FTRC_SOYBN
ID FTRC_SOYBN Reviewed; 144 AA.
AC O49856;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, 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;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Williams 83;
RA Raeber L., Gaymard E., Schurmann P.;
RT "Cloning and sequencing of a full-length cDNA coding for the precursor of
RT the catalytic subunit of ferredoxin:thioredoxin reductase from soybean.";
RL (er) Plant Gene Register PGR98-010(1998).
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.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta
CC subunit family. {ECO:0000305}.
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DR EMBL; Y15076; CAA75356.1; -; mRNA.
DR PIR; T07147; T07147.
DR RefSeq; NP_001236326.1; NM_001249397.1.
DR AlphaFoldDB; O49856; -.
DR SMR; O49856; -.
DR STRING; 3847.GLYMA13G04640.2; -.
DR PRIDE; O49856; -.
DR ProMEX; O49856; -.
DR EnsemblPlants; KRH18580; KRH18580; GLYMA_13G069100.
DR GeneID; 547937; -.
DR Gramene; KRH18580; KRH18580; GLYMA_13G069100.
DR KEGG; gmx:547937; -.
DR eggNOG; ENOG502RZRI; Eukaryota.
DR HOGENOM; CLU_108772_1_1_1; -.
DR InParanoid; O49856; -.
DR OMA; QAFWNCP; -.
DR OrthoDB; 1530745at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
DR Genevisible; O49856; GM.
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..31
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 32..144
FT /note="Ferredoxin-thioredoxin reductase catalytic chain,
FT chloroplastic"
FT /id="PRO_0000019427"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 102
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 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 114
FT /note="Increases the nucleophilicity of the active site
FT Cys"
FT /evidence="ECO:0000250"
FT DISULFID 85..115
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 144 AA; 16107 MW; 879733E8452DB0E1 CRC64;
MTTQASTFAV AVPSVATPFR RHRNPFVVRA QAEPSDKSVE IMRKFSEQYA RKSGTYFCVD
KGVTSVVIKG LADHKDTLGA PLCPCRHYDD KAAEVAQGFW NCPCVPMRER KECHCMLFLT
PDNDFAGNEQ TITLDEIKES TANM
