TSA2_YEAST
ID TSA2_YEAST Reviewed; 196 AA.
AC Q04120; D6VT78;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Peroxiredoxin TSA2 {ECO:0000305};
DE Short=Prx;
DE EC=1.11.1.24 {ECO:0000269|PubMed:15210711};
DE AltName: Full=Cytoplasmic thiol peroxidase 2 {ECO:0000303|PubMed:10681558};
DE Short=cTPx 2 {ECO:0000303|PubMed:10681558};
DE AltName: Full=Thiol-specific antioxidant protein 2;
DE AltName: Full=Thioredoxin peroxidase type Ib {ECO:0000303|PubMed:9888818};
DE Short=TPx type Ib;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin TSA2 {ECO:0000305};
GN Name=TSA2 {ECO:0000303|PubMed:11741925};
GN OrderedLocusNames=YDR453C {ECO:0000312|SGD:S000002861}; ORFNames=D9461.38;
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=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 [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 FUNCTION.
RX PubMed=9888818; DOI=10.1021/bi9817818;
RA Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.;
RT "Purification and characterization of a second type thioredoxin peroxidase
RT (type II TPx) from Saccharomyces cerevisiae.";
RL Biochemistry 38:776-783(1999).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-48.
RX PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
RA Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
RT "Distinct physiological functions of thiol peroxidase isoenzymes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:5723-5732(2000).
RN [5]
RP FUNCTION.
RX PubMed=11741925; DOI=10.1074/jbc.m106846200;
RA Wong C.M., Zhou Y., Ng R.W., Kung Hf H.F., Jin D.Y.;
RT "Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular
RT defense against oxidative and nitrosative stress.";
RL J. Biol. Chem. 277:5385-5394(2002).
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 FUNCTION.
RX PubMed=15163410; DOI=10.1016/j.cell.2004.05.002;
RA Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R.,
RA Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W.,
RA Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.;
RT "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-
RT dependent switching from a peroxidase to a molecular chaperone function.";
RL Cell 117:625-635(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=15210711; DOI=10.1074/jbc.m313773200;
RA Munhoz D.C., Netto L.E.;
RT "Cytosolic thioredoxin peroxidase I and II are important defenses of yeast
RT against organic hydroperoxide insult: catalases and peroxiredoxins
RT cooperate in the decomposition of H2O2 by yeast.";
RL J. Biol. Chem. 279:35219-35227(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT SER-48, AND DISULFIDE
RP BONDS.
RX PubMed=26894543; DOI=10.1107/s2059798315023815;
RA Nielsen M.H., Kidmose R.T., Jenner L.B.;
RT "Structure of TSA2 reveals novel features of the active-site loop of
RT peroxiredoxins.";
RL Acta Crystallogr. D 72:158-167(2016).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events (PubMed:10681558, PubMed:11741925, PubMed:15210711).
CC Can act alternatively as peroxidase and molecular chaperone. Oxidative
CC stress and heat shock exposure cause a reversible shift of the protein
CC structure from low MW species to high MW complexes, triggering a
CC peroxidase-to-chaperone functional switch. The chaperone function of
CC the protein enhances resistance to heat shock (PubMed:15163410).
CC {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:11741925,
CC ECO:0000269|PubMed:15163410, ECO:0000269|PubMed:15210711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:15210711};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.8 uM for H(2)O(2) {ECO:0000269|PubMed:15210711};
CC KM=4.5 uM for cumene hydroperoxide {ECO:0000269|PubMed:15210711};
CC KM=5.1 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:15210711};
CC Vmax=0.39 uM/sec/mg enzyme for H(2)O(2)
CC {ECO:0000269|PubMed:15210711};
CC Vmax=0.28 uM/sec/mg enzyme for cumene hydroperoxide
CC {ECO:0000269|PubMed:15210711};
CC Vmax=0.29 uM/sec/mg enzyme for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:15210711};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558}.
CC -!- INDUCTION: By peroxides. {ECO:0000269|PubMed:15210711}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P34760}.
CC -!- MISCELLANEOUS: Present with 4820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; U33007; AAB64886.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12288.1; -; Genomic_DNA.
DR PIR; S69732; S69732.
DR RefSeq; NP_010741.1; NM_001180761.1.
DR PDB; 5DVB; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=1-196.
DR PDB; 5EPT; X-ray; 5.00 A; A/B/C/D/E/F/G/H/I/J=1-196.
DR PDB; 6UTL; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=1-196.
DR PDBsum; 5DVB; -.
DR PDBsum; 5EPT; -.
DR PDBsum; 6UTL; -.
DR AlphaFoldDB; Q04120; -.
DR SMR; Q04120; -.
DR BioGRID; 32508; 63.
DR DIP; DIP-4317N; -.
DR IntAct; Q04120; 9.
DR MINT; Q04120; -.
DR STRING; 4932.YDR453C; -.
DR MoonProt; Q04120; -.
DR PeroxiBase; 4467; Sce2CysPrx02.
DR MaxQB; Q04120; -.
DR PaxDb; Q04120; -.
DR PRIDE; Q04120; -.
DR TopDownProteomics; Q04120; -.
DR EnsemblFungi; YDR453C_mRNA; YDR453C; YDR453C.
DR GeneID; 852064; -.
DR KEGG; sce:YDR453C; -.
DR SGD; S000002861; TSA2.
DR VEuPathDB; FungiDB:YDR453C; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000153430; -.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; Q04120; -.
DR OMA; EDSESCY; -.
DR BioCyc; YEAST:YDR453C-MON; -.
DR BRENDA; 1.11.1.24; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:Q04120; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04120; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:SGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR GO; GO:0050821; P:protein stabilization; IDA:CAFA.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Disulfide bond; Isopeptide bond;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..196
FT /note="Peroxiredoxin TSA2"
FT /id="PRO_0000135096"
FT DOMAIN 3..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:26894543"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT DISULFID 48
FT /note="Interchain (with C-171); in linked form"
FT /evidence="ECO:0000269|PubMed:26894543,
FT ECO:0007744|PDB:5EPT"
FT DISULFID 171
FT /note="Interchain (with C-48); in linked form"
FT /evidence="ECO:0000269|PubMed:26894543,
FT ECO:0007744|PDB:5EPT"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT MUTAGEN 48
FT /note="C->S: No activity."
FT /evidence="ECO:0000269|PubMed:10681558"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:5DVB"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:5DVB"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5DVB"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:5DVB"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5DVB"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:5DVB"
SQ SEQUENCE 196 AA; 21615 MW; 43CC57C92081D745 CRC64;
MVAEVQKQAP PFKKTAVVDG IFEEISLEKY KGKYVVLAFV PLAFSFVCPT EIVAFSDAAK
KFEDQGAQVL FASTDSEYSL LAWTNLPRKD GGLGPVKVPL LADKNHSLSR DYGVLIEKEG
IALRGLFIID PKGIIRHITI NDLSVGRNVN EALRLVEGFQ WTDKNGTVLP CNWTPGAATI
KPDVKDSKEY FKNANN
