ID   TRXB2_YEAST             Reviewed;         342 AA.
AC   P38816; D3DL56;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Thioredoxin reductase 2, mitochondrial {ECO:0000303|PubMed:10037727};
DE            EC=1.8.1.9 {ECO:0000269|PubMed:10037727};
DE   Flags: Precursor;
GN   Name=TRR2 {ECO:0000303|PubMed:10037727}; OrderedLocusNames=YHR106W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=10037727; DOI=10.1074/jbc.274.10.6366;
RA   Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.-A.,
RA   Wright A.P.H., Spyrou G.;
RT   "Identification and functional characterization of a novel mitochondrial
RT   thioredoxin system in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 274:6366-6373(1999).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
CC   -!- FUNCTION: Acts on mitochondrial thioredoxin 3. Implicated in the
CC       defense against oxidative stress. {ECO:0000269|PubMed:10037727}.
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:0000269|PubMed:10037727};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29509};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P29509};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10037727}.
CC   -!- INTERACTION:
CC       P38816; P29509: TRR1; NbExp=4; IntAct=EBI-19502, EBI-19497;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10037727,
CC       ECO:0000269|PubMed:16823961}.
CC   -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; U00059; AAB68856.1; -; Genomic_DNA.
DR   EMBL; AY557882; AAS56208.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06800.1; -; Genomic_DNA.
DR   PIR; S48948; S48948.
DR   RefSeq; NP_011974.1; NM_001179236.1.
DR   AlphaFoldDB; P38816; -.
DR   SMR; P38816; -.
DR   BioGRID; 36539; 53.
DR   DIP; DIP-1942N; -.
DR   IntAct; P38816; 2.
DR   MINT; P38816; -.
DR   STRING; 4932.YHR106W; -.
DR   MaxQB; P38816; -.
DR   PaxDb; 4932-YHR106W; -.
DR   PeptideAtlas; P38816; -.
DR   EnsemblFungi; YHR106W_mRNA; YHR106W; YHR106W.
DR   GeneID; 856506; -.
DR   KEGG; sce:YHR106W; -.
DR   AGR; SGD:S000001148; -.
DR   SGD; S000001148; TRR2.
DR   VEuPathDB; FungiDB:YHR106W; -.
DR   eggNOG; KOG0404; Eukaryota.
DR   GeneTree; ENSGT00940000176591; -.
DR   HOGENOM; CLU_031864_5_1_1; -.
DR   InParanoid; P38816; -.
DR   OMA; ANKFYWI; -.
DR   OrthoDB; 1125295at2759; -.
DR   BioCyc; YEAST:YHR106W-MONOMER; -.
DR   BioGRID-ORCS; 856506; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P38816; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38816; Protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IDA:SGD.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   NCBIfam; TIGR01292; TRX_reduct; 1.
DR   PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..342
FT                   /note="Thioredoxin reductase 2, mitochondrial"
FT                   /id="PRO_0000030303"
FT   BINDING         34..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         56..68
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         63..64
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         68
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         77
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         110
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         168
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         311..320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         318..320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   DISULFID        165..168
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
SQ   SEQUENCE   342 AA;  37087 MW;  739F302AA0837A5A CRC64;
     MIKHIVSPFR TNFVGISKSV LSRMIHHKVT IIGSGPAAHT AAIYLARAEM KPTLYEGMMA
     NGIAAGGQLT TTTDIENFPG FPESLSGSEL MERMRKQSAK FGTNIITETV SKVDLSSKPF
     RLWTEFNEDA EPVTTDAIIL ATGASAKRMH LPGEETYWQQ GISACAVCDG AVPIFRNKPL
     AVIGGGDSAC EEAEFLTKYA SKVYILVRKD HFRASVIMQR RIEKNPNIIV LFNTVALEAK
     GDGKLLNMLR IKNTKSNVEN DLEVNGLFYA IGHSPATDIV KGQVDEEETG YIKTVPGSSL
     TSVPGFFAAG DVQDSRYRQA VTSAGSGCIA ALDAERYLSA QE
//