GPX1_SCHPO
ID GPX1_SCHPO Reviewed; 158 AA.
AC O59858;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glutathione peroxidase-like peroxiredoxin gpx1 {ECO:0000305};
DE EC=1.11.1.24 {ECO:0000269|PubMed:18162174};
DE AltName: Full=Glutathione peroxidase homolog {ECO:0000303|PubMed:10455235};
DE Short=GPx;
DE AltName: Full=Thioredoxin peroxidase gpx1 {ECO:0000303|PubMed:18162174};
GN Name=gpx1 {ECO:0000303|PubMed:10455235};
GN ORFNames=SPBC32F12.03c {ECO:0000312|PomBase:SPBC32F12.03c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=JY741;
RX PubMed=10455235;
RX DOI=10.1002/(sici)1097-0061(199908)15:11<1125::aid-yea442>3.0.co;2-z;
RA Yamada K., Nakagawa C.W., Mutoh N.;
RT "Schizosaccharomyces pombe homologue of glutathione peroxidase, which does
RT not contain selenocysteine, is induced by several stresses and works as an
RT antioxidant.";
RL Yeast 15:1125-1132(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18162174; DOI=10.1016/j.bbrc.2007.12.105;
RA Lee S.Y., Song J.Y., Kwon E.S., Roe J.H.;
RT "Gpx1 is a stationary phase-specific thioredoxin peroxidase in fission
RT yeast.";
RL Biochem. Biophys. Res. Commun. 367:67-71(2008).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20356456; DOI=10.5483/bmbrep.2010.43.3.170;
RA Kim J.S., Bang M.A., Lee S., Chae H.Z., Kim K.;
RT "Distinct functional roles of peroxiredoxin isozymes and glutathione
RT peroxidase from fission yeast, Schizosaccharomyces pombe.";
RL BMB Rep. 43:170-175(2010).
CC -!- FUNCTION: Glutathione peroxidase-like protein that protects cells
CC during oxidative stress. Has peroxidase activity reducing hydrogen
CC peroxide, alkyl and phospholipid hydroperoxides using preferentially
CC thioredoxin as a reducing power. May act as a scavenger of H(2)O(2).
CC {ECO:0000269|PubMed:10455235, ECO:0000269|PubMed:20356456}.
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:18162174};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20356456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18162174}.
CC Mitochondrion {ECO:0000269|PubMed:18162174}.
CC -!- INDUCTION: By oxidative, osmo- and heat stress.
CC {ECO:0000269|PubMed:10455235}.
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:0000250|UniProtKB:P40581}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a glutathione peroxidase
CC (PubMed:10455235), but functions as an atypical 2-Cys peroxiredoxin
CC using thioredoxin as reducing power instead (PubMed:18162174).
CC {ECO:0000305|PubMed:10455235, ECO:0000305|PubMed:18162174}.
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; AB012395; BAA25326.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19364.1; -; Genomic_DNA.
DR PIR; T43376; T43376.
DR RefSeq; NP_596146.1; NM_001022065.2.
DR AlphaFoldDB; O59858; -.
DR SMR; O59858; -.
DR BioGRID; 276755; 15.
DR STRING; 4896.SPBC32F12.03c.1; -.
DR PeroxiBase; 3744; SpomGPx01.
DR iPTMnet; O59858; -.
DR MaxQB; O59858; -.
DR PaxDb; O59858; -.
DR PRIDE; O59858; -.
DR EnsemblFungi; SPBC32F12.03c.1; SPBC32F12.03c.1:pep; SPBC32F12.03c.
DR GeneID; 2540222; -.
DR KEGG; spo:SPBC32F12.03c; -.
DR PomBase; SPBC32F12.03c; gpx1.
DR VEuPathDB; FungiDB:SPBC32F12.03c; -.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_3_2_1; -.
DR InParanoid; O59858; -.
DR OMA; FPMMSKI; -.
DR PhylomeDB; O59858; -.
DR PRO; PR:O59858; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:PomBase.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IDA:PomBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:PomBase.
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; Cytoplasm; Disulfide bond; Mitochondrion; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome; Stress response.
FT CHAIN 1..158
FT /note="Glutathione peroxidase-like peroxiredoxin gpx1"
FT /id="PRO_0000066644"
FT ACT_SITE 36
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P40581"
FT DISULFID 36..82
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P40581"
SQ SEQUENCE 158 AA; 18061 MW; 2D7009280B676876 CRC64;
MSHFYDLAPK DKDGNPFPFS NLKGKVVLVV NTASKCGFTP QYKGLEALYQ KYKDRGFIIL
GFPCNQFGNQ EPGSDEEIAQ FCQKNYGVTF PVLAKINVNG DNVDPVYQFL KSQKKQLGLE
RIKWNFEKFL VNRQGQVIER YSSISKPEHL ENDIESVL
