ID   TRXB_DICDI              Reviewed;         319 AA.
AC   Q54UU8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=trrA; ORFNames=DDB_G0280815;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P0A9P4};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000038; EAL67065.1; -; Genomic_DNA.
DR   RefSeq; XP_641039.1; XM_635947.1.
DR   AlphaFoldDB; Q54UU8; -.
DR   SMR; Q54UU8; -.
DR   STRING; 44689.DDB0231235; -.
DR   PaxDb; Q54UU8; -.
DR   EnsemblProtists; EAL67065; EAL67065; DDB_G0280815.
DR   GeneID; 8622741; -.
DR   KEGG; ddi:DDB_G0280815; -.
DR   dictyBase; DDB_G0280815; trrA.
DR   eggNOG; KOG0404; Eukaryota.
DR   HOGENOM; CLU_031864_5_1_1; -.
DR   InParanoid; Q54UU8; -.
DR   OMA; VDNFPGY; -.
DR   PhylomeDB; Q54UU8; -.
DR   PRO; PR:Q54UU8; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:dictyBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IDA:dictyBase.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..319
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000318657"
FT   BINDING         36..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         289..298
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        144..147
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   319 AA;  34208 MW;  A03B2A592B189957 CRC64;
     MSTEKIQKVV IIGSGPAGHT AGIYAGRARL EPLMFEGFMA GGVAAGGQLT TTTEIENFPG
     FPIDISGSEL MDKMREQNIK CGTTIETKTI SKVDLKQRPF TIYVEDEEDK PIKAQSIIIA
     TGATAKRMGV PGETEFWSKG VSACAVCDGA LPIYRNKHLV VVGGGDTAAE EATFLTHFAS
     KVTLLVRRNV MRASKAMQQK VFSNPKIEVL WDTTLVEIKG EKSVTSVGIY NSETKVSSNL
     DAQGLFYAIG HTPNSAFLNG QLNTDETGYI ITQPGSTKTN VEGVFACGDV QDKVYRQAIT
     AAGNGCMAAL DCERFLSSL