ID   FTRC2_SPIOL             Reviewed;         148 AA.
AC   P41349;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic;
DE            Short=FTR-C;
DE            EC=1.8.7.2;
DE   AltName: Full=B1;
DE   AltName: Full=Ferredoxin-thioredoxin reductase subunit B;
DE            Short=FTR-B;
DE   Flags: Precursor;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Green leaf;
RX   PubMed=8167141; DOI=10.1016/0005-2728(94)90218-6;
RA   Falkenstein E., von Schaewen A., Scheibe R.;
RT   "Full-length cDNA sequences for both ferredoxin-thioredoxin reductase
RT   subunits from spinach (Spinacia oleracea L.).";
RL   Biochim. Biophys. Acta 1185:252-254(1994).
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.
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;
CC       Note=Binds 1 [4Fe-4S] cluster.;
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; X77164; CAA54409.1; -; mRNA.
DR   PIR; T09150; T09150.
DR   AlphaFoldDB; P41349; -.
DR   SMR; P41349; -.
DR   PRIDE; P41349; -.
DR   OrthoDB; 1530745at2759; -.
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; Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..148
FT                   /note="Ferredoxin-thioredoxin reductase catalytic chain,
FT                   chloroplastic"
FT                   /id="PRO_0000019429"
FT   ACT_SITE        89
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   BINDING         106
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   BINDING         117
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   SITE            118
FT                   /note="Increases the nucleophilicity of the active site
FT                   Cys"
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..119
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  16676 MW;  7AAEEB67608D6D66 CRC64;
     MKALQASTSY SFFSKSSSAT LQRRTHRPQC VILSKVEPSD KSVEIMRKFS EQYARKSGTY
     FCVDKGVTSV VIKGLAEHKD SLGAPLCPCR YYDDKAAEAT QGFWNCPCVP MRERKECHCM
     LFLTPENDFA GKDQTIGLDE IREVTANM