GPX1_YEAST
ID GPX1_YEAST Reviewed; 167 AA.
AC P36014; D6VXQ8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Glutathione peroxidase-like peroxiredoxin 1 {ECO:0000305};
DE EC=1.11.1.24 {ECO:0000269|PubMed:20572871, ECO:0000269|PubMed:22659048};
DE EC=1.11.1.9 {ECO:0000269|PubMed:20572871, ECO:0000269|PubMed:22659048};
DE AltName: Full=Glutathione peroxidase homolog 1 {ECO:0000303|PubMed:10480913};
DE Short=GPx 1;
GN Name=GPX1 {ECO:0000303|PubMed:10480913};
GN OrderedLocusNames=YKL026C {ECO:0000312|SGD:S000001509};
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(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, AND INDUCTION.
RX PubMed=10480913; DOI=10.1074/jbc.274.38.27002;
RA Inoue Y., Matsuda T., Sugiyama K., Izawa S., Kimura A.;
RT "Genetic analysis of glutathione peroxidase in oxidative stress response of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:27002-27009(1999).
RN [5]
RP FUNCTION.
RX PubMed=11445588; DOI=10.1074/jbc.m105672200;
RA Avery A.M., Avery S.V.;
RT "Saccharomyces cerevisiae expresses three phospholipid hydroperoxide
RT glutathione peroxidases.";
RL J. Biol. Chem. 276:33730-33735(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF CYS-36.
RX PubMed=20572871; DOI=10.1111/j.1567-1364.2010.00651.x;
RA Ohdate T., Kita K., Inoue Y.;
RT "Kinetics and redox regulation of Gpx1, an atypical 2-Cys peroxiredoxin, in
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 10:787-790(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22659048; DOI=10.1016/j.bbalip.2012.05.004;
RA Ohdate T., Inoue Y.;
RT "Involvement of glutathione peroxidase 1 in growth and peroxisome formation
RT in Saccharomyces cerevisiae in oleic acid medium.";
RL Biochim. Biophys. Acta 1821:1295-1305(2012).
CC -!- FUNCTION: Glutathione peroxidase-like protein that protects cells from
CC phospholipid hydroperoxides and nonphospholipid peroxides during
CC oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase
CC activity using thioredoxin or glutathione as a reducing power
CC (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation
CC (PubMed:22659048). {ECO:0000269|PubMed:10480913,
CC ECO:0000269|PubMed:11445588, ECO:0000269|PubMed:20572871,
CC ECO:0000269|PubMed:22659048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000269|PubMed:20572871, ECO:0000269|PubMed:22659048};
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:20572871, ECO:0000269|PubMed:22659048};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=141 uM for H(2)O(2) (using glutathione as electron donor)
CC {ECO:0000269|PubMed:20572871};
CC KM=75 uM for tert-butyl hydroperoxide (using glutathione as electron
CC donor) {ECO:0000269|PubMed:20572871};
CC KM=120 uM for H(2)O(2) (using thioredoxin as electron donor)
CC {ECO:0000269|PubMed:20572871};
CC KM=223 uM for tert-butyl hydroperoxide (using glutathione as electron
CC donor) {ECO:0000269|PubMed:20572871};
CC Vmax=2.98 umol/min/mg enzyme for H(2)O(2) (using glutathione as
CC electron donor) {ECO:0000269|PubMed:20572871};
CC Vmax=0.579 umol/min/mg enzyme for tert-butyl hydroperoxide (using
CC glutathione as electron donor) {ECO:0000269|PubMed:20572871};
CC Vmax=0.739 umol/min/mg enzyme for H(2)O(2) (using thioredoxin as
CC electron donor) {ECO:0000269|PubMed:20572871};
CC Vmax=1.25 umol/min/mg enzyme for tert-butyl hydroperoxide (using
CC thioredoxin as electron donor) {ECO:0000269|PubMed:20572871};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20572871}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:22659048}.
CC Mitochondrion outer membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:22659048}.
CC -!- INDUCTION: By glucose starvation. {ECO:0000269|PubMed:10480913}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth and peroxisome formation in oleic
CC acid medium. {ECO:0000269|PubMed:22659048}.
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 atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. {ECO:0000305|PubMed:20572871}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a glutathione peroxidase
CC (PubMed:10480913) or a phospholipid hydroperoxide glutathione
CC peroxidase (PubMed:11445588), but functions as an atypical 2-Cys
CC peroxiredoxin using both glutathione and thioredoxin almost equally as
CC reducing power instead (PubMed:20572871). {ECO:0000305|PubMed:10480913,
CC ECO:0000305|PubMed:11445588, ECO:0000305|PubMed:20572871}.
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DR EMBL; Z28026; CAA81861.1; -; Genomic_DNA.
DR EMBL; AY557895; AAS56221.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09128.1; -; Genomic_DNA.
DR PIR; S37843; S37843.
DR RefSeq; NP_012899.3; NM_001179592.3.
DR AlphaFoldDB; P36014; -.
DR SMR; P36014; -.
DR BioGRID; 34105; 31.
DR DIP; DIP-5437N; -.
DR IntAct; P36014; 1.
DR MINT; P36014; -.
DR STRING; 4932.YKL026C; -.
DR PeroxiBase; 3740; SceGPx01.
DR MaxQB; P36014; -.
DR PaxDb; P36014; -.
DR PRIDE; P36014; -.
DR EnsemblFungi; YKL026C_mRNA; YKL026C; YKL026C.
DR GeneID; 853842; -.
DR KEGG; sce:YKL026C; -.
DR SGD; S000001509; GPX1.
DR VEuPathDB; FungiDB:YKL026C; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000165680; -.
DR HOGENOM; CLU_029507_3_2_1; -.
DR InParanoid; P36014; -.
DR OMA; KVVRFWR; -.
DR BioCyc; YEAST:YKL026C-MON; -.
DR PRO; PR:P36014; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36014; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IMP:SGD.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Disulfide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Oxidoreductase; Peroxidase; Peroxisome;
KW Redox-active center; Reference proteome.
FT CHAIN 1..167
FT /note="Glutathione peroxidase-like peroxiredoxin 1"
FT /id="PRO_0000066641"
FT ACT_SITE 36
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:20572871,
FT ECO:0000305|PubMed:22659048"
FT DISULFID 36..82
FT /note="Redox-active"
FT /evidence="ECO:0000305|PubMed:20572871"
FT MUTAGEN 36
FT /note="C->S: Prevents oxidation of the protein."
FT /evidence="ECO:0000269|PubMed:20572871"
SQ SEQUENCE 167 AA; 19485 MW; 8C421FFF813391DD CRC64;
MQEFYSFSPI DENGNPFPFN SLRNKVVLIV NVASHCAFTP QYKELEYLYE KYKSHGLVIV
AFPCGQFGNQ EFEKDKEINK FCQDKYGVTF PILHKIRCNG QKQDPVYKFL KNSVSGKSGI
KMIKWNFEKF VVDRNGKVVK RFSCMTRPLE LCPIIEELLN QPPEEQI
