ID TRXR2_DROME Reviewed; 516 AA.
AC Q9VNT5;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Thioredoxin reductase 2, mitochondrial {ECO:0000312|FlyBase:FBgn0037170};
DE EC=1.8.1.9;
DE Flags: Precursor;
GN Name=Trxr2 {ECO:0000312|FlyBase:FBgn0037170};
GN Synonyms=Trxr-2 {ECO:0000312|FlyBase:FBgn0037170};
GN ORFNames=CG11401 {ECO:0000312|FlyBase:FBgn0037170};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF64152.1};
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF64152.1}
RP NUCLEOTIDE SEQUENCE.
RA Kanzok S., Becker K., Schirmer R.H.;
RT "Drosophila melanogaster thioredoxin reductase 2.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Thioredoxin system is a major player in glutathione
CC metabolism, due to the demonstrated absence of a glutathione reductase.
CC Functionally interacts with the Sod/Cat reactive oxidation species
CC (ROS) defense system and thereby has a role in preadult development and
CC life span. Lack of a glutathione reductase suggests antioxidant defense
CC in Drosophila, and probably in related insects, differs fundamentally
CC from that in other organisms. {ECO:0000250|UniProtKB:P91938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000250|UniProtKB:P91938};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P91938}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF236866; AAF64152.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51835.1; -; Genomic_DNA.
DR EMBL; AY121613; AAM51940.1; -; mRNA.
DR RefSeq; NP_524216.1; NM_079492.3.
DR AlphaFoldDB; Q9VNT5; -.
DR SMR; Q9VNT5; -.
DR BioGRID; 65709; 2.
DR DIP; DIP-19796N; -.
DR IntAct; Q9VNT5; 1.
DR STRING; 7227.FBpp0078166; -.
DR PaxDb; 7227-FBpp0078166; -.
DR DNASU; 40475; -.
DR EnsemblMetazoa; FBtr0078514; FBpp0078166; FBgn0037170.
DR GeneID; 40475; -.
DR KEGG; dme:Dmel_CG11401; -.
DR AGR; FB:FBgn0037170; -.
DR CTD; 40475; -.
DR FlyBase; FBgn0037170; Trxr2.
DR VEuPathDB; VectorBase:FBgn0037170; -.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000167606; -.
DR HOGENOM; CLU_016755_2_4_1; -.
DR InParanoid; Q9VNT5; -.
DR OMA; CFDYVKP; -.
DR OrthoDB; 5473641at2759; -.
DR PhylomeDB; Q9VNT5; -.
DR Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DME-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-DME-5263617; Metabolism of ingested MeSeO2H into MeSeH.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR BioGRID-ORCS; 40475; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Trxr-2; fly.
DR GenomeRNAi; 40475; -.
DR PRO; PR:Q9VNT5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0037170; Expressed in testis and 6 other cell types or tissues.
DR Genevisible; Q9VNT5; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISM:FlyBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IDA:FlyBase.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:FlyBase.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF6; THIOREDOXIN REDUCTASE 2; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..516
FT /note="Thioredoxin reductase 2, mitochondrial"
FT /id="PRO_0000030293"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 62..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 79..84
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 56277 MW; D82A89CBF6A4B7E8 CRC64;
MSTIKFLRSS THNALRSSLG WCRLAASRPR YDYDLVVLGG GSAGLACAKE AAGCGARVLC
FDYVKPTPVG TKWGIGGTCV NVGCIPKKLM HQASLLGEAV HEAVAYGWNV DDTNIRPDWR
KLVRSVQNHI KSVNWVTRVD LRDKKVEYVN SMATFRDSHT IEYVAMPGAE HRQVTSEYVV
VAVGGRPRYP DIPGAVELGI TSDDIFSYER EPGRTLVVGA GYVGLECACF LKGLGYEPTV
MVRSIVLRGF DRQMSELLAA MMTERGIPFL GTTIPKAVER QADGRLLVRY RNTTTQMDGS
DVFDTVLWAI GRKGLIEDLN LDAAGVKTHD DKIVVDAAEA TSVPHIFAVG DIIYGRPELT
PVAILSGRLL ARRLFAGSTQ LMDYADVATT VFTPLEYSCV GMSEETAIEL RGADNIEVFH
GYYKPTEFFI PQKSVRHCYL KAVAEVSGDQ KILGLHYIGP VAGEVIQGFA AALKTGLTVK
TLLNTVGIHP TTAEEFTRLS ITKRSGRDPT PASCCS
//
