TRXB2_YEAST
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 03-AUG-2022, entry version 178.
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; 50.
DR DIP; DIP-1942N; -.
DR IntAct; P38816; 2.
DR MINT; P38816; -.
DR STRING; 4932.YHR106W; -.
DR MaxQB; P38816; -.
DR PaxDb; P38816; -.
DR PRIDE; P38816; -.
DR EnsemblFungi; YHR106W_mRNA; YHR106W; YHR106W.
DR GeneID; 856506; -.
DR KEGG; sce:YHR106W; -.
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; FRAEDYW; -.
DR BioCyc; YEAST:YHR106W-MON; -.
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 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; -; 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 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
