FTRC1_SPIOL
ID FTRC1_SPIOL Reviewed; 144 AA.
AC P41348;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic;
DE Short=FTR-C;
DE EC=1.8.7.2;
DE AltName: Full=B2;
DE AltName: Full=Ferredoxin-thioredoxin reductase subunit B;
DE Short=FTR-B;
DE Flags: Precursor;
GN Name=FTRC;
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].
RX PubMed=7916641; DOI=10.1016/0005-2728(93)90020-g;
RA Marc-Martin S., Spielmann A., Stutz E., Schuermann P.;
RT "Cloning and sequencing of a corn (Zea mays) nuclear gene coding for the
RT chloroplast specific catalytic subunit of ferredoxin-thioredoxin
RT reductase.";
RL Biochim. Biophys. Acta 1183:207-209(1993).
RN [2]
RP SEQUENCE REVISION TO 26.
RA Schuermann P.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 32-144, AND CATALYTIC ACTIVITY.
RA Iwadate H., Yano K., Aso K., Kamo M., Gardet-Salvi L., Schuermann P.,
RA Tsugita A.;
RL (In) Murata N. (eds.);
RL Research in photosynthesis, pp.2:539-542, Kluwer Academic Publishers,
RL Dordrecht (1992).
RN [4]
RP PROTEIN SEQUENCE OF 32-144.
RC TISSUE=Leaf;
RX PubMed=7628465; DOI=10.1111/j.1432-1033.1995.tb20681.x;
RA Chow L.-P., Iwadate H., Yano K., Kamo M., Tsugita A., Gardet-Salvi L.,
RA Stritt-Etter A.-L., Schuermann P.;
RT "Amino acid sequence of spinach ferredoxin:thioredoxin reductase catalytic
RT subunit and identification of thiol groups constituting a redox-active
RT disulfide and a [4Fe-4S] cluster.";
RL Eur. J. Biochem. 231:149-156(1995).
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 Evidence={ECO:0000269|Ref.3};
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; X74881; CAA52867.1; -; mRNA.
DR PIR; S65943; RDSPTB.
DR AlphaFoldDB; P41348; -.
DR SMR; P41348; -.
DR KEGG; ag:CAA52867; -.
DR OrthoDB; 1530745at2759; -.
DR BRENDA; 1.8.7.2; 5812.
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 1: Evidence at protein level;
KW 4Fe-4S; Chloroplast; Direct protein sequencing; Disulfide bond; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Plastid; Redox-active center;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:7628465, ECO:0000269|Ref.3"
FT CHAIN 32..144
FT /note="Ferredoxin-thioredoxin reductase catalytic chain,
FT chloroplastic"
FT /id="PRO_0000019428"
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 BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
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"
SQ SEQUENCE 144 AA; 16349 MW; C30B7343714F77DD CRC64;
MKALQASIAY SFPISSPAAS PRRFSRVIRA QADPSDKSME VMRKFSEQFC RKSDTYFCVD
KSVTAVVIKG LADHRDTLGA PLCPCRHYDD KEAEAKQGFW NCPCVPMRER KECHCMLFLT
PDNDFAGKEQ TITLDEIREV TSNM
