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Thioredoxin reductase 1, mitochondrial (TrxR-1) (EC 1.8.1.9)

 TRXR1_DROME             Reviewed;         596 AA.
P91938; Q1RKZ0; Q53YG2; Q961E3; Q9W3H2; Q9W3H3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JAN-2003, sequence version 2.
30-AUG-2017, entry version 177.
RecName: Full=Thioredoxin reductase 1, mitochondrial;
Short=TrxR-1;
EC=1.8.1.9;
Flags: Precursor;
Name=Trxr-1; Synonyms=GR; ORFNames=CG2151;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=9056265; DOI=10.1006/abbi.1996.9872;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND D), FUNCTION, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-594
AND CYS-595.
PubMed=11158675; DOI=10.1126/science.291.5504.643;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
STRAIN=Berkeley;
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-447 (ISOFORM B).
STRAIN=Berkeley; TISSUE=Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11525742; DOI=10.1016/S0960-9822(01)00393-1;
Missirlis F., Phillips J.P., Jackle H.;
"Cooperative action of antioxidant defense systems in Drosophila.";
Curr. Biol. 11:1272-1277(2001).
[8]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11782468; DOI=10.1074/jbc.M109234200;
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).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=11796729; DOI=10.1074/jbc.M111692200;
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).
[10]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11877442; DOI=10.1074/jbc.M200636200;
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).
[11]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-569.
PubMed=18211101; DOI=10.1021/bi702040u;
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).
[12]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-574.
PubMed=18991392; DOI=10.1021/bi801449h;
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).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 111-593 IN COMPLEX WITH FAD
AND NADP, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND
DISULFIDE BOND.
PubMed=17385893; DOI=10.1021/bi602394p;
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).
-!- 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. {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11525742, ECO:0000269|PubMed:11796729}.
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH. {ECO:0000269|PubMed:11158675}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.5 uM for NADPH (at pH 7.4) {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
KM=1 uM for NADPH (at pH 7.4, 2 mM EDTA, 100 mM KPO(4))
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
KM=1 uM for NADPH (isoform B at pH 7.4, 2 mM EDTA, 100 mM
KPO(4)) {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
KM=7.0 uM for dhd (at pH 7.4, 200 uM NADPH, 100 mM KPO(4))
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
KM=141 uM for dhd (at pH 7.0, 0.15 mM NADPH, 1 mM EDTA, 1 mg/ml
insulin, 50 mM KPO(4), 25 degrees Celsius)
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
KM=7 uM for dhd (at pH 7.4, 2 mM EDTA, 100 mM KPO(4))
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
KM=19 uM for dhd (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO(4))
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
KM=5.9 uM for Trx-2 (at pH 7.4, 100 uM NADPH, 2 mM EDTA, 100 mM
KPO(4)) {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
KM=310 uM for 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) (at pH
7.4, 100 uM NADPH, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
KM=0.17 mM for DTNB (at pH 7.0, 0.2 mM NADPH, 10 mM EDTA, 100 mM
KPO(4), 25 degrees Celsius) {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
KM=380 uM for DTNB (at pH 7.4, 2 mM EDTA, 100 mM KPO(4))
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
KM=410 uM for DTNB (isoform B at pH 7.4, 2 mM EDTA, 100 mM
KPO(4)) {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
KM=675 uM for methylseleninate (100 uM NADPH)
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
Vmax=24.3 umol/min/mg enzyme toward NADPH (at pH 7.4)
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
Vmax=16 umol/min/mg enzyme toward Trx-2 (at pH 7.4, 100 uM
NADPH, 2 mM EDTA, 100 mM KPO(4), 25 degrees Celsius)
{ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468,
ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442,
ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101,
ECO:0000269|PubMed:18991392};
Note=Measurements were conducted with isoform A unless noted
otherwise.;
pH dependence:
Optimum pH is 7.6 for isoform A with Trx-2 and NADPH as
substrates. {ECO:0000269|PubMed:11158675,
ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729,
ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893,
ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17385893}.
-!- SUBCELLULAR LOCATION: Isoform B: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform A: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=B; Synonyms=Mito;
IsoId=P91938-1; Sequence=Displayed;
Note=Can partially substitute for the cytoplasmic enzyme
activity.;
Name=A; Synonyms=Cyto;
IsoId=P91938-2; Sequence=VSP_005572, VSP_005574;
Note=Unable to compensate for the loss of the mitochondrial
enzyme activity.;
Name=C;
IsoId=P91938-3; Sequence=VSP_005571, VSP_005573;
Name=D;
IsoId=P91938-4; Sequence=VSP_005572;
Note=Produced by alternative initiation at Met-106 of isoform
B.;
-!- TISSUE SPECIFICITY: During embryogenesis, expression is seen in
germ cell progenitors, developing midgut, hindgut and
proventriculus. {ECO:0000269|PubMed:11525742}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
during all stages of development, highest expression during adult
stages. {ECO:0000269|PubMed:11525742,
ECO:0000269|PubMed:11796729}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be a glutathione reductase.
{ECO:0000305|PubMed:9056265}.
-!- SEQUENCE CAUTION:
Sequence=AAK93067.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Chimeric cDNA originating from chromosomes X and 3.; Evidence={ECO:0000305};
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EMBL; U81995; AAB48441.1; -; mRNA.
EMBL; AF301145; AAG25640.1; -; mRNA.
EMBL; AF301144; AAG25639.1; -; mRNA.
EMBL; AE014298; AAF46354.1; -; Genomic_DNA.
EMBL; AE014298; AAF46355.2; -; Genomic_DNA.
EMBL; AE014298; AAN09228.1; -; Genomic_DNA.
EMBL; BT003266; AAO25023.1; -; mRNA.
EMBL; BT025070; ABE73241.1; -; mRNA.
EMBL; AY051643; AAK93067.1; ALT_SEQ; mRNA.
RefSeq; NP_511082.2; NM_078527.3. [P91938-2]
RefSeq; NP_727251.1; NM_167149.2. [P91938-1]
RefSeq; NP_727252.1; NM_167150.2. [P91938-3]
UniGene; Dm.20991; -.
PDB; 2NVK; X-ray; 2.40 A; X=111-593.
PDB; 3DGH; X-ray; 1.75 A; A/B=111-588.
PDB; 3DH9; X-ray; 2.25 A; A/B=111-591.
PDBsum; 2NVK; -.
PDBsum; 3DGH; -.
PDBsum; 3DH9; -.
ProteinModelPortal; P91938; -.
SMR; P91938; -.
BioGrid; 58221; 32.
DIP; DIP-19145N; -.
IntAct; P91938; 12.
MINT; MINT-916376; -.
STRING; 7227.FBpp0071116; -.
PaxDb; P91938; -.
PRIDE; P91938; -.
EnsemblMetazoa; FBtr0071167; FBpp0071115; FBgn0020653. [P91938-2]
EnsemblMetazoa; FBtr0071168; FBpp0071116; FBgn0020653. [P91938-1]
EnsemblMetazoa; FBtr0071169; FBpp0071117; FBgn0020653. [P91938-3]
GeneID; 31760; -.
KEGG; dme:Dmel_CG2151; -.
CTD; 31760; -.
FlyBase; FBgn0020653; Trxr-1.
eggNOG; KOG0405; Eukaryota.
eggNOG; COG1249; LUCA.
GeneTree; ENSGT00390000007578; -.
InParanoid; P91938; -.
KO; K00384; -.
OMA; VYGLHYL; -.
OrthoDB; EOG091G03IU; -.
PhylomeDB; P91938; -.
BRENDA; 1.8.1.9; 1994.
Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
ChiTaRS; Trxr-1; fly.
EvolutionaryTrace; P91938; -.
GenomeRNAi; 31760; -.
PRO; PR:P91938; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0020653; -.
Genevisible; P91938; DM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0004362; F:glutathione-disulfide reductase activity; IMP:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
GO; GO:0000305; P:response to oxygen radical; IBA:GO_Central.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01438; TGR; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein;
Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase;
Redox-active center; Reference proteome; Transit peptide.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 596 Thioredoxin reductase 1, mitochondrial.
/FTId=PRO_0000030291.
NP_BIND 120 126 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 143 147 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 159 170 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 233 235 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 262 266 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 322 328 NADP. {ECO:0000269|PubMed:17385893}.
NP_BIND 392 399 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 429 432 FAD. {ECO:0000269|PubMed:17385893}.
NP_BIND 438 443 FAD. {ECO:0000269|PubMed:17385893}.
ACT_SITE 569 569 Proton acceptor.
{ECO:0000269|PubMed:17385893}.
BINDING 282 282 FAD. {ECO:0000269|PubMed:17385893}.
BINDING 286 286 FAD. {ECO:0000269|PubMed:17385893}.
BINDING 302 302 FAD. {ECO:0000269|PubMed:17385893}.
BINDING 355 355 NADP. {ECO:0000269|PubMed:17385893}.
BINDING 472 472 FAD. {ECO:0000269|PubMed:17385893}.
BINDING 570 570 FAD. {ECO:0000269|PubMed:17385893}.
DISULFID 162 167 Redox-active.
{ECO:0000269|PubMed:17385893}.
DISULFID 594 595 Redox-active.
{ECO:0000269|PubMed:17385893}.
VAR_SEQ 1 105 Missing (in isoform A and isoform D).
{ECO:0000303|PubMed:11158675,
ECO:0000303|PubMed:9056265,
ECO:0000303|Ref.5}.
/FTId=VSP_005572.
VAR_SEQ 1 88 Missing (in isoform C).
{ECO:0000303|Ref.5}.
/FTId=VSP_005571.
VAR_SEQ 89 110 QHPHCDRAAMYAQPVRKMSTKG -> MLKYMICAIVVGAKK
STSSKYN (in isoform C).
{ECO:0000303|Ref.5}.
/FTId=VSP_005573.
VAR_SEQ 106 110 MSTKG -> MAPVQ (in isoform A).
{ECO:0000303|PubMed:11158675,
ECO:0000303|PubMed:9056265,
ECO:0000303|Ref.5}.
/FTId=VSP_005574.
MUTAGEN 569 569 H->Q: Almost complete loss of TrX
reduction. {ECO:0000269|PubMed:18211101}.
MUTAGEN 574 574 E->A: Reduced Trx reduction.
{ECO:0000269|PubMed:18991392}.
MUTAGEN 574 574 E->Q: Reduced Trx reduction.
{ECO:0000269|PubMed:18991392}.
MUTAGEN 594 594 C->S: Loss of Trx reduction.
{ECO:0000269|PubMed:11158675}.
MUTAGEN 595 595 C->S: Loss of Trx reduction.
{ECO:0000269|PubMed:11158675}.
CONFLICT 88 88 F -> L (in Ref. 6; AAK93067).
{ECO:0000305}.
CONFLICT 134 134 V -> S (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 151 151 Missing (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 189 190 Missing (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 195 195 E -> D (in Ref. 1; AAB48441 and 6;
AAK93067). {ECO:0000305}.
CONFLICT 203 207 KLVQS -> RLCAV (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 213 216 KSVN -> SRH (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 220 220 R -> V (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 239 247 DSHTLLAKL -> TRTHCCPSM (in Ref. 1;
AAB48441). {ECO:0000305}.
CONFLICT 264 264 Missing (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 276 280 VEYGI -> AEIGT (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 292 292 Missing (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 317 318 EP -> G (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 351 386 RKTVPLSVEKQDDGKLLVKYKNVETGEEAEDVYDTV -> A
DVDRCREADDAAAREYRLTQIRFTTSHHR (in Ref. 1;
AAB48441). {ECO:0000305}.
CONFLICT 379 379 A -> S (in Ref. 6; AAK93067).
{ECO:0000305}.
CONFLICT 396 398 VDD -> CDS (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 403 406 NAGV -> MPAL (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 424 425 AN -> PH (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 455 455 Y -> F (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 461 461 R -> S (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 473 483 TPLEYACVGLS -> SWSTSASGLA (in Ref. 1;
AAB48441). {ECO:0000305}.
CONFLICT 488 495 VKQFGADE -> SSSSEPR (in Ref. 1;
AAB48441). {ECO:0000305}.
CONFLICT 559 560 IN -> L (in Ref. 1; AAB48441).
{ECO:0000305}.
CONFLICT 583 583 K -> KP (in Ref. 1; AAB48441).
{ECO:0000305}.
STRAND 114 120 {ECO:0000244|PDB:3DGH}.
HELIX 124 135 {ECO:0000244|PDB:3DGH}.
STRAND 140 143 {ECO:0000244|PDB:3DGH}.
TURN 150 152 {ECO:0000244|PDB:3DGH}.
HELIX 161 165 {ECO:0000244|PDB:3DGH}.
HELIX 167 188 {ECO:0000244|PDB:3DGH}.
HELIX 201 225 {ECO:0000244|PDB:3DGH}.
STRAND 229 231 {ECO:0000244|PDB:3DGH}.
STRAND 233 239 {ECO:0000244|PDB:3DGH}.
STRAND 242 246 {ECO:0000244|PDB:3DGH}.
STRAND 252 261 {ECO:0000244|PDB:3DGH}.
STRAND 265 267 {ECO:0000244|PDB:3DGH}.
HELIX 275 278 {ECO:0000244|PDB:3DGH}.
HELIX 282 285 {ECO:0000244|PDB:3DGH}.
STRAND 294 298 {ECO:0000244|PDB:3DGH}.
HELIX 302 313 {ECO:0000244|PDB:3DGH}.
STRAND 317 324 {ECO:0000244|PDB:3DGH}.
HELIX 332 344 {ECO:0000244|PDB:3DGH}.
STRAND 349 351 {ECO:0000244|PDB:3DGH}.
STRAND 353 360 {ECO:0000244|PDB:3DGH}.
STRAND 366 372 {ECO:0000244|PDB:3DGH}.
TURN 373 375 {ECO:0000244|PDB:3DGH}.
STRAND 378 388 {ECO:0000244|PDB:3DGH}.
STRAND 392 394 {ECO:0000244|PDB:3DGH}.
HELIX 397 399 {ECO:0000244|PDB:3DGH}.
HELIX 401 403 {ECO:0000244|PDB:3DGH}.
STRAND 409 413 {ECO:0000244|PDB:2NVK}.
STRAND 426 428 {ECO:0000244|PDB:3DGH}.
HELIX 430 432 {ECO:0000244|PDB:3DH9}.
HELIX 440 455 {ECO:0000244|PDB:3DGH}.
STRAND 469 471 {ECO:0000244|PDB:3DGH}.
STRAND 473 481 {ECO:0000244|PDB:3DGH}.
HELIX 484 491 {ECO:0000244|PDB:3DGH}.
HELIX 493 495 {ECO:0000244|PDB:3DGH}.
STRAND 496 502 {ECO:0000244|PDB:3DGH}.
HELIX 506 508 {ECO:0000244|PDB:3DGH}.
TURN 509 512 {ECO:0000244|PDB:3DGH}.
STRAND 519 527 {ECO:0000244|PDB:3DGH}.
STRAND 531 539 {ECO:0000244|PDB:3DGH}.
HELIX 542 554 {ECO:0000244|PDB:3DGH}.
HELIX 559 563 {ECO:0000244|PDB:3DGH}.
HELIX 573 578 {ECO:0000244|PDB:3DGH}.
TURN 583 585 {ECO:0000244|PDB:3DGH}.
SEQUENCE 596 AA; 64322 MW; 8DA6FC08CF6A7292 CRC64;
MNLCNSRFSV TFVRQCSTIL TSPSAGIIQN RGSLTTKVPH WISSSLSCAH HTFQRTMNLT
GQRGSRDSTG ATGGNAPAGS GAGAPPPFQH PHCDRAAMYA QPVRKMSTKG GSYDYDLIVI
GGGSAGLACA KEAVLNGARV ACLDFVKPTP TLGTKWGVGG TCVNVGCIPK KLMHQASLLG
EAVHEAAAYG WNVDEKIKPD WHKLVQSVQN HIKSVNWVTR VDLRDKKVEY INGLGSFVDS
HTLLAKLKSG ERTITAQTFV IAVGGRPRYP DIPGAVEYGI TSDDLFSLDR EPGKTLVVGA
GYIGLECAGF LKGLGYEPTV MVRSIVLRGF DQQMAELVAA SMEERGIPFL RKTVPLSVEK
QDDGKLLVKY KNVETGEEAE DVYDTVLWAI GRKGLVDDLN LPNAGVTVQK DKIPVDSQEA
TNVANIYAVG DIIYGKPELT PVAVLAGRLL ARRLYGGSTQ RMDYKDVATT VFTPLEYACV
GLSEEDAVKQ FGADEIEVFH GYYKPTEFFI PQKSVRYCYL KAVAERHGDQ RVYGLHYIGP
VAGEVIQGFA AALKSGLTIN TLINTVGIHP TTAEEFTRLA ITKRSGLDPT PASCCS


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