P91938 (TRXR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin reductase 1, mitochondrial
Short name=TrxR-1
EC=1.8.1.9

Gene names

Name:	Trxr-1
Synonyms:	GR
ORF Names:	CG2151

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms. Ref.2 Ref.7 Ref.9
Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. Ref.2
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer. Ref.13
Subcellular location	Isoform B: Mitochondrion Ref.9. Isoform A: Cytoplasm Ref.9.
Tissue specificity	During embryogenesis, expression is seen in germ cell progenitors, developing midgut, hindgut and proventriculus. Ref.7
Developmental stage	Expressed both maternally and zygotically during all stages of development, highest expression during adult stages. Ref.7 Ref.9
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Caution	Was originally (Ref.1) thought to be a glutathione reductase.
Biophysicochemical properties	Kinetic parameters: Measurements were conducted with isoform A unless noted otherwise. KM=6.5 µM for NADPH (at pH 7.4) Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 KM=1 µM for NADPH (at pH 7.4, 2 mM EDTA, 100 mM KPO4) KM=1 µM for NADPH (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO4) KM=7.0 µM for dhd (at pH 7.4, 200 µM NADPH, 100 mM KPO4) KM=141 µM for dhd (at pH 7.0, 0.15 mM NADPH, 1 mM EDTA, 1 mg/ml insulin, 50 mM KPO4, 25 degrees Celsius) KM=7 µM for dhd (at pH 7.4, 2 mM EDTA, 100 mM KPO4) KM=19 µM for dhd (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO4) KM=5.9 µM for Trx-2 (at pH 7.4, 100 µM NADPH, 2 mM EDTA, 100 mM KPO4) KM=310 µM for 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) (at pH 7.4, 100 µM NADPH, 100 mM KPO4) KM=0.17 mM for DTNB (at pH 7.0, 0.2 mM NADPH, 10 mM EDTA, 100 mM KPO4, 25 degrees Celsius) KM=380 µM for DTNB (at pH 7.4, 2 mM EDTA, 100 mM KPO4) KM=410 µM for DTNB (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO4) KM=675 µM for methylseleninate (100 µM NADPH) Vmax=24.3 µmol/min/mg enzyme toward NADPH (at pH 7.4) Vmax=16 µmol/min/mg enzyme toward Trx-2 (at pH 7.4, 100 µM NADPH, 2 mM EDTA, 100 mM KPO4, 25 degrees Celsius) pH dependence: Optimum pH is 7.6 for isoform A with Trx-2 and NADPH as substrates.
Sequence caution	The sequence AAK93067.1 differs from that shown. Reason: Chimeric cDNA. Chimeric cDNA originating from chromosomes X and 3.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative initiation Alternative splicing
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NADP Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from mutant phenotype Ref.2. Source: UniProtKB determination of adult lifespan Inferred from mutant phenotype. Source: FlyBase response to DNA damage stimulus Inferred from mutant phenotype. Source: FlyBase response to hypoxia Inferred from mutant phenotype. Source: FlyBase
Cellular component	microtubule associated complex Inferred from direct assay. Source: FlyBase mitochondrion Inferred from direct assay Ref.9. Source: UniProtKB
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Inferred from mutant phenotype. Source: FlyBase protein homodimerization activity Inferred from direct assay Ref.2. Source: FlyBase thioredoxin-disulfide reductase activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform B (identifier: P91938-1)

Also known as: Mito;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Can partially substitute for the cytoplasmic enzyme activity.

Isoform A (identifier: P91938-2)

Also known as: Cyto;

The sequence of this isoform differs from the canonical sequence as follows:
     1-105: Missing.
     106-110: MSTKG → MAPVQ

Note: Unable to compensate for the loss of the mitochondrial enzyme activity.

Isoform C (identifier: P91938-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.
     89-110: QHPHCDRAAMYAQPVRKMSTKG → MLKYMICAIVVGAKKSTSSKYN

Isoform D (identifier: P91938-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-105: Missing.

Note: Produced by alternative initiation at Met-106 of isoform B.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 596

Thioredoxin reductase 1, mitochondrial

PRO_0000030291

Regions

Nucleotide binding

120 – 126

7

FAD

Nucleotide binding

143 – 147

5

FAD

Nucleotide binding

159 – 170

12

FAD

Nucleotide binding

233 – 235

3

FAD

Nucleotide binding

262 – 266

5

FAD

Nucleotide binding

322 – 328

7

NADP

Nucleotide binding

392 – 399

8

FAD

Nucleotide binding

429 – 432

4

FAD

Nucleotide binding

438 – 443

6

FAD

Sites

Active site

569

1

Proton acceptor Ref.13

Binding site

282

1

FAD

Binding site

286

1

FAD

Binding site

302

1

FAD

Binding site

355

1

NADP

Binding site

472

1

FAD

Binding site

570

1

FAD

Amino acid modifications

Disulfide bond

162 ↔ 167

Redox-active Ref.13

Disulfide bond

594 ↔ 595

Redox-active Ref.13

Natural variations

Alternative sequence

1 – 105

105

Missing in isoform A and isoform D.

VSP_005572

Alternative sequence

1 – 88

88

Missing in isoform C.

VSP_005571

Alternative sequence

89 – 110

22

QHPHC…MSTKG → MLKYMICAIVVGAKKSTSSK YN in isoform C.

VSP_005573

Alternative sequence

106 – 110

5

MSTKG → MAPVQ in isoform A.

VSP_005574

Experimental info

Mutagenesis

569

1

H → Q: Almost complete loss of TrX reduction. Ref.11

Mutagenesis

574

1

E → A: Reduced Trx reduction. Ref.12

Mutagenesis

574

1

E → Q: Reduced Trx reduction. Ref.12

Mutagenesis

594

1

C → S: Loss of Trx reduction. Ref.2

Mutagenesis

595

1

C → S: Loss of Trx reduction. Ref.2

Sequence conflict

88

1

F → L in AAK93067. Ref.6

Sequence conflict

134

1

V → S in AAB48441. Ref.1

Sequence conflict

151

1

Missing in AAB48441. Ref.1

Sequence conflict

189 – 190

2

Missing in AAB48441. Ref.1

Sequence conflict

195

1

E → D in AAB48441. Ref.1

Sequence conflict

195

1

E → D in AAK93067. Ref.6

Sequence conflict

203 – 207

5

KLVQS → RLCAV in AAB48441. Ref.1

Sequence conflict

213 – 216

4

KSVN → SRH in AAB48441. Ref.1

Sequence conflict

220

1

R → V in AAB48441. Ref.1

Sequence conflict

239 – 247

9

DSHTLLAKL → TRTHCCPSM in AAB48441. Ref.1

Sequence conflict

264

1

Missing in AAB48441. Ref.1

Sequence conflict

276 – 280

5

VEYGI → AEIGT in AAB48441. Ref.1

Sequence conflict

292

1

Missing in AAB48441. Ref.1

Sequence conflict

317 – 318

2

EP → G in AAB48441. Ref.1

Sequence conflict

351 – 386

36

RKTVP…VYDTV → ADVDRCREADDAAAREYRLT QIRFTTSHHR in AAB48441. Ref.1

Sequence conflict

379

1

A → S in AAK93067. Ref.6

Sequence conflict

396 – 398

3

VDD → CDS in AAB48441. Ref.1

Sequence conflict

403 – 406

4

NAGV → MPAL in AAB48441. Ref.1

Sequence conflict

424 – 425

2

AN → PH in AAB48441. Ref.1

Sequence conflict

455

1

Y → F in AAB48441. Ref.1

Sequence conflict

461

1

R → S in AAB48441. Ref.1

Sequence conflict

473 – 483

11

TPLEYACVGLS → SWSTSASGLA in AAB48441. Ref.1

Sequence conflict

488 – 495

8

VKQFGADE → SSSSEPR in AAB48441. Ref.1

Sequence conflict

559 – 560

2

IN → L in AAB48441. Ref.1

Sequence conflict

583

1

K → KP in AAB48441. Ref.1

Secondary structure

1

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596

Helix Strand Turn

Details...

Beta strand

116 – 120

5

Helix

124 – 135

12

Beta strand

140 – 143

4

Turn

150 – 152

3

Helix

161 – 165

5

Helix

167 – 186

20

Helix

187 – 189

3

Helix

201 – 225

25

Beta strand

229 – 231

3

Beta strand

233 – 239

7

Beta strand

242 – 247

6

Beta strand

257 – 261

5

Beta strand

265 – 267

3

Helix

275 – 278

4

Helix

282 – 285

4

Beta strand

294 – 298

5

Helix

302 – 313

12

Beta strand

317 – 321

5

Helix

332 – 344

13

Beta strand

353 – 360

8

Beta strand

366 – 375

10

Beta strand

378 – 388

11

Beta strand

392 – 394

3

Helix

397 – 399

3

Helix

401 – 403

3

Beta strand

409 – 413

5

Beta strand

426 – 428

3

Helix

440 – 455

16

Beta strand

469 – 471

3

Beta strand

473 – 481

9

Helix

484 – 491

8

Helix

493 – 495

3

Beta strand

496 – 502

7

Helix

506 – 508

3

Turn

509 – 512

4

Beta strand

519 – 527

9

Beta strand

531 – 539

9

Helix

542 – 554

13

Helix

559 – 564

6

Helix

573 – 578

6

Turn

583 – 586

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform B (Mito) [UniParc]. Last modified January 27, 2003. Version 2. Checksum: 8DA6FC08CF6A7292	FASTA	596	64,322
	10 20 30 40 50 60 MNLCNSRFSV TFVRQCSTIL TSPSAGIIQN RGSLTTKVPH WISSSLSCAH HTFQRTMNLT 70 80 90 100 110 120 GQRGSRDSTG ATGGNAPAGS GAGAPPPFQH PHCDRAAMYA QPVRKMSTKG GSYDYDLIVI 130 140 150 160 170 180 GGGSAGLACA KEAVLNGARV ACLDFVKPTP TLGTKWGVGG TCVNVGCIPK KLMHQASLLG 190 200 210 220 230 240 EAVHEAAAYG WNVDEKIKPD WHKLVQSVQN HIKSVNWVTR VDLRDKKVEY INGLGSFVDS 250 260 270 280 290 300 HTLLAKLKSG ERTITAQTFV IAVGGRPRYP DIPGAVEYGI TSDDLFSLDR EPGKTLVVGA 310 320 330 340 350 360 GYIGLECAGF LKGLGYEPTV MVRSIVLRGF DQQMAELVAA SMEERGIPFL RKTVPLSVEK 370 380 390 400 410 420 QDDGKLLVKY KNVETGEEAE DVYDTVLWAI GRKGLVDDLN LPNAGVTVQK DKIPVDSQEA 430 440 450 460 470 480 TNVANIYAVG DIIYGKPELT PVAVLAGRLL ARRLYGGSTQ RMDYKDVATT VFTPLEYACV 490 500 510 520 530 540 GLSEEDAVKQ FGADEIEVFH GYYKPTEFFI PQKSVRYCYL KAVAERHGDQ RVYGLHYIGP 550 560 570 580 590 VAGEVIQGFA AALKSGLTIN TLINTVGIHP TTAEEFTRLA ITKRSGLDPT PASCCS
	Isoform A (Cyto) [UniParc]. Checksum: E40B8AA667768E87	FASTA	491	53,223
	10 20 30 40 50 60 MAPVQGSYDY DLIVIGGGSA GLACAKEAVL NGARVACLDF VKPTPTLGTK WGVGGTCVNV 70 80 90 100 110 120 GCIPKKLMHQ ASLLGEAVHE AAAYGWNVDE KIKPDWHKLV QSVQNHIKSV NWVTRVDLRD 130 140 150 160 170 180 KKVEYINGLG SFVDSHTLLA KLKSGERTIT AQTFVIAVGG RPRYPDIPGA VEYGITSDDL 190 200 210 220 230 240 FSLDREPGKT LVVGAGYIGL ECAGFLKGLG YEPTVMVRSI VLRGFDQQMA ELVAASMEER 250 260 270 280 290 300 GIPFLRKTVP LSVEKQDDGK LLVKYKNVET GEEAEDVYDT VLWAIGRKGL VDDLNLPNAG 310 320 330 340 350 360 VTVQKDKIPV DSQEATNVAN IYAVGDIIYG KPELTPVAVL AGRLLARRLY GGSTQRMDYK 370 380 390 400 410 420 DVATTVFTPL EYACVGLSEE DAVKQFGADE IEVFHGYYKP TEFFIPQKSV RYCYLKAVAE 430 440 450 460 470 480 RHGDQRVYGL HYIGPVAGEV IQGFAAALKS GLTINTLINT VGIHPTTAEE FTRLAITKRS 490 GLDPTPASCC S
	Isoform C [UniParc]. Checksum: F34F360FD31FA197	FASTA	508	55,114
	10 20 30 40 50 60 MLKYMICAIV VGAKKSTSSK YNGSYDYDLI VIGGGSAGLA CAKEAVLNGA RVACLDFVKP 70 80 90 100 110 120 TPTLGTKWGV GGTCVNVGCI PKKLMHQASL LGEAVHEAAA YGWNVDEKIK PDWHKLVQSV 130 140 150 160 170 180 QNHIKSVNWV TRVDLRDKKV EYINGLGSFV DSHTLLAKLK SGERTITAQT FVIAVGGRPR 190 200 210 220 230 240 YPDIPGAVEY GITSDDLFSL DREPGKTLVV GAGYIGLECA GFLKGLGYEP TVMVRSIVLR 250 260 270 280 290 300 GFDQQMAELV AASMEERGIP FLRKTVPLSV EKQDDGKLLV KYKNVETGEE AEDVYDTVLW 310 320 330 340 350 360 AIGRKGLVDD LNLPNAGVTV QKDKIPVDSQ EATNVANIYA VGDIIYGKPE LTPVAVLAGR 370 380 390 400 410 420 LLARRLYGGS TQRMDYKDVA TTVFTPLEYA CVGLSEEDAV KQFGADEIEV FHGYYKPTEF 430 440 450 460 470 480 FIPQKSVRYC YLKAVAERHG DQRVYGLHYI GPVAGEVIQG FAAALKSGLT INTLINTVGI 490 500 HPTTAEEFTR LAITKRSGLD PTPASCCS
	Isoform D [UniParc]. Checksum: 567BE40B2DA226DF	FASTA	491	53,201
	10 20 30 40 50 60 MSTKGGSYDY DLIVIGGGSA GLACAKEAVL NGARVACLDF VKPTPTLGTK WGVGGTCVNV 70 80 90 100 110 120 GCIPKKLMHQ ASLLGEAVHE AAAYGWNVDE KIKPDWHKLV QSVQNHIKSV NWVTRVDLRD 130 140 150 160 170 180 KKVEYINGLG SFVDSHTLLA KLKSGERTIT AQTFVIAVGG RPRYPDIPGA VEYGITSDDL 190 200 210 220 230 240 FSLDREPGKT LVVGAGYIGL ECAGFLKGLG YEPTVMVRSI VLRGFDQQMA ELVAASMEER 250 260 270 280 290 300 GIPFLRKTVP LSVEKQDDGK LLVKYKNVET GEEAEDVYDT VLWAIGRKGL VDDLNLPNAG 310 320 330 340 350 360 VTVQKDKIPV DSQEATNVAN IYAVGDIIYG KPELTPVAVL AGRLLARRLY GGSTQRMDYK 370 380 390 400 410 420 DVATTVFTPL EYACVGLSEE DAVKQFGADE IEVFHGYYKP TEFFIPQKSV RYCYLKAVAE 430 440 450 460 470 480 RHGDQRVYGL HYIGPVAGEV IQGFAAALKS GLTINTLINT VGIHPTTAEE FTRLAITKRS 490 GLDPTPASCC S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular organization of the glutathione reductase gene in Drosophila melanogaster." Candas M., Sohal R.S., Radyuk S.N., Klichko V.I., Orr W.C. Arch. Biochem. Biophys. 339:323-334(1997) [PubMed: 9056265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]	"Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster." Kanzok S.M., Fechner A., Bauer H., Ulschmid J.K., Muller H.M., Botella-Munoz J., Schneuwly S., Schirmer R., Becker K. Science 291:643-646(2001) [PubMed: 11158675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND D), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-594 AND CYS-595.
[3]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C). Strain: Berkeley.
[6]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-447 (ISOFORM B). Strain: Berkeley. Tissue: Ovary.
[7]	"Cooperative action of antioxidant defense systems in Drosophila." Missirlis F., Phillips J.P., Jackle H. Curr. Biol. 11:1272-1277(2001) [PubMed: 11525742] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]	"Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium." Gromer S., Gross J.H. J. Biol. Chem. 277:9701-9706(2002) [PubMed: 11782468] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability." Missirlis F., Ulschmid J.K., Hirosawa-Takamori M., Groenke S., Schaefer U., Becker K., Phillips J.P., Jaeckle H. J. Biol. Chem. 277:11521-11526(2002) [PubMed: 11796729] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[10]	"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." Bauer H., Kanzok S.M., Schirmer R.H. J. Biol. Chem. 277:17457-17463(2002) [PubMed: 11877442] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[11]	"Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster." Huang H.H., Arscott L.D., Ballou D.P., Williams C.H. Jr. Biochemistry 47:1721-1731(2008) [PubMed: 18211101] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-569.
[12]	"Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster." Huang H.H., Arscott L.D., Ballou D.P., Williams C.H. Biochemistry 47:12769-12776(2008) [PubMed: 18991392] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-574.
[13]	"Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases." Eckenroth B.E., Rould M.A., Hondal R.J., Everse S.J. Biochemistry 46:4694-4705(2007) [PubMed: 17385893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 111-593 IN COMPLEX WITH FAD AND NADP, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U81995 mRNA. Translation: AAB48441.1.
AF301145 mRNA. Translation: AAG25640.1.
AF301144 mRNA. Translation: AAG25639.1.
AE014298 Genomic DNA. Translation: AAF46354.1.
AE014298 Genomic DNA. Translation: AAF46355.2.
AE014298 Genomic DNA. Translation: AAN09228.1.
BT003266 mRNA. Translation: AAO25023.1.
BT025070 mRNA. Translation: ABE73241.1.
AY051643 mRNA. Translation: AAK93067.1. Sequence problems.

RefSeq

NP_511082.2. NM_078527.2.
NP_727251.1. NM_167149.1.
NP_727252.1. NM_167150.1.

UniGene

Dm.20991.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NVK	X-ray	2.40	X	111-593	[»]
3DGH	X-ray	1.75	A/B	111-588	[»]
3DH9	X-ray	2.25	A/B	111-591	[»]

ProteinModelPortal

P91938.

SMR

P91938. Positions 111-591.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-19145N.

IntAct

P91938. 6 interactions.

MINT

MINT-916376.

STRING

P91938.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0071168; FBpp0071116; FBgn0020653.

GeneID

31760.

KEGG

dme:Dmel_CG2151.

Organism-specific databases

CTD

31760.

FlyBase

FBgn0020653. Trxr-1.

Phylogenomic databases

eggNOG

inNOG05949.

GeneTree

EMGT00050000007101.

InParanoid

P91938.

OMA

FSPLEYG.

OrthoDB

EOG48932M.

PhylomeDB

P91938.

Enzyme and pathway databases

BRENDA

1.8.1.9. 1994.

Gene expression databases

Bgee

P91938.

GermOnline

CG2151. Drosophila melanogaster.

Family and domain databases

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

KO

K00384.

PANTHER

PTHR22912:SF23. Reduct_Se. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

TIGRFAMs

TIGR01438. TGR. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

775165.

Entry information

Entry name

TRXR1_DROME

Accession

Primary (citable) accession number: P91938
Secondary accession number(s): Q1RKZ0 , Q53YG2, Q961E3, Q9W3H2, Q9W3H3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 27, 2003
Last modified:	January 25, 2012
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project