Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ferredoxin-thioredoxin reductase, catalytic chain (FTR-C) (EC 1.8.7.2) (Ferredoxin-thioredoxin reductase subunit B) (FTR-B)

 FTRC_SYNY3              Reviewed;         118 AA.
Q55389;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 109.
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};
Short=FTR-C {ECO:0000303|PubMed:10649999, ECO:0000303|PubMed:17611542, ECO:0000303|PubMed:19132843, ECO:0000303|PubMed:19908864};
EC=1.8.7.2 {ECO:0000269|PubMed:14769790};
AltName: Full=Ferredoxin-thioredoxin reductase subunit B {ECO:0000250|UniProtKB:P41348};
Short=FTR-B {ECO:0000250|UniProtKB:P41348};
Name=ftrC {ECO:0000303|PubMed:19825613, ECO:0000312|EMBL:BAA10479.1};
ORFNames=sll0554;
Synechocystis sp. (strain PCC 6803 / Kazusa).
Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
Synechocystis.
NCBI_TaxID=1111708;
[1] {ECO:0000312|EMBL:BAA10479.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 6803 / Kazusa;
PubMed=8905231; DOI=10.1093/dnares/3.3.109;
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium
Synechocystis sp. strain PCC6803. II. Sequence determination of the
entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).
[2] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-58; HIS-87 AND CYS-88.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:14769790};
PubMed=14769790; DOI=10.1074/jbc.M313851200;
Glauser D.A., Bourquin F., Manieri W., Schurmann P.;
"Characterization of ferredoxin:thioredoxin reductase modified by
site-directed mutagenesis.";
J. Biol. Chem. 279:16662-16669(2004).
[3] {ECO:0000305}
COFACTOR, SUBUNIT, AND NMR SPECTROSCOPY OF THE COMPLEX CONTAINING THE
FTR HETERODIMER AND FERREDOXIN.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:17134703};
PubMed=17134703; DOI=10.1016/j.febslet.2006.11.027;
Xu X., Kim S.K., Schurmann P., Hirasawa M., Tripathy J.N., Smith J.,
Knaff D.B., Ubbink M.;
"Ferredoxin/ferredoxin-thioredoxin reductase complex: Complete NMR
mapping of the interaction site on ferredoxin by gallium
substitution.";
FEBS Lett. 580:6714-6720(2006).
[4] {ECO:0000305}
CATALYTIC ACTIVITY, COFACTOR, EPR SPECTROSCOPY; RESONANCE RAMAN
SPECTROSCOPY; MOSSBAUER SPECTROSCOPY AND MAGNETIC CIRCULAR DICHROISM,
SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF HIS-87.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:19132843};
PubMed=19132843; DOI=10.1021/bi802074p;
Walters E.M., Garcia-Serres R., Naik S.G., Bourquin F., Glauser D.A.,
Schurmann P., Huynh B.H., Johnson M.K.;
"Role of histidine-86 in the catalytic mechanism of
ferredoxin:thioredoxin reductase.";
Biochemistry 48:1016-1024(2009).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND NMR SPECTROSCOPY
OF THE COMPLEX CONTAINING FERREDOXIN; THE FTR HETERODIMER AND TRX-M.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:19908864};
PubMed=19908864; DOI=10.1021/ja904205k;
Xu X., Schurmann P., Chung J.S., Hass M.A., Kim S.K., Hirasawa M.,
Tripathy J.N., Knaff D.B., Ubbink M.;
"Ternary protein complex of ferredoxin, ferredoxin:thioredoxin
reductase, and thioredoxin studied by paramagnetic NMR spectroscopy.";
J. Am. Chem. Soc. 131:17576-17582(2009).
[6] {ECO:0000305}
INDUCTION.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:19825613};
PubMed=19825613; DOI=10.1093/mp/ssn070;
Perez-Perez M.E., Martin-Figueroa E., Florencio F.J.;
"Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC
6803 thioredoxin system and functional analysis of TrxB (Trx x) and
TrxQ (Trx y) thioredoxins.";
Mol. Plant 2:270-283(2009).
[7] {ECO:0000305, ECO:0000312|PDB:1DJ7}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-118 IN COMPLEX WITH
IRON-SULFUR (4FE-4S) AND FTRV, FUNCTION, COFACTOR, SUBUNIT, ACTIVE
SITE, AND DISULFIDE BOND.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:10649999};
PubMed=10649999; DOI=10.1126/science.287.5453.655;
Dai S., Schwendtmayer C., Schurmann P., Ramaswamy S., Eklund H.;
"Redox signaling in chloroplasts: cleavage of disulfides by an iron-
sulfur cluster.";
Science 287:655-658(2000).
[8] {ECO:0000305, ECO:0000312|PDB:2PU9}
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 8-118 IN COMPLEXES WITH
IRON-SULFUR (4FE-4S); FTRV; PETF/FERREDOXIN; TRX-F AND TRX-M,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND
DISULFIDE BOND.
STRAIN=ATCC 27184 / PCC 6803 / N-1 {ECO:0000269|PubMed:17611542};
PubMed=17611542; DOI=10.1038/nature05937;
Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W.,
Schurmann P., Eklund H.;
"Structural snapshots along the reaction pathway of ferredoxin-
thioredoxin reductase.";
Nature 448:92-96(2007).
-!- FUNCTION: Catalytic subunit of the ferredoxin-thioredoxin
reductase (FTR), which catalyzes the two-electron reduction of
thioredoxins by the electrons provided by reduced ferredoxin.
{ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:14769790,
ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19908864}.
-!- CATALYTIC ACTIVITY: 2 reduced ferredoxin + thioredoxin disulfide =
2 oxidized ferredoxin + thioredoxin + 2 H(+).
{ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17611542,
ECO:0000269|PubMed:19132843, ECO:0000269|PubMed:19908864}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17134703,
ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843,
ECO:0000269|PubMed:19908864};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17134703,
ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843,
ECO:0000269|PubMed:19908864};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Redox potential:
E(0) is -320 mV. {ECO:0000269|PubMed:14769790};
-!- SUBUNIT: Heterodimer of subunit A (variable subunit) and subunit B
(catalytic subunit). Heterodimeric FTR forms a complex with
ferredoxin and thioredoxin. {ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17134703,
ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843,
ECO:0000269|PubMed:19908864}.
-!- INTERACTION:
P07591:- (xeno); NbExp=4; IntAct=EBI-863211, EBI-537449;
P09856:- (xeno); NbExp=5; IntAct=EBI-863211, EBI-863615;
Q55781:ftrV; NbExp=4; IntAct=EBI-863211, EBI-863219;
P27320:petF; NbExp=4; IntAct=EBI-863211, EBI-863421;
-!- INDUCTION: Dependent on photosynthetic conditions. Expression
declines about 80-90% in the darkness. Re-illumination up-
regulates the expression to normal levels. In the presence of
glucose, expression is down-regulated by about 20%.
{ECO:0000269|PubMed:19825613}.
-!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta
subunit family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BA000022; BAA10479.1; -; Genomic_DNA.
PIR; S75744; S75744.
PDB; 1DJ7; X-ray; 1.60 A; A=2-118.
PDB; 2PU9; X-ray; 1.65 A; A=9-118.
PDB; 2PUK; X-ray; 3.00 A; A/E=9-116.
PDB; 2PUO; X-ray; 1.70 A; A=8-116.
PDB; 2PVD; X-ray; 1.95 A; A=12-118.
PDB; 2PVG; X-ray; 2.40 A; A=11-116.
PDB; 2PVO; X-ray; 3.40 A; A=9-118.
PDBsum; 1DJ7; -.
PDBsum; 2PU9; -.
PDBsum; 2PUK; -.
PDBsum; 2PUO; -.
PDBsum; 2PVD; -.
PDBsum; 2PVG; -.
PDBsum; 2PVO; -.
ProteinModelPortal; Q55389; -.
SMR; Q55389; -.
DIP; DIP-35307N; -.
IntAct; Q55389; 10.
STRING; 1148.SYNGTS_2516; -.
PRIDE; Q55389; -.
EnsemblBacteria; BAA10479; BAA10479; BAA10479.
KEGG; syn:sll0554; -.
HOGENOM; HOG000265597; -.
InParanoid; Q55389; -.
KO; K17892; -.
OMA; RTGTYFC; -.
PhylomeDB; Q55389; -.
BioCyc; MetaCyc:MONOMER-14463; -.
EvolutionaryTrace; Q55389; -.
Proteomes; UP000001425; Chromosome.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
GO; GO:0103012; F:ferredoxin-thioredoxin reductase activity; IEA:UniProtKB-EC.
GO; GO:0030385; F:ferredoxin:thioredoxin reductase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0015979; P:photosynthesis; IEP:UniProtKB.
Gene3D; 3.90.460.10; -; 1.
InterPro; IPR024707; FTR_bsu.
InterPro; IPR004209; FTR_bsu_dom.
InterPro; IPR036644; FTR_bsu_sf.
Pfam; PF02943; FeThRed_B; 1.
PIRSF; PIRSF000260; FTRc; 1.
SUPFAM; SSF57662; SSF57662; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Complete proteome; Disulfide bond;
Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
Redox-active center; Reference proteome; Transport.
CHAIN 1 118 Ferredoxin-thioredoxin reductase,
catalytic chain.
/FTId=PRO_0000423926.
ACT_SITE 58 58 Nucleophile.
{ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:14769790,
ECO:0000269|PubMed:17611542,
ECO:0000269|PubMed:19132843}.
METAL 56 56 Iron-sulfur (4Fe-4S).
{ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:17611542}.
METAL 75 75 Iron-sulfur (4Fe-4S).
{ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:17611542}.
METAL 77 77 Iron-sulfur (4Fe-4S).
{ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:17611542}.
METAL 86 86 Iron-sulfur (4Fe-4S).
{ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:17611542}.
SITE 87 87 Increases the nucleophilicity of the
active site Cys.
{ECO:0000269|PubMed:19132843}.
DISULFID 58 88 Redox-active.
{ECO:0000269|PubMed:10649999,
ECO:0000269|PubMed:17611542}.
MUTAGEN 58 58 C->S: Loss of enzyme activity.
{ECO:0000269|PubMed:14769790}.
MUTAGEN 87 87 H->Y: Greatly reduced catalytic activity.
Abolishes significant electronic
interaction between the disulfide and a
unique Fe site of the [4Fe-4S](2+)
cluster in oxidized form of the
reductase. {ECO:0000269|PubMed:14769790,
ECO:0000269|PubMed:19132843}.
MUTAGEN 88 88 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:14769790}.
HELIX 9 25 {ECO:0000244|PDB:1DJ7}.
STRAND 31 33 {ECO:0000244|PDB:1DJ7}.
HELIX 34 51 {ECO:0000244|PDB:1DJ7}.
STRAND 57 59 {ECO:0000244|PDB:1DJ7}.
HELIX 64 70 {ECO:0000244|PDB:1DJ7}.
STRAND 74 76 {ECO:0000244|PDB:1DJ7}.
HELIX 78 83 {ECO:0000244|PDB:1DJ7}.
STRAND 89 92 {ECO:0000244|PDB:1DJ7}.
STRAND 96 99 {ECO:0000244|PDB:2PVG}.
HELIX 107 115 {ECO:0000244|PDB:1DJ7}.
SEQUENCE 118 AA; 13390 MW; 93B2F674C59A3CCE CRC64;
MTSSDTQNNK TLAAMKNFAE QYAKRTDTYF CSDLSVTAVV IEGLARHKEE LGSPLCPCRH
YEDKEAEVKN TFWNCPCVPM RERKECHCML FLTPDNDFAG DAQDIPMETL EEVKASMA


Related products :

Catalog number Product name Quantity
EIAAB44144 NADPH-dependent thioredoxin reductase,Rat,Rattus norvegicus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
EIAAB44153 Homo sapiens,Human,TGR,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,TRXR3,TXNRD3
orb90288 Yeast Thioredoxin Reductase protein Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin R 5
EIAAB44154 Mouse,Mus musculus,Tgr,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,Trxr3,Txnrd3
EIAAB43736 Homo sapiens,Human,Protein TXNRD3NB,Thioredoxin reductase 2 intronic transcript 1,Thioredoxin reductase 3 intronic transcript 1,Thioredoxin reductase 3 neighbor gene protein,Thioredoxin reductase 3 ne
LF-MA0033 anti-Ferredoxin Reductase (6C2), Mouse monoclonal to Ferredoxin Reductase, Isotype IgG1, Host Mouse 100 ul
LF-PA0003 anti-Ferredoxin Reductase, Rabbit polyclonal to Ferredoxin Reductase, Isotype IgG, Host Rabbit 100 ul
EIAAB44150 Homo sapiens,Human,KIAA1652,Selenoprotein Z,SelZ,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,TR-beta,TRXR2,TXNRD2
EIAAB44146 Mouse,Mus musculus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
EIAAB44152 Rat,Rattus norvegicus,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,Trxr2,Txnrd2
EIAAB44151 Bos taurus,Bovine,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,TRXR2,TXNRD2
EIAAB44149 Mouse,Mus musculus,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,Trxr2,Txnrd2
EIAAB44145 Bos taurus,Bovine,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,TXNRD1
EIAAB44147 Pig,Sus scrofa,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,TXNRD1
LF-MA0054 anti-Thioredoxin Reductase 2 (25B3), Mouse monoclonal to Thioredoxin Reductase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0015 anti-Thioredoxin Reductase 1 (19A1), Mouse monoclonal to Thioredoxin Reductase 1, Isotype IgG1, Host Mouse 100 ul
LF-MA0025 anti-Thioredoxin Reductase 2 (7B2), Mouse monoclonal to Thioredoxin Reductase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0020 anti-Thioredoxin Reductase 1 (5A5), Mouse monoclonal to Thioredoxin Reductase 1, Isotype IgG1, Host Mouse 100 ul
LF-PA0024 anti-Thioredoxin Reductase 2, Rabbit polyclonal to Thioredoxin Reductase 2, Isotype IgG, Host Rabbit 100 ul
LF-PA0023 anti-Thioredoxin Reductase 1, Rabbit polyclonal to Thioredoxin Reductase 1, Isotype IgG, Host Rabbit 100 ul
LF-PA10017 anti-Thioredoxin Reductase 1, Rabbit polyclonal to Thioredoxin Reductase 1, Isotype , Host Rabbit 100 ug
LF-PA41227 anti-Thioredoxin Reductase 2 , Rabbit polyclonal to Thioredoxin Reductase 2 , Isotype IgG, Host Rabbit 50 ug
PC-564 Ferredoxin Reductase 100 uL
LF-MA0033 Ferredoxin reductase 0.1 ml
PC-564 Ferredoxin Reductase Poly 100 uL


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur