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Protein

Thioredoxin reductase 2, mitochondrial

Gene

Trxr-2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.By similarity

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei489 – 4891Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 7918FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiR-DME-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 2, mitochondrial (EC:1.8.1.9)
Short name:
TrxR-2
Gene namesi
Name:Trxr-2
ORF Names:CG11401
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0037170. Trxr-2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 516Thioredoxin reductase 2, mitochondrialPRO_0000030293
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi79 ↔ 84Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9VNT5.
PRIDEiQ9VNT5.

Expressioni

Gene expression databases

BgeeiQ9VNT5.
GenevisibleiQ9VNT5. DM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi65709. 2 interactions.
DIPiDIP-19796N.
IntActiQ9VNT5. 1 interaction.
MINTiMINT-790959.
STRINGi7227.FBpp0078166.

Structurei

3D structure databases

ProteinModelPortaliQ9VNT5.
SMRiQ9VNT5. Positions 31-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
InParanoidiQ9VNT5.
KOiK00384.
OMAiHFRTRAR.
OrthoDBiEOG779NXG.
PhylomeDBiQ9VNT5.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 3 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]

Sequencei

Sequence statusi: Complete.

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

Q9VNT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTIKFLRSS THNALRSSLG WCRLAASRPR YDYDLVVLGG GSAGLACAKE
60 70 80 90 100
AAGCGARVLC FDYVKPTPVG TKWGIGGTCV NVGCIPKKLM HQASLLGEAV
110 120 130 140 150
HEAVAYGWNV DDTNIRPDWR KLVRSVQNHI KSVNWVTRVD LRDKKVEYVN
160 170 180 190 200
SMATFRDSHT IEYVAMPGAE HRQVTSEYVV VAVGGRPRYP DIPGAVELGI
210 220 230 240 250
TSDDIFSYER EPGRTLVVGA GYVGLECACF LKGLGYEPTV MVRSIVLRGF
260 270 280 290 300
DRQMSELLAA MMTERGIPFL GTTIPKAVER QADGRLLVRY RNTTTQMDGS
310 320 330 340 350
DVFDTVLWAI GRKGLIEDLN LDAAGVKTHD DKIVVDAAEA TSVPHIFAVG
360 370 380 390 400
DIIYGRPELT PVAILSGRLL ARRLFAGSTQ LMDYADVATT VFTPLEYSCV
410 420 430 440 450
GMSEETAIEL RGADNIEVFH GYYKPTEFFI PQKSVRHCYL KAVAEVSGDQ
460 470 480 490 500
KILGLHYIGP VAGEVIQGFA AALKTGLTVK TLLNTVGIHP TTAEEFTRLS
510
ITKRSGRDPT PASCCS
Length:516
Mass (Da):56,277
Last modified:May 1, 2000 - v1
Checksum:iD82A89CBF6A4B7E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236866 Genomic DNA. Translation: AAF64152.1.
AE014296 Genomic DNA. Translation: AAF51835.1.
AY121613 mRNA. Translation: AAM51940.1.
RefSeqiNP_524216.1. NM_079492.3.
UniGeneiDm.2498.

Genome annotation databases

EnsemblMetazoaiFBtr0078514; FBpp0078166; FBgn0037170.
GeneIDi40475.
KEGGidme:Dmel_CG11401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236866 Genomic DNA. Translation: AAF64152.1.
AE014296 Genomic DNA. Translation: AAF51835.1.
AY121613 mRNA. Translation: AAM51940.1.
RefSeqiNP_524216.1. NM_079492.3.
UniGeneiDm.2498.

3D structure databases

ProteinModelPortaliQ9VNT5.
SMRiQ9VNT5. Positions 31-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65709. 2 interactions.
DIPiDIP-19796N.
IntActiQ9VNT5. 1 interaction.
MINTiMINT-790959.
STRINGi7227.FBpp0078166.

Proteomic databases

PaxDbiQ9VNT5.
PRIDEiQ9VNT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078514; FBpp0078166; FBgn0037170.
GeneIDi40475.
KEGGidme:Dmel_CG11401.

Organism-specific databases

CTDi40475.
FlyBaseiFBgn0037170. Trxr-2.

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
InParanoidiQ9VNT5.
KOiK00384.
OMAiHFRTRAR.
OrthoDBiEOG779NXG.
PhylomeDBiQ9VNT5.

Enzyme and pathway databases

ReactomeiR-DME-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiTrxr-2. fly.
GenomeRNAii40475.
PROiQ9VNT5.

Gene expression databases

BgeeiQ9VNT5.
GenevisibleiQ9VNT5. DM.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 3 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. "Drosophila melanogaster thioredoxin reductase 2."
    Kanzok S., Becker K., Schirmer R.H.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Testis.

Entry informationi

Entry nameiTRXR2_DROME
AccessioniPrimary (citable) accession number: Q9VNT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 130 of the entry and version 1 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.