FTRC_MAIZE
ID FTRC_MAIZE Reviewed; 152 AA.
AC P41347;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
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).
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; X73549; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S43714; S43714.
DR RefSeq; NP_001292798.1; NM_001305869.1.
DR AlphaFoldDB; P41347; -.
DR SMR; P41347; -.
DR STRING; 4577.GRMZM2G122793_P01; -.
DR PaxDb; P41347; -.
DR PRIDE; P41347; -.
DR EnsemblPlants; Zm00001eb373700_T001; Zm00001eb373700_P001; Zm00001eb373700.
DR GeneID; 542532; -.
DR Gramene; Zm00001eb373700_T001; Zm00001eb373700_P001; Zm00001eb373700.
DR KEGG; zma:542532; -.
DR MaizeGDB; 61547; -.
DR eggNOG; ENOG502RZRI; Eukaryota.
DR HOGENOM; CLU_108772_1_0_1; -.
DR OMA; QAFWNCP; -.
DR OrthoDB; 1530745at2759; -.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; P41347; baseline and differential.
DR Genevisible; P41347; ZM.
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; Reference proteome; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 39..152
FT /note="Ferredoxin-thioredoxin reductase catalytic chain,
FT chloroplastic"
FT /id="PRO_0000019426"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 122
FT /note="Increases the nucleophilicity of the active site
FT Cys"
FT /evidence="ECO:0000250"
FT DISULFID 93..123
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 16740 MW; 09618B305C682DFD CRC64;
MTSTVTTTVG CGGLPVRPLS TATRGRPRRC AVRAQAAGAD ASNDKSVEVM RKFSEQYARR
SNTFFCADKT VTAVVIKGLA DHRDTLGAPL CPCRHYDDKA AEVAQGFWNC PCVPMRERKE
CHCMLFLTPD NDFAGKDQVI SFEEIKEATS KF
