ID   FTRC_NEOYE              Reviewed;         116 AA.
AC   Q1XDA1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Ferredoxin-thioredoxin reductase, catalytic chain;
DE            Short=FTR-C;
DE            EC=1.8.7.2;
DE   AltName: Full=Ferredoxin-thioredoxin reductase subunit B;
DE            Short=FTR-B;
GN   Name=ftrB;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) 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.
CC   -!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta
CC       subunit family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE92510.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP006715; BAE92510.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_537067.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDA1; -.
DR   SMR; Q1XDA1; -.
DR   GeneID; 3978885; -.
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: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; IPR024707; FTR_bsu_Cyanobacter.
DR   InterPro; IPR036644; FTR_bsu_sf.
DR   PANTHER; PTHR35113; PTHR35113; 1.
DR   Pfam; PF02943; FeThRed_B; 1.
DR   PIRSF; PIRSF000260; FTRc; 1.
DR   SUPFAM; SSF57662; SSF57662; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Chloroplast; Disulfide bond; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Plastid; Redox-active center.
FT   CHAIN           1..116
FT                   /note="Ferredoxin-thioredoxin reductase, catalytic chain"
FT                   /id="PRO_0000277250"
FT   ACT_SITE        59
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   SITE            88
FT                   /note="Increases the nucleophilicity of the active site
FT                   Cys"
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..89
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   116 AA;  13405 MW;  A2AB1C86AEFFA18B CRC64;
     MKKQNLVSFP ENLEAMRKFS ETYAKRTGTF FCIDSSVTAV VIEGLARHKD QYGAPLCPCR
     HYEDKKAEIS ATYWNCPCVP MRERRECHCM LFLTPDNEFA SDLQEIDKTT LTEQIS