TRXB1_YEAST
ID TRXB1_YEAST Reviewed; 319 AA.
AC P29509; D6VSY3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Thioredoxin reductase 1;
DE Short=TR;
DE Short=TrxR;
DE EC=1.8.1.9 {ECO:0000269|PubMed:7961686};
DE AltName: Full=Thioredoxin peroxidase 1 {ECO:0000303|PubMed:7961686};
DE Short=TPx {ECO:0000303|PubMed:7961686};
DE AltName: Full=Thioredoxin-dependent peroxide reductase 1 {ECO:0000303|PubMed:7961686};
GN Name=TRR1; OrderedLocusNames=YDR353W; ORFNames=D9476.5;
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 [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 2-16; 90-97;
RP 126-137; 176-179; 233-238 AND 296-303, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 200358 / YNN 295;
RX PubMed=7961686; DOI=10.1016/s0021-9258(18)47038-x;
RA Chae H.Z., Chung S.J., Rhee S.G.;
RT "Thioredoxin-dependent peroxide reductase from yeast.";
RL J. Biol. Chem. 269:27670-27678(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-319.
RX PubMed=2428012; DOI=10.1093/nar/14.16.6357;
RA Furter R., Paravicini G., Aebi M., Braus G., Prantl F., Niederberger P.,
RA Huetter R.;
RT "The TRP4 gene of Saccharomyces cerevisiae: isolation and structural
RT analysis.";
RL Nucleic Acids Res. 14:6357-6373(1986).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-319 IN COMPLEX WITH FAD,
RP COFACTOR, AND SUBUNIT.
RX PubMed=18930846; DOI=10.1016/j.bbapap.2008.09.011;
RA Zhang Z., Bao R., Zhang Y., Yu J., Zhou C.Z., Chen Y.;
RT "Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin
RT reductase Trr1 reveals the structural basis for species-specific
RT recognition of thioredoxin.";
RL Biochim. Biophys. Acta 1794:124-128(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-319 IN COMPLEX WITH FAD,
RP FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=20235561; DOI=10.1021/bi901962p;
RA Oliveira M.A., Discola K.F., Alves S.V., Medrano F.J., Guimaraes B.G.,
RA Netto L.E.;
RT "Insights into the specificity of thioredoxin reductase-thioredoxin
RT interactions. A structural and functional investigation of the yeast
RT thioredoxin system.";
RL Biochemistry 49:3317-3326(2010).
CC -!- FUNCTION: Central component in the thioredoxin system. Reduces
CC thioredoxins 1 and 2. {ECO:0000269|PubMed:20235561,
CC ECO:0000269|PubMed:7961686}.
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:7961686};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20346;
CC Evidence={ECO:0000269|PubMed:7961686};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:18930846,
CC ECO:0000269|PubMed:20235561};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18930846,
CC ECO:0000269|PubMed:20235561, ECO:0000269|PubMed:7961686}.
CC -!- INTERACTION:
CC P29509; P53879: RHO5; NbExp=4; IntAct=EBI-19497, EBI-29054;
CC P29509; P38816: TRR2; NbExp=4; IntAct=EBI-19497, EBI-19502;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000305|PubMed:7961686}.
CC -!- MISCELLANEOUS: Present with 292000 molecules/cell in log phase SD
CC medium. {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; U10274; AAA64747.1; -; Genomic_DNA.
DR EMBL; U28372; AAB64789.1; -; Genomic_DNA.
DR EMBL; X04273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY557749; AAS56075.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12193.1; -; Genomic_DNA.
DR PIR; S61150; S61150.
DR RefSeq; NP_010640.1; NM_001180661.1.
DR PDB; 3D8X; X-ray; 2.80 A; A/B=2-319.
DR PDB; 3ITJ; X-ray; 2.40 A; A/B/C/D=2-319.
DR PDBsum; 3D8X; -.
DR PDBsum; 3ITJ; -.
DR AlphaFoldDB; P29509; -.
DR SMR; P29509; -.
DR BioGRID; 32410; 56.
DR DIP; DIP-4319N; -.
DR IntAct; P29509; 10.
DR MINT; P29509; -.
DR STRING; 4932.YDR353W; -.
DR iPTMnet; P29509; -.
DR MaxQB; P29509; -.
DR PaxDb; P29509; -.
DR PRIDE; P29509; -.
DR EnsemblFungi; YDR353W_mRNA; YDR353W; YDR353W.
DR GeneID; 851955; -.
DR KEGG; sce:YDR353W; -.
DR SGD; S000002761; TRR1.
DR VEuPathDB; FungiDB:YDR353W; -.
DR eggNOG; KOG0404; Eukaryota.
DR GeneTree; ENSGT00940000176591; -.
DR HOGENOM; CLU_031864_5_1_1; -.
DR InParanoid; P29509; -.
DR OMA; VDNFPGY; -.
DR BioCyc; YEAST:YDR353W-MON; -.
DR BRENDA; 1.8.1.9; 984.
DR EvolutionaryTrace; P29509; -.
DR PRO; PR:P29509; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P29509; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008198; F:ferrous iron binding; IDA:SGD.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI: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 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein;
KW Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7961686"
FT CHAIN 2..319
FT /note="Thioredoxin reductase 1"
FT /id="PRO_0000166770"
FT BINDING 11..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 40..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT BINDING 295..297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18930846,
FT ECO:0000269|PubMed:20235561"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT DISULFID 142..145
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:20235561"
FT CONFLICT 18
FT /note="A -> V (in Ref. 1; AAA64747)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="T -> A (in Ref. 1; AAA64747)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="T -> A (in Ref. 1; AAA64747)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..196
FT /note="VFMLVRKDHLRASTIMQ -> CLCLSEKTICVLLPLCK (in Ref. 1;
FT AAA64747)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3ITJ"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:3ITJ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 210..230
FT /evidence="ECO:0007829|PDB:3ITJ"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3ITJ"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3D8X"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3ITJ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:3ITJ"
FT HELIX 297..315
FT /evidence="ECO:0007829|PDB:3ITJ"
SQ SEQUENCE 319 AA; 34238 MW; 9F9E58A4BAD859E1 CRC64;
MVHNKVTIIG SGPAAHTAAI YLARAEIKPI LYEGMMANGI AAGGQLTTTT EIENFPGFPD
GLTGSELMDR MREQSTKFGT EIITETVSKV DLSSKPFKLW TEFNEDAEPV TTDAIILATG
ASAKRMHLPG EETYWQKGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV
FMLVRKDHLR ASTIMQKRAE KNEKIEILYN TVALEAKGDG KLLNALRIKN TKKNEETDLP
VSGLFYAIGH TPATKIVAGQ VDTDEAGYIK TVPGSSLTSV PGFFAAGDVQ DSKYRQAITS
AGSGCMAALD AEKYLTSLE
