FTRC_SYNY3
ID FTRC_SYNY3 Reviewed; 118 AA.
AC Q55389;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ferredoxin-thioredoxin reductase, catalytic chain {ECO:0000303|PubMed:10649999, ECO:0000303|PubMed:17611542, ECO:0000303|PubMed:19132843, ECO:0000303|PubMed:19825613, ECO:0000312|EMBL:BAA10479.1};
DE Short=FTR-C {ECO:0000303|PubMed:10649999, ECO:0000303|PubMed:17611542, ECO:0000303|PubMed:19132843, ECO:0000303|PubMed:19908864};
DE EC=1.8.7.2 {ECO:0000269|PubMed:14769790};
DE AltName: Full=Ferredoxin-thioredoxin reductase subunit B {ECO:0000250|UniProtKB:P41348};
DE Short=FTR-B {ECO:0000250|UniProtKB:P41348};
GN Name=ftrC {ECO:0000303|PubMed:19825613, ECO:0000312|EMBL:BAA10479.1};
GN ORFNames=sll0554;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1] {ECO:0000312|EMBL:BAA10479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-58; HIS-87 AND CYS-88.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:14769790};
RX PubMed=14769790; DOI=10.1074/jbc.m313851200;
RA Glauser D.A., Bourquin F., Manieri W., Schurmann P.;
RT "Characterization of ferredoxin:thioredoxin reductase modified by site-
RT directed mutagenesis.";
RL J. Biol. Chem. 279:16662-16669(2004).
RN [3] {ECO:0000305}
RP COFACTOR, SUBUNIT, AND NMR SPECTROSCOPY OF THE COMPLEX CONTAINING THE FTR
RP HETERODIMER AND FERREDOXIN.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:17134703};
RX PubMed=17134703; DOI=10.1016/j.febslet.2006.11.027;
RA Xu X., Kim S.K., Schurmann P., Hirasawa M., Tripathy J.N., Smith J.,
RA Knaff D.B., Ubbink M.;
RT "Ferredoxin/ferredoxin-thioredoxin reductase complex: Complete NMR mapping
RT of the interaction site on ferredoxin by gallium substitution.";
RL FEBS Lett. 580:6714-6720(2006).
RN [4] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, EPR SPECTROSCOPY; RESONANCE RAMAN
RP SPECTROSCOPY; MOSSBAUER SPECTROSCOPY AND MAGNETIC CIRCULAR DICHROISM,
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF HIS-87.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:19132843};
RX PubMed=19132843; DOI=10.1021/bi802074p;
RA Walters E.M., Garcia-Serres R., Naik S.G., Bourquin F., Glauser D.A.,
RA Schurmann P., Huynh B.H., Johnson M.K.;
RT "Role of histidine-86 in the catalytic mechanism of ferredoxin:thioredoxin
RT reductase.";
RL Biochemistry 48:1016-1024(2009).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND NMR SPECTROSCOPY OF
RP THE COMPLEX CONTAINING FERREDOXIN; THE FTR HETERODIMER AND TRX-M.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:19908864};
RX PubMed=19908864; DOI=10.1021/ja904205k;
RA Xu X., Schurmann P., Chung J.S., Hass M.A., Kim S.K., Hirasawa M.,
RA Tripathy J.N., Knaff D.B., Ubbink M.;
RT "Ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase,
RT and thioredoxin studied by paramagnetic NMR spectroscopy.";
RL J. Am. Chem. Soc. 131:17576-17582(2009).
RN [6] {ECO:0000305}
RP INDUCTION.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:19825613};
RX PubMed=19825613; DOI=10.1093/mp/ssn070;
RA Perez-Perez M.E., Martin-Figueroa E., Florencio F.J.;
RT "Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803
RT thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y)
RT thioredoxins.";
RL Mol. Plant 2:270-283(2009).
RN [7] {ECO:0000305, ECO:0000312|PDB:1DJ7}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-118 IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S) AND FTRV, FUNCTION, COFACTOR, SUBUNIT, ACTIVE SITE, AND DISULFIDE
RP BOND.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:10649999};
RX PubMed=10649999; DOI=10.1126/science.287.5453.655;
RA Dai S., Schwendtmayer C., Schurmann P., Ramaswamy S., Eklund H.;
RT "Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur
RT cluster.";
RL Science 287:655-658(2000).
RN [8] {ECO:0000305, ECO:0000312|PDB:2PU9}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 8-118 IN COMPLEXES WITH
RP IRON-SULFUR (4FE-4S); FTRV; PETF/FERREDOXIN; TRX-F AND TRX-M, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND DISULFIDE BOND.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:17611542};
RX PubMed=17611542; DOI=10.1038/nature05937;
RA Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., Schurmann P.,
RA Eklund H.;
RT "Structural snapshots along the reaction pathway of ferredoxin-thioredoxin
RT reductase.";
RL Nature 448:92-96(2007).
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:0000269|PubMed:10649999, ECO:0000269|PubMed:14769790,
CC ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19908864}.
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|PubMed:14769790, ECO:0000269|PubMed:17611542,
CC ECO:0000269|PubMed:19132843, ECO:0000269|PubMed:19908864};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:14769790,
CC ECO:0000269|PubMed:17134703, ECO:0000269|PubMed:17611542,
CC ECO:0000269|PubMed:19132843, ECO:0000269|PubMed:19908864};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:10649999,
CC ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17134703,
CC ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843,
CC ECO:0000269|PubMed:19908864};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -320 mV. {ECO:0000269|PubMed:14769790};
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:0000269|PubMed:10649999,
CC ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17134703,
CC ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843,
CC ECO:0000269|PubMed:19908864}.
CC -!- INTERACTION:
CC Q55389; Q55781: ftrV; NbExp=4; IntAct=EBI-863211, EBI-863219;
CC Q55389; P27320: petF; NbExp=4; IntAct=EBI-863211, EBI-863421;
CC Q55389; P07591; Xeno; NbExp=4; IntAct=EBI-863211, EBI-537449;
CC Q55389; P09856; Xeno; NbExp=5; IntAct=EBI-863211, EBI-863615;
CC -!- INDUCTION: Dependent on photosynthetic conditions. Expression declines
CC about 80-90% in the darkness. Re-illumination up-regulates the
CC expression to normal levels. In the presence of glucose, expression is
CC down-regulated by about 20%. {ECO:0000269|PubMed:19825613}.
CC -!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta
CC subunit family. {ECO:0000305}.
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; BA000022; BAA10479.1; -; Genomic_DNA.
DR PIR; S75744; S75744.
DR PDB; 1DJ7; X-ray; 1.60 A; A=2-118.
DR PDB; 2PU9; X-ray; 1.65 A; A=9-118.
DR PDB; 2PUK; X-ray; 3.00 A; A/E=9-116.
DR PDB; 2PUO; X-ray; 1.70 A; A=8-116.
DR PDB; 2PVD; X-ray; 1.95 A; A=12-118.
DR PDB; 2PVG; X-ray; 2.40 A; A=11-116.
DR PDB; 2PVO; X-ray; 3.40 A; A=9-118.
DR PDBsum; 1DJ7; -.
DR PDBsum; 2PU9; -.
DR PDBsum; 2PUK; -.
DR PDBsum; 2PUO; -.
DR PDBsum; 2PVD; -.
DR PDBsum; 2PVG; -.
DR PDBsum; 2PVO; -.
DR AlphaFoldDB; Q55389; -.
DR SMR; Q55389; -.
DR DIP; DIP-35307N; -.
DR IntAct; Q55389; 10.
DR STRING; 1148.1001238; -.
DR PaxDb; Q55389; -.
DR EnsemblBacteria; BAA10479; BAA10479; BAA10479.
DR KEGG; syn:sll0554; -.
DR eggNOG; COG4802; Bacteria.
DR InParanoid; Q55389; -.
DR OMA; QAFWNCP; -.
DR PhylomeDB; Q55389; -.
DR BioCyc; MetaCyc:MON-14463; -.
DR BRENDA; 1.8.7.2; 6192.
DR EvolutionaryTrace; Q55389; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0103012; F:ferredoxin-thioredoxin reductase activity; IDA: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 GO; GO:0015979; P:photosynthesis; IEP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Disulfide bond; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..118
FT /note="Ferredoxin-thioredoxin reductase, catalytic chain"
FT /id="PRO_0000423926"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:10649999,
FT ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17611542,
FT ECO:0000269|PubMed:19132843"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10649999,
FT ECO:0000269|PubMed:17611542"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10649999,
FT ECO:0000269|PubMed:17611542"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10649999,
FT ECO:0000269|PubMed:17611542"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10649999,
FT ECO:0000269|PubMed:17611542"
FT SITE 87
FT /note="Increases the nucleophilicity of the active site
FT Cys"
FT /evidence="ECO:0000269|PubMed:19132843"
FT DISULFID 58..88
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:10649999,
FT ECO:0000269|PubMed:17611542"
FT MUTAGEN 58
FT /note="C->S: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:14769790"
FT MUTAGEN 87
FT /note="H->Y: Greatly reduced catalytic activity. Abolishes
FT significant electronic interaction between the disulfide
FT and a unique Fe site of the [4Fe-4S](2+) cluster in
FT oxidized form of the reductase."
FT /evidence="ECO:0000269|PubMed:14769790,
FT ECO:0000269|PubMed:19132843"
FT MUTAGEN 88
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:14769790"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:1DJ7"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1DJ7"
FT HELIX 34..51
FT /evidence="ECO:0007829|PDB:1DJ7"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1DJ7"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:1DJ7"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1DJ7"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1DJ7"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1DJ7"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2PVG"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1DJ7"
SQ SEQUENCE 118 AA; 13390 MW; 93B2F674C59A3CCE CRC64;
MTSSDTQNNK TLAAMKNFAE QYAKRTDTYF CSDLSVTAVV IEGLARHKEE LGSPLCPCRH
YEDKEAEVKN TFWNCPCVPM RERKECHCML FLTPDNDFAG DAQDIPMETL EEVKASMA
