ID   A0A7U1AQM8_9PHAE        Unreviewed;       115 AA.
AC   A0A7U1AQM8;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   27-NOV-2024, entry version 8.
DE   RecName: Full=Ferredoxin-thioredoxin reductase, catalytic chain {ECO:0000256|ARBA:ARBA00021195, ECO:0000256|PIRNR:PIRNR000260};
DE            Short=FTR-C {ECO:0000256|PIRNR:PIRNR000260};
DE            EC=1.8.7.2 {ECO:0000256|ARBA:ARBA00012358, ECO:0000256|PIRNR:PIRNR000260};
DE   AltName: Full=Ferredoxin-thioredoxin reductase subunit B {ECO:0000256|ARBA:ARBA00030295, ECO:0000256|PIRNR:PIRNR000260};
GN   Name=ftrB {ECO:0000313|EMBL:QQY85078.1};
OS   Laminaria rodriguezii.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QQY85078.1}.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Laminariales; Laminariaceae; Laminaria.
OX   NCBI_TaxID=1740620 {ECO:0000313|EMBL:QQY85078.1};
RN   [1] {ECO:0000313|EMBL:QQY85078.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rana S., Valentin K., Bartsch I., Gloeckner G.;
RT   "Kelp chloroplast genomes.";
RL   Submitted (JUL-2020) 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.
CC       {ECO:0000256|ARBA:ARBA00003945, ECO:0000256|PIRNR:PIRNR000260}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + 2 reduced [2Fe-2S]-[ferredoxin] + 2
CC         H(+) = [thioredoxin]-dithiol + 2 oxidized [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:42336, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:50058; EC=1.8.7.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001385,
CC         ECO:0000256|PIRNR:PIRNR000260};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000260,
CC         ECO:0000256|PIRSR:PIRSR000260-2};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|PIRNR:PIRNR000260,
CC       ECO:0000256|PIRSR:PIRSR000260-2};
CC   -!- SUBUNIT: Heterodimer of subunit A (variable subunit) and subunit B
CC       (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin
CC       and thioredoxin. {ECO:0000256|ARBA:ARBA00026011,
CC       ECO:0000256|PIRNR:PIRNR000260}.
CC   -!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta
CC       subunit family. {ECO:0000256|ARBA:ARBA00007941,
CC       ECO:0000256|PIRNR:PIRNR000260}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MT732096; QQY85078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7U1AQM8; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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   FunFam; 3.90.460.10:FF:000001; Ferredoxin-thioredoxin reductase, catalytic chain; 1.
DR   Gene3D; 3.90.460.10; Ferredoxin thioredoxin reductase catalytic beta subunit; 1.
DR   InterPro; IPR004209; FTR_bsu.
DR   InterPro; IPR024707; FTR_bsu_Cyanobacter.
DR   InterPro; IPR036644; FTR_bsu_sf.
DR   PANTHER; PTHR35113; FERREDOXIN-THIOREDOXIN REDUCTASE CATALYTIC CHAIN, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR35113:SF1; FERREDOXIN-THIOREDOXIN REDUCTASE CATALYTIC CHAIN, CHLOROPLASTIC; 1.
DR   Pfam; PF02943; FeThRed_B; 1.
DR   PIRSF; PIRSF000260; FTRc; 1.
DR   SUPFAM; SSF57662; Ferredoxin thioredoxin reductase (FTR), catalytic beta chain; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR000260};
KW   Chloroplast {ECO:0000313|EMBL:QQY85078.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000260-4};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000260};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR000260};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000260};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000260}; Plastid {ECO:0000313|EMBL:QQY85078.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   ACT_SITE        59
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-1"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-2"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-2"
FT   BINDING         78
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-2"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-2"
FT   SITE            88
FT                   /note="Increases the nucleophilicity of the active site
FT                   Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-3"
FT   DISULFID        59..89
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000260-4"
SQ   SEQUENCE   115 AA;  13417 MW;  821344D72AD03C95 CRC64;
     MHSTKSENFY NRLKEMHNFA EIYAKQTNTF FCLDPSITSV IITGLATYKD QYGVPLCPCR
     NFRSEKAEIE LNYWICPCVS MRERKECHCK LFVQPNDSSA SETQKISLDT IYKNL
//