PRX1_YEAST
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 03-AUG-2022, entry version 181.
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}.
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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; 82.
DR DIP; DIP-6412N; -.
DR IntAct; P34227; 12.
DR MINT; P34227; -.
DR STRING; 4932.YBL064C; -.
DR iPTMnet; P34227; -.
DR UCD-2DPAGE; P34227; -.
DR MaxQB; P34227; -.
DR PaxDb; P34227; -.
DR PRIDE; P34227; -.
DR TopDownProteomics; P34227; -.
DR EnsemblFungi; YBL064C_mRNA; YBL064C; YBL064C.
DR GeneID; 852215; -.
DR KEGG; sce:YBL064C; -.
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 BioCyc; YEAST:G3O-28961-MON; -.
DR BRENDA; 1.11.1.25; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:0004601; F:peroxidase activity; IBA:GO_Central.
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; IGI:SGD.
DR GO; GO:1903205; P:regulation of hydrogen peroxide-induced cell death; IMP:SGD.
DR GO; GO:0046686; P:response to cadmium ion; IMP:SGD.
DR CDD; cd03016; PRX_1cys; 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 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; 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
