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

Thioredoxin M-type, chloroplastic (Trx-M) [Cleaved into: Thioredoxin M-type Mc; Thioredoxin M-type Md]

 TRXM_SPIOL              Reviewed;         181 AA.
P07591; Q41394; Q41395;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 120.
RecName: Full=Thioredoxin M-type, chloroplastic;
Short=Trx-M;
Contains:
RecName: Full=Thioredoxin M-type Mc;
Contains:
RecName: Full=Thioredoxin M-type Md;
Flags: Precursor;
Spinacia oleracea (Spinach).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae;
Anserineae; Spinacia.
NCBI_TaxID=3562;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1536927; DOI=10.1007/BF00040668;
Wedel N., Clausmeyer S., Herrmann R.G., Gardet-Salvi L., Schurmann P.;
"Nucleotide sequence of cDNAs encoding the entire precursor
polypeptide for thioredoxin m from spinach chloroplasts.";
Plant Mol. Biol. 18:527-533(1992).
[2]
PROTEIN SEQUENCE OF 68-181.
PubMed=3510868; DOI=10.1111/j.1432-1033.1986.tb09379.x;
Maeda K., Tsugita A., Dalzoppo D., Vilbois F., Schurmann P.;
"Further characterization and amino acid sequence of m-type
thioredoxins from spinach chloroplasts.";
Eur. J. Biochem. 154:197-203(1986).
[3]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 75-179, AND DISULFIDE BOND.
PubMed=10964566; DOI=10.1006/jmbi.2000.4006;
Capitani G., Markovic-Housley Z., DelVal G., Morris M.,
Jansonius J.N., Schurmann P.;
"Crystal structures of two functionally different thioredoxins in
spinach chloroplasts.";
J. Mol. Biol. 302:135-154(2000).
[4]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 75-180 OF MUTANT SER-107 IN
COMPLEXES WITH BACTERIAL FTRC; FTRV AND PETF/FERREDOXIN, SUBUNIT, AND
MUTAGENESIS OF CYS-107.
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: Participates in various redox reactions through the
reversible oxidation of the active center dithiol to a disulfide.
The M form is known to activate NADP-malate dehydrogenase.
-!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
reductase (FTR) and ferredoxin. {ECO:0000269|PubMed:17611542}.
-!- INTERACTION:
Q55389:ftrC (xeno); NbExp=4; IntAct=EBI-537449, EBI-863211;
Q9LU86:PRXQ (xeno); NbExp=2; IntAct=EBI-537449, EBI-540311;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X51462; CAA35826.1; -; mRNA.
EMBL; X51463; CAA35827.1; -; mRNA.
PIR; S20496; TXSPM.
PDB; 1FB0; X-ray; 2.26 A; A/B=75-179.
PDB; 1FB6; X-ray; 2.10 A; A/B=75-179.
PDB; 1GL8; NMR; -; A=76-179.
PDB; 2PUK; X-ray; 3.00 A; C/G=75-180.
PDBsum; 1FB0; -.
PDBsum; 1FB6; -.
PDBsum; 1GL8; -.
PDBsum; 2PUK; -.
ProteinModelPortal; P07591; -.
SMR; P07591; -.
DIP; DIP-33500N; -.
IntAct; P07591; 43.
PRIDE; P07591; -.
SABIO-RK; P07591; -.
EvolutionaryTrace; P07591; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
InterPro; IPR005746; Thioredoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10438; PTHR10438; 1.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR01068; thioredoxin; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Chloroplast; Direct protein sequencing; Disulfide bond;
Electron transport; Plastid; Redox-active center; Transit peptide;
Transport.
TRANSIT 1 67 Chloroplast.
{ECO:0000269|PubMed:3510868}.
CHAIN 68 181 Thioredoxin M-type, chloroplastic.
/FTId=PRO_0000034178.
CHAIN 69 181 Thioredoxin M-type Mc.
/FTId=PRO_0000045891.
CHAIN 70 181 Thioredoxin M-type Md.
/FTId=PRO_0000045892.
DOMAIN 68 180 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 104 104 Nucleophile.
ACT_SITE 107 107 Nucleophile.
SITE 98 98 Deprotonates C-terminal active site Cys.
SITE 105 105 Contributes to redox potential value.
SITE 106 106 Contributes to redox potential value.
DISULFID 104 107 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691,
ECO:0000269|PubMed:10964566}.
VARIANT 25 25 H -> Y.
VARIANT 33 33 V -> L.
VARIANT 37 37 T -> S.
MUTAGEN 107 107 C->S: Prevents scission of the
intermolecular disulfide bond by the
second Cys of the active site.
{ECO:0000269|PubMed:17611542}.
CONFLICT 83 83 S -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 90 95 ESEVPV -> QSSEPS (in Ref. 2; AA
sequence). {ECO:0000305}.
CONFLICT 128 128 Y -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 165 170 AVPKST -> DVSKYQ (in Ref. 2; AA
sequence). {ECO:0000305}.
TURN 81 83 {ECO:0000244|PDB:1FB6}.
HELIX 84 87 {ECO:0000244|PDB:1FB6}.
TURN 88 90 {ECO:0000244|PDB:1FB6}.
STRAND 91 93 {ECO:0000244|PDB:1GL8}.
STRAND 95 100 {ECO:0000244|PDB:1FB6}.
HELIX 102 104 {ECO:0000244|PDB:1GL8}.
HELIX 105 120 {ECO:0000244|PDB:1FB6}.
TURN 121 124 {ECO:0000244|PDB:1FB6}.
STRAND 126 131 {ECO:0000244|PDB:1FB6}.
TURN 132 134 {ECO:0000244|PDB:1FB6}.
HELIX 136 141 {ECO:0000244|PDB:1FB6}.
STRAND 146 154 {ECO:0000244|PDB:1FB6}.
STRAND 157 164 {ECO:0000244|PDB:1FB6}.
HELIX 168 178 {ECO:0000244|PDB:1FB6}.
SEQUENCE 181 AA; 19840 MW; 5127D4BDF72D81E9 CRC64;
MAIENCLQLS TSASVGTVAV KSHVHHLQPS SKVNVPTFRG LKRSFPALSS SVSSSSPRQF
RYSSVVCKAS EAVKEVQDVN DSSWKEFVLE SEVPVMVDFW APWCGPCKLI APVIDELAKE
YSGKIAVYKL NTDEAPGIAT QYNIRSIPTV LFFKNGERKE SIIGAVPKST LTDSIEKYLS
P


Related products :

Catalog number Product name Quantity
EIAAB44640 Mouse,Mus musculus,Spermatid-specific thioredoxin-3,Sptrx3,Sptrx-3,Thioredoxin domain-containing protein 8,Thioredoxin-6,Trx6,Txndc8
EIAAB44639 Homo sapiens,Human,Spermatid-specific thioredoxin-3,SPTRX3,Sptrx-3,Thioredoxin domain-containing protein 8,Thioredoxin-6,TRX6,TXNDC8
EIAAB44631 Mouse,Mus musculus,Spermatid-specific thioredoxin-1,Sptrx,Sptrx1,Sptrx-1,Thioredoxin domain-containing protein 2,Thioredoxin-4,Trx4,Txndc2
SCH-MCA1538 MOUSE ANTI HUMAN THIOREDOXIN, Product Type Monoclonal Antibody, Specificity THIOREDOXIN, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications C, E, WB, Clone 2B1 0.2 mg
0100-0468 RABBIT ANTI THIOREDOXIN, Product Type Polyclonal Antibody, Specificity THIOREDOXIN, Target Species Bacterial, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications E, Clone 1 ml
SCH-0100-0468 RABBIT ANTI THIOREDOXIN, Product Type Polyclonal Antibody, Specificity THIOREDOXIN, Target Species Bacterial, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications E, Clone 1 ml
MCA1538 MOUSE ANTI HUMAN THIOREDOXIN, Product Type Monoclonal Antibody, Specificity THIOREDOXIN, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications C, E, WB, Clone 2B1 0.2 mg
EIAAB44144 NADPH-dependent thioredoxin reductase,Rat,Rattus norvegicus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
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
EIAAB44637 Endoplasmic reticulum resident protein 46,ER protein 46,ERp46,Mouse,Mus musculus,PC-TRP,Plasma cell-specific thioredoxin-related protein,Thioredoxin domain-containing protein 5,Thioredoxin-like protei
EIAAB44153 Homo sapiens,Human,TGR,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,TRXR3,TXNRD3
EIAAB44613 14 kDa thioredoxin-related protein,Homo sapiens,Human,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,TXNDC17,TXNL5
EIAAB44154 Mouse,Mus musculus,Tgr,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,Trxr3,Txnrd3
EIAAB44614 14 kDa thioredoxin-related protein,Mouse,Mus musculus,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,Txndc17,Txnl5
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
MCA3521Z MOUSE ANTI HUMAN THIOREDOXIN Azide Free, Product Type Monoclonal Antibody, Specificity THIOREDOXIN, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applications IF, WB, Clon 0.1 mg
EIAAB42264 MTRX,Mt-Trx,Rat,Rattus norvegicus,Thioredoxin, mitochondrial,Thioredoxin-2,Trx2,Txn2
EIAAB42265 Bos taurus,Bovine,MTRX,Mt-Trx,Thioredoxin, mitochondrial,Thioredoxin-2,TXN2
EIAAB42266 Mouse,MTRX,Mt-Trx,Mus musculus,Thioredoxin, mitochondrial,Thioredoxin-2,Txn2
EIAAB42267 Homo sapiens,Human,MTRX,Mt-Trx,Thioredoxin, mitochondrial,Thioredoxin-2,TRX2,TXN2
Mab-607057 Monoclonal Antibodies: Thioredoxin (TRX); Specificity: Thioredoxin (TRX) ; Application: IHC 0.1ml
EIAAB44634 Rat,Rattus norvegicus,Spermatid-specific thioredoxin-2,Sptrx2,Sptrx-2,Thioredoxin domain-containing protein 3,Txndc3
EIAAB44633 Mouse,Mus musculus,Spermatid-specific thioredoxin-2,Sptrx2,Sptrx-2,Thioredoxin domain-containing protein 3,Txndc3
EIAAB44641 Rat,Rattus norvegicus,Spermatid-specific thioredoxin-3,Sptrx3,Sptrx-3,Thioredoxin domain-containing protein 8,Txndc8
20-271-80109 Thioredoxin (TRX) - Mouse Anti Thioredoxin (TRX) Monoclonal 0.1 mg


 

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