FTRC_PORPU
ID FTRC_PORPU Reviewed; 118 AA.
AC P51386;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX NCBI_TaxID=2787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Avonport;
RA Reith M.E., Munholland J.;
RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT genome.";
RL Plant Mol. Biol. Rep. 13:333-335(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. {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}.
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DR EMBL; U38804; AAC08272.1; -; Genomic_DNA.
DR PIR; S73307; S73307.
DR RefSeq; NP_053996.1; NC_000925.1.
DR AlphaFoldDB; P51386; -.
DR SMR; P51386; -.
DR GeneID; 810027; -.
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..118
FT /note="Ferredoxin-thioredoxin reductase, catalytic chain"
FT /id="PRO_0000167673"
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 118 AA; 13539 MW; E490AE73708630A8 CRC64;
MKKQNLVSFS DNLEAMRKFS ETYAKRTGTF FCADNSVTAV VIEGLARHKD KYGAPLCPCR
HYEDKKAEIS ATYWNCPCVP MRERKECHCM LFLTPDNEFT SDLQEIDKTT LLEKIASS
