46410 {ECO:0000305};
GN ORFNames=OsJ_25429 {ECO:0000312|EMBL:AP014963};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=15292215; DOI=10.1074/jbc.m404696200;
RA Serrato A.J., Perez-Ruiz J.M., Spinola M.C., Cejudo F.J.;
RT "A novel NADPH thioredoxin reductase, localized in the chloroplast, which
RT deficiency causes hypersensitivity to abiotic stress in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 279:43821-43827(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-203; CYS-206; CYS-440 AND CYS-443.
RX PubMed=16891402; DOI=10.1105/tpc.106.041541;
RA Perez-Ruiz J.M., Spinola M.C., Kirchsteiger K., Moreno J., Sahrawy M.,
RA Cejudo F.J.;
RT "Rice NTRC is a high-efficiency redox system for chloroplast protection
RT against oxidative damage.";
RL Plant Cell 18:2356-2368(2006).
RN [7]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH BAS1.
RX PubMed=19345687; DOI=10.1016/j.febslet.2009.03.067;
RA Perez-Ruiz J.M., Cejudo F.J.;
RT "A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an
RT enzyme with protein disulfide reductase activity.";
RL FEBS Lett. 583:1399-1402(2009).
RN [8]
RP FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF ALA-227; VAL-245 AND ARG-246.
RX PubMed=19825629; DOI=10.1093/mp/ssp011;
RA Perez-Ruiz J.M., Gonzalez M., Spinola M.C., Sandalio L.M., Cejudo F.J.;
RT "The quaternary structure of NADPH thioredoxin reductase C is redox-
RT sensitive.";
RL Mol. Plant 2:457-467(2009).
CC -!- FUNCTION: Thioredoxin reductase (TR) that exhibits both TR and
CC thioredoxin (Trx) activities. Contains a C-terminal functional Trx
CC domain. Functions as an electron donor for the plastidial 2-Cys
CC peroxiredoxin BAS1 and participates in a NADPH-dependent hydrogen
CC peroxide scavenging system in chloroplasts in the dark.
CC {ECO:0000269|PubMed:15292215, ECO:0000269|PubMed:16891402,
CC ECO:0000269|PubMed:19345687, ECO:0000269|PubMed:19825629}.
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:0000269|PubMed:15292215};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000269|PubMed:15292215};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q39243};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q39243};
CC -!- SUBUNIT: Homodimerizes under reducing conditions. Interacts (via
CC thioredoxin domain) with the plastidial 2-Cys peroxiredoxin BAS1.
CC {ECO:0000269|PubMed:19345687}.
CC -!- INTERACTION:
CC Q70G58; Q6ER94: BAS1; NbExp=5; IntAct=EBI-6956411, EBI-6956385;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15292215}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:15292215}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF22429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAE46765.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AJ582621; CAE46765.1; ALT_SEQ; mRNA.
DR EMBL; AP008213; BAF22429.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000144; EEE67738.1; -; Genomic_DNA.
DR RefSeq; XP_015646853.1; XM_015791367.1.
DR AlphaFoldDB; Q70G58; -.
DR SMR; Q70G58; -.
DR DIP; DIP-57118N; -.
DR IntAct; Q70G58; 3.
DR MINT; Q70G58; -.
DR STRING; 4530.OS07T0657900-01; -.
DR PaxDb; Q70G58; -.
DR PRIDE; Q70G58; -.
DR EnsemblPlants; Os07t0657900-02; Os07t0657900-02; Os07g0657900.
DR GeneID; 4344159; -.
DR Gramene; Os07t0657900-02; Os07t0657900-02; Os07g0657900.
DR KEGG; osa:4344159; -.
DR eggNOG; KOG0404; Eukaryota.
DR HOGENOM; CLU_031864_5_6_1; -.
DR InParanoid; Q70G58; -.
DR OrthoDB; 1108990at2759; -.
DR BRENDA; 1.8.1.9; 4460.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q70G58; baseline and differential.
DR Genevisible; Q70G58; OS.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IEA:EnsemblPlants.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:EnsemblPlants.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010581; P:regulation of starch biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Electron transport; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Plastid; Redox-active center; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..515
FT /note="Thioredoxin reductase NTRC"
FT /id="PRO_0000394859"
FT DOMAIN 377..515
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 440
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 443
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 77..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 98..99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 106..110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 206
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT BINDING 357..359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT SITE 227
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19825629"
FT SITE 245
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19825629"
FT SITE 246
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19825629"
FT DISULFID 203..206
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q39243"
FT DISULFID 440..443
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 203
FT /note="C->S: Loss of thioredoxin reductase activity."
FT /evidence="ECO:0000269|PubMed:16891402"
FT MUTAGEN 206
FT /note="C->S: Loss of thioredoxin reductase activity."
FT /evidence="ECO:0000269|PubMed:16891402"
FT MUTAGEN 227
FT /note="A->G: Reduces activity 30-fold; when associated with
FT E-245 and F-246."
FT /evidence="ECO:0000269|PubMed:19825629"
FT MUTAGEN 245
FT /note="V->E: Reduces activity 30-fold; when associated with
FT G-227 and F-246."
FT /evidence="ECO:0000269|PubMed:19825629"
FT MUTAGEN 246
FT /note="R->F: Reduces activity 30-fold; when associated with
FT G-227 and E-245."
FT /evidence="ECO:0000269|PubMed:19825629"
FT MUTAGEN 440
FT /note="C->S: Loss of thioredoxin activity."
FT /evidence="ECO:0000269|PubMed:16891402"
FT MUTAGEN 443
FT /note="C->S: Loss of thioredoxin activity."
FT /evidence="ECO:0000269|PubMed:16891402"
SQ 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
