ID   TRXB2_YEAST             Reviewed;         342 AA.
AC   P38816;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 86.
DE   RecName: Full=Thioredoxin reductase 2, mitochondrial;
DE            EC=1.8.1.9;
DE   Flags: Precursor;
GN   Name=TRR2; OrderedLocusNames=YHR106W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=94378003; PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=99156917; 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
RT   mitochondrial thioredoxin system in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 274:6366-6373(1999).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Acts on mitochondrial thioredoxin 3. Implicated in the
CC       defense against oxidative stress.
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; U00059; AAB68856.1; -; Genomic_DNA.
DR   EMBL; AY557882; AAS56208.1; -; Genomic_DNA.
DR   PIR; S48948; S48948.
DR   RefSeq; NP_011974.1; -.
DR   HSSP; Q39243; 1VDC.
DR   DIP; DIP:1942N; -.
DR   IntAct; P38816; 6.
DR   PeptideAtlas; P38816; -.
DR   Ensembl; YHR106W; Saccharomyces cerevisiae.
DR   GeneID; 856506; -.
DR   GenomeReviews; U00093_GR; YHR106W.
DR   KEGG; sce:YHR106W; -.
DR   NMPDR; fig|4932.3.peg.3135; -.
DR   CYGD; YHR106w; -.
DR   SGD; S000001148; TRR2.
DR   HOGENOM; P38816; -.
DR   OMA; P38816; GEIKKVW.
DR   BRENDA; 1.8.1.9; 250.
DR   NextBio; 982236; -.
DR   GermOnline; YHR106W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:SGD.
DR   GO; GO:0045454; P:cell redox homeostasis; IC:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; FAD; Flavoprotein; Mitochondrion;
KW   NADP; Oxidoreductase; Redox-active center; Transit peptide.
FT   TRANSIT       1     23       Mitochondrion (Potential).
FT   CHAIN        24    342       Thioredoxin reductase 2, mitochondrial.
FT                                /FTId=PRO_0000030303.
FT   NP_BIND      56     68       FAD (By similarity).
FT   NP_BIND     311    320       FAD (By similarity).
FT   DISULFID    165    168       Redox-active (By similarity).
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
//