Sequence of TRXR1_DROME
EC Number:1.8.1.9
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
Other sequences found for EC No. 1.8.1.9
General information:
Sequence
0 MNLCNSRFSV TFVRQCSTIL TSPSAGIIQN RGSLTTKVPH WISSSLSCAH HTFQRTMNLT
60 GQRGSRDSTG ATGGNAPAGS GAGAPPPFQH PHCDRAAMYA QPVRKMSTKG GSYDYDLIVI
120 GGGSAGLACA KEAVLNGARV ACLDFVKPTP TLGTKWGVGG TCVNVGCIPK KLMHQASLLG
180 EAVHEAAAYG WNVDEKIKPD WHKLVQSVQN HIKSVNWVTR VDLRDKKVEY INGLGSFVDS
240 HTLLAKLKSG ERTITAQTFV IAVGGRPRYP DIPGAVEYGI TSDDLFSLDR EPGKTLVVGA
300 GYIGLECAGF LKGLGYEPTV MVRSIVLRGF DQQMAELVAA SMEERGIPFL RKTVPLSVEK
360 QDDGKLLVKY KNVETGEEAE DVYDTVLWAI GRKGLVDDLN LPNAGVTVQK DKIPVDSQEA
420 TNVANIYAVG DIIYGKPELT PVAVLAGRLL ARRLYGGSTQ RMDYKDVATT VFTPLEYACV
480 GLSEEDAVKQ FGADEIEVFH GYYKPTEFFI PQKSVRYCYL KAVAERHGDQ RVYGLHYIGP
540 VAGEVIQGFA AALKSGLTIN TLINTVGIHP TTAEEFTRLA ITKRSGLDPT PASCCS
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
495990
Candas M.,Sohal R.S.,Radyuk S.N.,Klichko V.I.,Orr W.C.
Molecular organization of the glutathione reductase gene in Drosophila melanogaster.
Arch. Biochem. Biophys.
339
323-334
1997
495991
Kanzok S.M.,Fechner A.,Bauer H.,Ulschmid J.K.,Muller H.M.,Botella-Munoz J.,Schneuwly S.,Schirmer R.,Becker K.
Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster.
Science
291
643-646
2001
495992
Adams M.D.,Celniker S.E.,Holt R.A.,Evans C.A.,Gocayne J.D.,Amanatides P.G.,Scherer S.E.,Li P.W.,Hoskins R.A.,Galle R.F.,George R.A.,Lewis S.E.,Richards S.,Ashburner M.,Henderson S.N.,Sutton G.G.,Wortman J.R.,Yandell M.D.,Zhang Q.,Chen L.X.,Brandon R.C.,Rogers Y.-H.C.,Blazej R.G.,Champe M.,Pfeiffer B.D.,Wan K.H.,Doyle C.,Baxter E.G.,Helt G.,Nelson C.R.,Miklos G.L.G.,Abril J.F.,Agbayani A.,An H.-J.,Andrews-Pfannkoch C.,Baldwin D.,Ballew R.M.,Basu A.,Baxendale J.,Bayraktaroglu L.,Beasley E.M.,Beeson K.Y.,Benos P.V.,Berman B.P.,Bhandari D.,Bolshakov S.,Borkova D.,Botchan M.R.,Bouck J.,Brokstein P.,Brottier P.,Burtis K.C.,Busam D.A.,Butler H.,Cadieu E.,Center A.,Chandra I.,Cherry J.M.,Cawley S.,Dahlke C.,Davenport L.B.,Davies P.,de Pablos B.,Delcher A.,Deng Z.,Mays A.D.,Dew I.,Dietz S.M.,Dodson K.,Doup L.E.,Downes M.,Dugan-Rocha S.,Dunkov B.C.,Dunn P.,Durbin K.J.,Evangelista C.C.,Ferraz C.,Ferriera S.,Fleischmann W.,Fosler C.,Gabrielian A.E.,Garg N.S.,Gelbart W.M.,Glasser K.,Glodek A.,Gong F.,Gorrell J.H.,Gu Z.,Guan P.,Harris M.,Harris N.L.,Harvey D.A.,Heiman T.J.,Hernandez J.R.,Houck J.,Hostin D.,Houston K.A.,Howland T.J.,Wei M.-H.,Ibegwam C.,Jalali M.,Kalush F.,Karpen G.H.,Ke Z.,Kennison J.A.,Ketchum K.A.,Kimmel B.E.,Kodira C.D.,Kraft C.L.,Kravitz S.,Kulp D.,Lai Z.,Lasko P.,Lei Y.,Levitsky A.A.,Li J.H.,Li Z.,Liang Y.,Lin X.,Liu X.,Mattei B.,McIntosh T.C.,McLeod M.P.,McPherson D.,Merkulov G.,Milshina N.V.,Mobarry C.,Morris J.,Moshrefi A.,Mount S.M.,Moy M.,Murphy B.,Murphy L.,Muzny D.M.,Nelson D.L.,Nelson D.R.,Nelson K.A.,Nixon K.,Nusskern D.R.,Pacleb J.M.,Palazzolo M.,Pittman G.S.,Pan S.,Pollard J.,Puri V.,Reese M.G.,Reinert K.,Remington K.,Saunders R.D.C.,Scheeler F.,Shen H.,Shue B.C.,Siden-Kiamos I.,Simpson M.,Skupski M.P.,Smith T.J.,Spier E.,Spradling A.C.,Stapleton M.,Strong R.,Sun E.,Svirskas R.,Tector C.,Turner R.,Venter E.,Wang A.H.,Wang X.,Wang Z.-Y.,Wassarman D.A.,Weinstock G.M.,Weissenbach J.,Williams S.M.,Woodage T.,Worley K.C.,Wu D.,Yang S.,Yao Q.A.,Ye J.,Yeh R.-F.,Zaveri J.S.,Zhan M.,Zhang G.,Zhao Q.,Zheng L.,Zheng X.H.,Zhong F.N.,Zhong W.,Zhou X.,Zhu S.C.,Zhu X.,Smith H.O.,Gibbs R.A.,Myers E.W.,Rubin G.M.,Venter J.C.
The genome sequence of Drosophila melanogaster.
Science
287
2185-2195
2000
495993
Misra S.,Crosby M.A.,Mungall C.J.,Matthews B.B.,Campbell K.S.,Hradecky P.,Huang Y.,Kaminker J.S.,Millburn G.H.,Prochnik S.E.,Smith C.D.,Tupy J.L.,Whitfield E.J.,Bayraktaroglu L.,Berman B.P.,Bettencourt B.R.,Celniker S.E.,de Grey A.D.N.J.,Drysdale R.A.,Harris N.L.,Richter J.,Russo S.,Schroeder A.J.,Shu S.Q.,Stapleton M.,Yamada C.,Ashburner M.,Gelbart W.M.,Rubin G.M.,Lewis S.E.
Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.
Genome Biol.
3
0-0
2002
495995
Stapleton M.,Carlson J.W.,Brokstein P.,Yu C.,Champe M.,George R.A.,Guarin H.,Kronmiller B.,Pacleb J.M.,Park S.,Wan K.H.,Rubin G.M.,Celniker S.E.
A Drosophila full-length cDNA resource.
Genome Biol.
3
0-0
2002
495996
Missirlis F.,Phillips J.P.,Jackle H.
Cooperative action of antioxidant defense systems in Drosophila.
Curr. Biol.
11
1272-1277
2001
495997
Gromer S.,Gross J.H.
Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium.
J. Biol. Chem.
277
9701-9706
2002
495998
Missirlis F.,Ulschmid J.K.,Hirosawa-Takamori M.,Groenke S.,Schaefer U.,Becker K.,Phillips J.P.,Jaeckle H.
Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability.
J. Biol. Chem.
277
11521-11526
2002
495999
Bauer H.,Kanzok S.M.,Schirmer R.H.
Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: isolation and characterization of a second thioredoxin in D.melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2.
J. Biol. Chem.
277
17457-17463
2002
496000
Huang H.H.,Arscott L.D.,Ballou D.P.,Williams C.H. Jr.
Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster.
Biochemistry
47
1721-1731
2008
496001
Huang H.H.,Arscott L.D.,Ballou D.P.,Williams C.H.
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster.
Biochemistry
47
12769-12776
2008
496002
Eckenroth B.E.,Rould M.A.,Hondal R.J.,Everse S.J.
Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases.
Biochemistry
46
4694-4705
2007
