FTRC_ARATH
ID FTRC_ARATH Reviewed; 146 AA.
AC Q9SJ89;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 Name=FTRC; OrderedLocusNames=At2g04700; ORFNames=F28I8.26;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006955; AAD22336.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05858.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61570.1; -; Genomic_DNA.
DR EMBL; AY063795; AAL36151.1; -; mRNA.
DR EMBL; AY117167; AAM51242.1; -; mRNA.
DR EMBL; AY088058; AAM65604.1; -; mRNA.
DR PIR; D84460; D84460.
DR RefSeq; NP_001323778.1; NM_001335245.1.
DR RefSeq; NP_178547.1; NM_126500.5.
DR PDB; 7BZK; X-ray; 1.59 A; A=32-146.
DR PDB; 7C2B; X-ray; 1.79 A; A=32-146.
DR PDB; 7C3F; X-ray; 2.40 A; A/D/G/J/M/P/S/V=32-146.
DR PDBsum; 7BZK; -.
DR PDBsum; 7C2B; -.
DR PDBsum; 7C3F; -.
DR AlphaFoldDB; Q9SJ89; -.
DR SMR; Q9SJ89; -.
DR BioGRID; 414; 1.
DR STRING; 3702.AT2G04700.1; -.
DR MetOSite; Q9SJ89; -.
DR PaxDb; Q9SJ89; -.
DR PRIDE; Q9SJ89; -.
DR ProteomicsDB; 230532; -.
DR EnsemblPlants; AT2G04700.1; AT2G04700.1; AT2G04700.
DR EnsemblPlants; AT2G04700.3; AT2G04700.3; AT2G04700.
DR GeneID; 815013; -.
DR Gramene; AT2G04700.1; AT2G04700.1; AT2G04700.
DR Gramene; AT2G04700.3; AT2G04700.3; AT2G04700.
DR KEGG; ath:AT2G04700; -.
DR Araport; AT2G04700; -.
DR TAIR; locus:2049228; AT2G04700.
DR eggNOG; ENOG502RZRI; Eukaryota.
DR HOGENOM; CLU_108772_1_1_1; -.
DR InParanoid; Q9SJ89; -.
DR OMA; QAFWNCP; -.
DR OrthoDB; 1530745at2759; -.
DR PhylomeDB; Q9SJ89; -.
DR BioCyc; ARA:AT2G04700-MON; -.
DR PRO; PR:Q9SJ89; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ89; baseline and differential.
DR Genevisible; Q9SJ89; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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; IDA:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chloroplast; Disulfide bond; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Plastid; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..146
FT /note="Ferredoxin-thioredoxin reductase catalytic chain,
FT chloroplastic"
FT /id="PRO_0000394553"
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"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 63..80
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:7BZK"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7C3F"
SQ SEQUENCE 146 AA; 16434 MW; 06372CBF48014884 CRC64;
MNLQAVSCSF GFLSSPLGVT PRTSFRRFVI RAKTEPSEKS VEIMRKFSEQ YARRSGTYFC
VDKGVTSVVI KGLAEHKDSY GAPLCPCRHY DDKAAEVGQG FWNCPCVPMR ERKECHCMLF
LTPDNDFAGK DQTITSDEIK ETTANM
