ID PRX1_YEAST Reviewed; 261 AA. AC P34227; D6VPT6; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 190. DE RecName: Full=Peroxiredoxin PRX1, mitochondrial {ECO:0000305}; DE Short=Prx; DE EC=1.11.1.25 {ECO:0000269|PubMed:20059400}; DE EC=1.11.1.27 {ECO:0000269|PubMed:19332553}; DE AltName: Full=1-Cys PRX; DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305}; DE AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305}; DE AltName: Full=Mitochondrial thiol peroxidase {ECO:0000303|PubMed:10681558}; DE Short=mTPx {ECO:0000303|PubMed:10681558}; DE AltName: Full=Thioredoxin peroxidase; DE Flags: Precursor; GN Name=PRX1 {ECO:0000303|PubMed:10821871}; OrderedLocusNames=YBL064C; GN ORFNames=YBL0503, YBL0524; 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]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8154187; DOI=10.1002/yea.320091210; RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.; RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm RT of yeast chromosome II. Identification of 26 open reading frames, including RT the KIP1 and SEC17 genes."; RL Yeast 9:1355-1371(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). 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 CHARACTERIZATION, AND MUTAGENESIS OF CYS-91. 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, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF CYS-38. RX PubMed=10821871; DOI=10.1074/jbc.275.21.16296; RA Pedrajas J.R., Miranda-Vizuete A., Javanmardy N., Gustafsson J.A., RA Spyrou G.; RT "Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine RT type peroxiredoxin with thioredoxin peroxidase activity."; RL J. Biol. Chem. 275:16296-16301(2000). 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200; RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; RT "Profiling phosphoproteins of yeast mitochondria reveals a role of RT phosphorylation in assembly of the ATP synthase."; RL Mol. Cell. Proteomics 6:1896-1906(2007). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19332553; DOI=10.1128/mcb.01918-08; RA Greetham D., Grant C.M.; RT "Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is RT dependent on thioredoxin reductase and glutathione in vivo."; RL Mol. Cell. Biol. 29:3229-3240(2009). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=20059400; DOI=10.1089/ars.2009.2950; RA Pedrajas J.R., Padilla C.A., McDonagh B., Barcena J.A.; RT "Glutaredoxin participates in the reduction of peroxides by the RT mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae."; RL Antioxid. Redox Signal. 13:249-258(2010). 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. Involved in mitochondrial protection of cadmium- CC induced oxidative stress. {ECO:0000269|PubMed:10821871, CC ECO:0000269|PubMed:19332553, ECO:0000269|PubMed:20059400}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione CC disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:58297; EC=1.11.1.27; CC Evidence={ECO:0000269|PubMed:19332553}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]- CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA- CC COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, CC ChEBI:CHEBI:50058; EC=1.11.1.25; CC Evidence={ECO:0000269|PubMed:20059400}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.2 uM for H(2)O(2) {ECO:0000269|PubMed:10821871}; CC KM=10.9 uM for tert-butyl hydroperoxide CC {ECO:0000269|PubMed:10821871}; CC KM=8.1 uM for TRX3 {ECO:0000269|PubMed:10821871}; CC Vmax=8.5 umol/min/mg enzyme for H(2)O(2) CC {ECO:0000269|PubMed:10821871}; CC Vmax=7.4 umol/min/mg enzyme for tert-butyl hydroperoxide CC {ECO:0000269|PubMed:10821871}; CC Vmax=9.5 umol/min/mg enzyme for TRX3 {ECO:0000269|PubMed:10821871}; CC pH dependence: CC Optimum pH is 7.0 (PubMed:10821871). Optimum pH is 8.5 (using CC glutaredoxin as electron donor) (PubMed:20059400). CC {ECO:0000269|PubMed:10821871, ECO:0000269|PubMed:20059400}; CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10821871, CC ECO:0000305|PubMed:20059400}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10821871, CC ECO:0000269|PubMed:14576278}. 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 1-Cys CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide CC with a cysteine from another protein or with a small thiol molecule. CC C(P) is reactivated by glutathionylation and subsequent reduction by CC either glutaredoxin GRX2 or thioredoxin reductase TRR2, coupled with CC reduced glutathione (GSH). {ECO:0000305|PubMed:19332553, CC ECO:0000305|PubMed:20059400}. CC -!- MISCELLANEOUS: Present with 4510 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z23261; CAA80784.1; -; Genomic_DNA. DR EMBL; Z35825; CAA84884.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07056.1; -; Genomic_DNA. DR PIR; S39825; S39825. DR RefSeq; NP_009489.1; NM_001178304.1. DR PDB; 5YKJ; X-ray; 1.53 A; A=49-261. DR PDB; 5YKW; X-ray; 2.08 A; B=88-95. DR PDBsum; 5YKJ; -. DR PDBsum; 5YKW; -. DR AlphaFoldDB; P34227; -. DR SMR; P34227; -. DR BioGRID; 32635; 90. DR DIP; DIP-6412N; -. DR IntAct; P34227; 12. DR MINT; P34227; -. DR STRING; 4932.YBL064C; -. DR iPTMnet; P34227; -. DR MaxQB; P34227; -. DR PaxDb; 4932-YBL064C; -. DR PeptideAtlas; P34227; -. DR TopDownProteomics; P34227; -. DR EnsemblFungi; YBL064C_mRNA; YBL064C; YBL064C. DR GeneID; 852215; -. DR KEGG; sce:YBL064C; -. DR AGR; SGD:S000000160; -. DR SGD; S000000160; PRX1. DR VEuPathDB; FungiDB:YBL064C; -. DR eggNOG; KOG0854; Eukaryota. DR GeneTree; ENSGT00940000171910; -. DR HOGENOM; CLU_042529_4_2_1; -. DR InParanoid; P34227; -. DR OMA; RLTMLYP; -. DR OrthoDB; 103042at2759; -. DR BioCyc; YEAST:G3O-28961-MONOMER; -. DR BRENDA; 1.11.1.25; 984. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 852215; 1 hit in 10 CRISPR screens. DR PRO; PR:P34227; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P34227; Protein. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; 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; IBA:GO_Central. DR CDD; cd03016; PRX_1cys; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR045020; PRX_1cys. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR43503; MCG48959-RELATED; 1. DR PANTHER; PTHR43503:SF9; PEROXIREDOXIN PRX1, MITOCHONDRIAL; 1. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. DR UCD-2DPAGE; P34227; -. PE 1: Evidence at protein level; KW 3D-structure; Antioxidant; Disulfide bond; Mitochondrion; Oxidoreductase; KW Peroxidase; Phosphoprotein; Redox-active center; Reference proteome; KW Transit peptide. FT TRANSIT 1..13 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 14..261 FT /note="Peroxiredoxin PRX1, mitochondrial" FT /id="PRO_0000135151" FT DOMAIN 49..212 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT ACT_SITE 91 FT /note="Cysteine sulfenic acid (-SOH) intermediate" FT /evidence="ECO:0000305|PubMed:10681558" FT MOD_RES 53 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17761666" FT DISULFID 38 FT /note="Interchain" FT /evidence="ECO:0000305|PubMed:10821871" FT MUTAGEN 38 FT /note="C->S: Impairs dimer formation." FT /evidence="ECO:0000269|PubMed:10821871" FT MUTAGEN 91 FT /note="C->S: No activity." FT /evidence="ECO:0000269|PubMed:10681558" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 69..73 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 76..84 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 89..100 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 102..106 FT /evidence="ECO:0007829|PDB:5YKJ" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 120..134 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 150..154 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:5YKJ" FT TURN 170..173 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 200..216 FT /evidence="ECO:0007829|PDB:5YKJ" FT HELIX 238..245 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:5YKJ" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:5YKJ" SQ SEQUENCE 261 AA; 29496 MW; F611A9ED85E4681A CRC64; MFSRICSAQL KRTAWTLPKQ AHLQSQTIKT FATAPILCKQ FKQSDQPRLR INSDAPNFDA DTTVGKINFY DYLGDSWGVL FSHPADFTPV CTTEVSAFAK LKPEFDKRNV KLIGLSVEDV ESHEKWIQDI KEIAKVKNVG FPIIGDTFRN VAFLYDMVDA EGFKNINDGS LKTVRSVFVI DPKKKIRLIF TYPSTVGRNT SEVLRVIDAL QLTDKEGVVT PINWQPADDV IIPPSVSNDE AKAKFGQFNE IKPYLRFTKS K //