TRXB3_ARATH
ID TRXB3_ARATH Reviewed; 529 AA.
AC O22229; Q0WM62; Q93ZQ1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=NADPH-dependent thioredoxin reductase 3;
DE Short=NTR3;
DE EC=1.8.1.9 {ECO:0000269|PubMed:16884685};
DE AltName: Full=NADPH-dependent thioredoxin reductase C {ECO:0000303|PubMed:16884685, ECO:0000303|PubMed:18625226, ECO:0000303|PubMed:19470473};
DE Short=ANTR-C {ECO:0000303|PubMed:16884685};
DE Short=AtNTRC {ECO:0000303|PubMed:18625226, ECO:0000303|PubMed:19470473};
DE Flags: Precursor;
GN Name=NTRC {ECO:0000303|PubMed:16884685, ECO:0000303|PubMed:18625226,
GN ECO:0000303|PubMed:19470473};
GN OrderedLocusNames=At2g41680 {ECO:0000312|Araport:AT2G41680};
GN ORFNames=T32G6.20 {ECO:0000312|EMBL:AAB84351.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-529.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP BAS1.
RX PubMed=16884685; DOI=10.1016/j.bbrc.2006.07.088;
RA Moon J.C., Jang H.H., Chae H.B., Lee J.R., Lee S.Y., Jung Y.J., Shin M.R.,
RA Lim H.S., Chung W.S., Yun D.-J., Lee K.O., Lee S.Y.;
RT "The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an electron
RT donor to 2-Cys peroxiredoxins in chloroplasts.";
RL Biochem. Biophys. Res. Commun. 348:478-484(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18625226; DOI=10.1016/j.febslet.2008.07.006;
RA Stenbaek A., Hansson A., Wulff R.P., Hansson M., Dietz K.J., Jensen P.E.;
RT "NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed
RT for the protection of Mg-protoporphyrin monomethyl ester cyclase.";
RL FEBS Lett. 582:2773-2778(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19470473; DOI=10.1073/pnas.0903559106;
RA Michalska J., Zauber H., Buchanan B.B., Cejudo F.J., Geigenberger P.;
RT "NTRC links built-in thioredoxin to light and sucrose in regulating starch
RT synthesis in chloroplasts and amyloplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9908-9913(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 plastidial 2-Cys
CC peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide
CC scavenging system in chloroplasts in the dark. Required for chlorophyll
CC biosynthesis and biogenesis of the photosynthetic apparatus. Activates
CC aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into
CC protochlorophyllide. Involved in a light-dependent regulation of starch
CC biosynthesis by redox activation of the ADP-glucose pyrophosphorylase
CC (AGPase), a central enzyme of starch synthesis.
CC {ECO:0000269|PubMed:16884685, ECO:0000269|PubMed:18625226,
CC ECO:0000269|PubMed:19470473}.
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:16884685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1};
CC -!- SUBUNIT: May homodimerize. Interacts with the 2-Cys peroxiredoxin BAS1.
CC {ECO:0000269|PubMed:16884685}.
CC -!- INTERACTION:
CC O22229; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-4427818, EBI-15193683;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16884685}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with chlorotic leaves. Accumulation
CC of Mg-protoporhyrin after feeding with 5-aminolevulinic acid.
CC {ECO:0000269|PubMed:18625226, ECO:0000269|PubMed:19470473}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AC002510; AAB84351.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10015.1; -; Genomic_DNA.
DR EMBL; AY056394; AAL08250.1; -; mRNA.
DR EMBL; BT000516; AAN18085.1; -; mRNA.
DR EMBL; AK229969; BAF01794.1; -; mRNA.
DR PIR; T00824; T00824.
DR RefSeq; NP_565954.1; NM_129731.6.
DR AlphaFoldDB; O22229; -.
DR SMR; O22229; -.
DR BioGRID; 4103; 15.
DR IntAct; O22229; 11.
DR MINT; O22229; -.
DR STRING; 3702.AT2G41680.1; -.
DR MetOSite; O22229; -.
DR PaxDb; O22229; -.
DR PRIDE; O22229; -.
DR ProteomicsDB; 228701; -.
DR EnsemblPlants; AT2G41680.1; AT2G41680.1; AT2G41680.
DR GeneID; 818766; -.
DR Gramene; AT2G41680.1; AT2G41680.1; AT2G41680.
DR KEGG; ath:AT2G41680; -.
DR Araport; AT2G41680; -.
DR TAIR; locus:2062683; AT2G41680.
DR eggNOG; KOG0404; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_031864_5_4_1; -.
DR InParanoid; O22229; -.
DR OMA; KMKSEYR; -.
DR OrthoDB; 1108990at2759; -.
DR PhylomeDB; O22229; -.
DR BRENDA; 1.8.1.9; 399.
DR PRO; PR:O22229; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22229; baseline and differential.
DR Genevisible; O22229; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:TAIR.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010581; P:regulation of starch biosynthetic process; IMP:UniProtKB.
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; IPR017937; Thioredoxin_CS.
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; PS00194; THIOREDOXIN_1; 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..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..529
FT /note="NADPH-dependent thioredoxin reductase 3"
FT /id="PRO_0000394552"
FT DOMAIN 403..529
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 54..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P09856"
FT ACT_SITE 457
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P09856"
FT BINDING 91..94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 113..120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 265
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 324
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 344
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 364
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 371..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 371
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT SITE 241
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT SITE 259
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT DISULFID 217..220
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 454..457
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 399
FT /note="E -> K (in Ref. 3; AAN18085/AAL08250)"
FT /evidence="ECO:0000305"
SQ 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
