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Protein

Thioredoxin reductase 1, mitochondrial

Gene

Trxr-1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.1 Publication

Cofactori

FADNote: Binds 1 FAD per subunit.

Kineticsi

Measurements were conducted with isoform A unless noted otherwise.

  1. KM=6.5 µM for NADPH (at pH 7.4)7 Publications
  2. KM=1 µM for NADPH (at pH 7.4, 2 mM EDTA, 100 mM KPO4)7 Publications
  3. KM=1 µM for NADPH (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO4)7 Publications
  4. KM=7.0 µM for dhd (at pH 7.4, 200 µM NADPH, 100 mM KPO4)7 Publications
  5. 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)7 Publications
  6. KM=7 µM for dhd (at pH 7.4, 2 mM EDTA, 100 mM KPO4)7 Publications
  7. KM=19 µM for dhd (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO4)7 Publications
  8. KM=5.9 µM for Trx-2 (at pH 7.4, 100 µM NADPH, 2 mM EDTA, 100 mM KPO4)7 Publications
  9. KM=310 µM for 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) (at pH 7.4, 100 µM NADPH, 100 mM KPO4)7 Publications
  10. KM=0.17 mM for DTNB (at pH 7.0, 0.2 mM NADPH, 10 mM EDTA, 100 mM KPO4, 25 degrees Celsius)7 Publications
  11. KM=380 µM for DTNB (at pH 7.4, 2 mM EDTA, 100 mM KPO4)7 Publications
  12. KM=410 µM for DTNB (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO4)7 Publications
  13. KM=675 µM for methylseleninate (100 µM NADPH)7 Publications
  1. Vmax=24.3 µmol/min/mg enzyme toward NADPH (at pH 7.4)7 Publications
  2. 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)7 Publications

pH dependencei

Optimum pH is 7.6 for isoform A with Trx-2 and NADPH as substrates.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei282 – 2821FAD1 Publication
Binding sitei286 – 2861FAD1 Publication
Binding sitei302 – 3021FAD1 Publication
Binding sitei355 – 3551NADP1 Publication
Binding sitei472 – 4721FAD1 Publication
Active sitei569 – 5691Proton acceptor1 Publication
Binding sitei570 – 5701FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 1267FAD1 Publication
Nucleotide bindingi143 – 1475FAD1 Publication
Nucleotide bindingi159 – 17012FAD1 PublicationAdd
BLAST
Nucleotide bindingi233 – 2353FAD1 Publication
Nucleotide bindingi262 – 2665FAD1 Publication
Nucleotide bindingi322 – 3287NADP1 Publication
Nucleotide bindingi392 – 3998FAD1 Publication
Nucleotide bindingi429 – 4324FAD1 Publication
Nucleotide bindingi438 – 4436FAD1 Publication

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB
  • flavin adenine dinucleotide binding Source: InterPro
  • glutathione-disulfide reductase activity Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

  • cell redox homeostasis Source: UniProtKB
  • cellular oxidant detoxification Source: GOC
  • cellular response to DNA damage stimulus Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • neurogenesis Source: FlyBase
  • response to hypoxia Source: FlyBase
  • sensory perception of pain Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.8.1.9. 1994.
ReactomeiR-DME-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 1, mitochondrial (EC:1.8.1.9)
Short name:
TrxR-1
Gene namesi
Name:Trxr-1
Synonyms:GR
ORF Names:CG2151
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0020653. Trxr-1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi569 – 5691H → Q: Almost complete loss of TrX reduction. 1 Publication
Mutagenesisi574 – 5741E → A: Reduced Trx reduction. 1 Publication
Mutagenesisi574 – 5741E → Q: Reduced Trx reduction. 1 Publication
Mutagenesisi594 – 5941C → S: Loss of Trx reduction. 1 Publication
Mutagenesisi595 – 5951C → S: Loss of Trx reduction. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 596Thioredoxin reductase 1, mitochondrialPRO_0000030291
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi162 ↔ 167Redox-active1 Publication
Disulfide bondi594 ↔ 595Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP91938.

Expressioni

Tissue specificityi

During embryogenesis, expression is seen in germ cell progenitors, developing midgut, hindgut and proventriculus.1 Publication

Developmental stagei

Expressed both maternally and zygotically during all stages of development, highest expression during adult stages.2 Publications

Gene expression databases

BgeeiP91938.
GenevisibleiP91938. DM.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi58221. 32 interactions.
DIPiDIP-19145N.
IntActiP91938. 12 interactions.
MINTiMINT-916376.
STRINGi7227.FBpp0071116.

Structurei

Secondary structure

1
596
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi114 – 1207Combined sources
Helixi124 – 13512Combined sources
Beta strandi140 – 1434Combined sources
Turni150 – 1523Combined sources
Helixi161 – 1655Combined sources
Helixi167 – 18822Combined sources
Helixi201 – 22525Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi233 – 2397Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi252 – 26110Combined sources
Beta strandi265 – 2673Combined sources
Helixi275 – 2784Combined sources
Helixi282 – 2854Combined sources
Beta strandi294 – 2985Combined sources
Helixi302 – 31312Combined sources
Beta strandi317 – 3248Combined sources
Helixi332 – 34413Combined sources
Beta strandi349 – 3513Combined sources
Beta strandi353 – 3608Combined sources
Beta strandi366 – 3727Combined sources
Turni373 – 3753Combined sources
Beta strandi378 – 38811Combined sources
Beta strandi392 – 3943Combined sources
Helixi397 – 3993Combined sources
Helixi401 – 4033Combined sources
Beta strandi409 – 4135Combined sources
Beta strandi426 – 4283Combined sources
Helixi430 – 4323Combined sources
Helixi440 – 45516Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi473 – 4819Combined sources
Helixi484 – 4918Combined sources
Helixi493 – 4953Combined sources
Beta strandi496 – 5027Combined sources
Helixi506 – 5083Combined sources
Turni509 – 5124Combined sources
Beta strandi519 – 5279Combined sources
Beta strandi531 – 5399Combined sources
Helixi542 – 55413Combined sources
Helixi559 – 5635Combined sources
Helixi573 – 5786Combined sources
Turni583 – 5853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NVKX-ray2.40X111-593[»]
3DGHX-ray1.75A/B111-588[»]
3DH9X-ray2.25A/B111-591[»]
ProteinModelPortaliP91938.
SMRiP91938. Positions 111-591.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP91938.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
InParanoidiP91938.
KOiK00384.
OMAiEIEVFHG.
OrthoDBiEOG779NXG.
PhylomeDBiP91938.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform B (identifier: P91938-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNLCNSRFSV TFVRQCSTIL TSPSAGIIQN RGSLTTKVPH WISSSLSCAH
60 70 80 90 100
HTFQRTMNLT GQRGSRDSTG ATGGNAPAGS GAGAPPPFQH PHCDRAAMYA
110 120 130 140 150
QPVRKMSTKG GSYDYDLIVI GGGSAGLACA KEAVLNGARV ACLDFVKPTP
160 170 180 190 200
TLGTKWGVGG TCVNVGCIPK KLMHQASLLG EAVHEAAAYG WNVDEKIKPD
210 220 230 240 250
WHKLVQSVQN HIKSVNWVTR VDLRDKKVEY INGLGSFVDS HTLLAKLKSG
260 270 280 290 300
ERTITAQTFV IAVGGRPRYP DIPGAVEYGI TSDDLFSLDR EPGKTLVVGA
310 320 330 340 350
GYIGLECAGF LKGLGYEPTV MVRSIVLRGF DQQMAELVAA SMEERGIPFL
360 370 380 390 400
RKTVPLSVEK QDDGKLLVKY KNVETGEEAE DVYDTVLWAI GRKGLVDDLN
410 420 430 440 450
LPNAGVTVQK DKIPVDSQEA TNVANIYAVG DIIYGKPELT PVAVLAGRLL
460 470 480 490 500
ARRLYGGSTQ RMDYKDVATT VFTPLEYACV GLSEEDAVKQ FGADEIEVFH
510 520 530 540 550
GYYKPTEFFI PQKSVRYCYL KAVAERHGDQ RVYGLHYIGP VAGEVIQGFA
560 570 580 590
AALKSGLTIN TLINTVGIHP TTAEEFTRLA ITKRSGLDPT PASCCS
Note: Can partially substitute for the cytoplasmic enzyme activity.
Length:596
Mass (Da):64,322
Last modified:January 27, 2003 - v2
Checksum:i8DA6FC08CF6A7292
GO
Isoform A (identifier: P91938-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:491
Mass (Da):53,223
Checksum:iE40B8AA667768E87
GO
Isoform C (identifier: P91938-3) [UniParc]FASTAAdd to basket

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

Show »
Length:508
Mass (Da):55,114
Checksum:iF34F360FD31FA197
GO
Isoform D (identifier: P91938-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:491
Mass (Da):53,201
Checksum:i567BE40B2DA226DF
GO

Sequence cautioni

The sequence AAK93067.1 differs from that shown.Chimeric cDNA. Chimeric cDNA originating from chromosomes X and 3.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881F → L in AAK93067 (PubMed:12537569).Curated
Sequence conflicti134 – 1341V → S in AAB48441 (PubMed:9056265).Curated
Sequence conflicti151 – 1511Missing in AAB48441 (PubMed:9056265).Curated
Sequence conflicti189 – 1902Missing in AAB48441 (PubMed:9056265).Curated
Sequence conflicti195 – 1951E → D in AAB48441 (PubMed:9056265).Curated
Sequence conflicti195 – 1951E → D in AAK93067 (PubMed:12537569).Curated
Sequence conflicti203 – 2075KLVQS → RLCAV in AAB48441 (PubMed:9056265).Curated
Sequence conflicti213 – 2164KSVN → SRH in AAB48441 (PubMed:9056265).Curated
Sequence conflicti220 – 2201R → V in AAB48441 (PubMed:9056265).Curated
Sequence conflicti239 – 2479DSHTLLAKL → TRTHCCPSM in AAB48441 (PubMed:9056265).Curated
Sequence conflicti264 – 2641Missing in AAB48441 (PubMed:9056265).Curated
Sequence conflicti276 – 2805VEYGI → AEIGT in AAB48441 (PubMed:9056265).Curated
Sequence conflicti292 – 2921Missing in AAB48441 (PubMed:9056265).Curated
Sequence conflicti317 – 3182EP → G in AAB48441 (PubMed:9056265).Curated
Sequence conflicti351 – 38636RKTVP…VYDTV → ADVDRCREADDAAAREYRLT QIRFTTSHHR in AAB48441 (PubMed:9056265).CuratedAdd
BLAST
Sequence conflicti379 – 3791A → S in AAK93067 (PubMed:12537569).Curated
Sequence conflicti396 – 3983VDD → CDS in AAB48441 (PubMed:9056265).Curated
Sequence conflicti403 – 4064NAGV → MPAL in AAB48441 (PubMed:9056265).Curated
Sequence conflicti424 – 4252AN → PH in AAB48441 (PubMed:9056265).Curated
Sequence conflicti455 – 4551Y → F in AAB48441 (PubMed:9056265).Curated
Sequence conflicti461 – 4611R → S in AAB48441 (PubMed:9056265).Curated
Sequence conflicti473 – 48311TPLEYACVGLS → SWSTSASGLA in AAB48441 (PubMed:9056265).CuratedAdd
BLAST
Sequence conflicti488 – 4958VKQFGADE → SSSSEPR in AAB48441 (PubMed:9056265).Curated
Sequence conflicti559 – 5602IN → L in AAB48441 (PubMed:9056265).Curated
Sequence conflicti583 – 5831K → KP in AAB48441 (PubMed:9056265).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 105105Missing in isoform A and isoform D. 3 PublicationsVSP_005572Add
BLAST
Alternative sequencei1 – 8888Missing in isoform C. 1 PublicationVSP_005571Add
BLAST
Alternative sequencei89 – 11022QHPHC…MSTKG → MLKYMICAIVVGAKKSTSSK YN in isoform C. 1 PublicationVSP_005573Add
BLAST
Alternative sequencei106 – 1105MSTKG → MAPVQ in isoform A. 3 PublicationsVSP_005574

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_511082.2. NM_078527.3. [P91938-2]
NP_727251.1. NM_167149.2. [P91938-1]
NP_727252.1. NM_167150.2. [P91938-3]
UniGeneiDm.20991.

Genome annotation databases

EnsemblMetazoaiFBtr0071168; FBpp0071116; FBgn0020653. [P91938-1]
GeneIDi31760.
KEGGidme:Dmel_CG2151.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_511082.2. NM_078527.3. [P91938-2]
NP_727251.1. NM_167149.2. [P91938-1]
NP_727252.1. NM_167150.2. [P91938-3]
UniGeneiDm.20991.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NVKX-ray2.40X111-593[»]
3DGHX-ray1.75A/B111-588[»]
3DH9X-ray2.25A/B111-591[»]
ProteinModelPortaliP91938.
SMRiP91938. Positions 111-591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58221. 32 interactions.
DIPiDIP-19145N.
IntActiP91938. 12 interactions.
MINTiMINT-916376.
STRINGi7227.FBpp0071116.

Proteomic databases

PaxDbiP91938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071168; FBpp0071116; FBgn0020653. [P91938-1]
GeneIDi31760.
KEGGidme:Dmel_CG2151.

Organism-specific databases

CTDi31760.
FlyBaseiFBgn0020653. Trxr-1.

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
InParanoidiP91938.
KOiK00384.
OMAiEIEVFHG.
OrthoDBiEOG779NXG.
PhylomeDBiP91938.

Enzyme and pathway databases

BRENDAi1.8.1.9. 1994.
ReactomeiR-DME-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiTrxr-1. fly.
EvolutionaryTraceiP91938.
GenomeRNAii31760.
PROiP91938.

Gene expression databases

BgeeiP91938.
GenevisibleiP91938. DM.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Entry informationi

Entry nameiTRXR1_DROME
AccessioniPrimary (citable) accession number: P91938
Secondary accession number(s): Q1RKZ0
, Q53YG2, Q961E3, Q9W3H2, Q9W3H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 27, 2003
Last modified: June 8, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Caution

Was originally thought to be a glutathione reductase.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.