FTRC_ORYSJ
ID FTRC_ORYSJ Reviewed; 146 AA.
AC Q6K471; A0A0P0XJ79; Q0J376;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic;
DE Short=FTR-C;
DE EC=1.8.7.2;
DE AltName: Full=Ferredoxin-thioredoxin reductase subunit B;
DE Short=FTR-B;
DE Flags: Precursor;
GN OrderedLocusNames=Os09g0249900, LOC_Os09g07570;
GN ORFNames=OJ1116_H10.13, OJ1695_A02.34, OsJ_28527;
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Catalytic subunit of the ferredoxin-thioredoxin reductase
CC (FTR), which catalyzes the two-electron reduction of thioredoxins by
CC the electrons provided by reduced ferredoxin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:42336, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:50058; EC=1.8.7.2;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of subunit A (variable subunit) and subunit B
CC (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin
CC and thioredoxin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta
CC subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF24589.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005553; BAD22216.1; -; Genomic_DNA.
DR EMBL; AP005578; BAD19914.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24589.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014965; BAT07039.1; -; Genomic_DNA.
DR EMBL; CM000146; EEE69266.1; -; Genomic_DNA.
DR EMBL; AK099860; BAG94324.1; -; mRNA.
DR RefSeq; XP_015651145.1; XM_015795659.1.
DR AlphaFoldDB; Q6K471; -.
DR SMR; Q6K471; -.
DR STRING; 4530.OS09T0249900-01; -.
DR PaxDb; Q6K471; -.
DR PRIDE; Q6K471; -.
DR EnsemblPlants; Os09t0249900-01; Os09t0249900-01; Os09g0249900.
DR GeneID; 4346508; -.
DR Gramene; Os09t0249900-01; Os09t0249900-01; Os09g0249900.
DR KEGG; osa:4346508; -.
DR eggNOG; ENOG502RZRI; Eukaryota.
DR HOGENOM; CLU_108772_1_0_1; -.
DR InParanoid; Q6K471; -.
DR OMA; QAFWNCP; -.
DR OrthoDB; 1530745at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q6K471; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0103012; F:ferredoxin-thioredoxin reductase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR Gene3D; 3.90.460.10; -; 1.
DR InterPro; IPR004209; FTR_bsu.
DR InterPro; IPR036644; FTR_bsu_sf.
DR PANTHER; PTHR35113; PTHR35113; 1.
DR Pfam; PF02943; FeThRed_B; 1.
DR SUPFAM; SSF57662; SSF57662; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Chloroplast; Disulfide bond; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Plastid; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..146
FT /note="Ferredoxin-thioredoxin reductase catalytic chain,
FT chloroplastic"
FT /id="PRO_0000394860"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 116
FT /note="Increases the nucleophilicity of the active site
FT Cys"
FT /evidence="ECO:0000250"
FT DISULFID 87..117
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 16101 MW; F4D88399C9857D90 CRC64;
MMSMASTTAS PFCPSPMPRG RKCTVRVQAG AAGADASDKS LEIMRKFSEQ YARRSNTFFC
SEKSVTAVVI KGLADHKDQL GAPLCPCRHY DDKAAEVAQG FWNCPCVPMR ERKECHCMLF
LTPDNDFAGQ DQAITLEEIK DATSKI
