PRX_SCHPO
ID PRX_SCHPO Reviewed; 195 AA.
AC O94561; A9QUS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Peroxiredoxin bcp1;
DE Short=Prx;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P40553};
DE AltName: Full=Bacterioferritin comigratory protein 1;
DE Short=BCP;
DE AltName: Full=Nuclear thiol peroxidase;
DE Short=nTPx;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin bcp1 {ECO:0000305};
GN Name=bcp1; ORFNames=SPBC1773.02c;
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].
RX PubMed=19229492; DOI=10.1007/s12275-008-0077-3;
RA Kang G.Y., Park E.H., Kim K., Lim C.J.;
RT "Overexpression of bacterioferritin comigratory protein (Bcp) enhances
RT viability and reduced glutathione level in the fission yeast under
RT stress.";
RL J. Microbiol. 47:60-67(2009).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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: 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 (By similarity). Acts as a scavenger of H(2)O(2)
CC (PubMed:20356456). {ECO:0000250|UniProtKB:P40553,
CC 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:0000250|UniProtKB:P40553};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20356456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- PTM: The active site is a conserved redox-active cysteine residue, the
CC peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the
CC peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine
CC sulfenic acid (C(P)-SOH), which then reacts with another cysteine
CC residue, the resolving cysteine (C(R)), to form a disulfide bridge. The
CC disulfide is subsequently reduced by an appropriate electron donor to
CC complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin,
CC C(R) is present in the same subunit to form an intramolecular
CC disulfide. The disulfide is subsequently reduced by thioredoxin.
CC {ECO:0000250|UniProtKB:P40553}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; EU266495; ABX64442.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21907.1; -; Genomic_DNA.
DR PIR; T39667; T39667.
DR RefSeq; NP_595117.1; NM_001021024.2.
DR AlphaFoldDB; O94561; -.
DR SMR; O94561; -.
DR BioGRID; 276173; 17.
DR STRING; 4896.SPBC1773.02c.1; -.
DR PeroxiBase; 4315; SpomBCP.
DR MaxQB; O94561; -.
DR PaxDb; O94561; -.
DR EnsemblFungi; SPBC1773.02c.1; SPBC1773.02c.1:pep; SPBC1773.02c.
DR GeneID; 2539615; -.
DR KEGG; spo:SPBC1773.02c; -.
DR PomBase; SPBC1773.02c; bcp1.
DR VEuPathDB; FungiDB:SPBC1773.02c; -.
DR eggNOG; KOG0855; Eukaryota.
DR HOGENOM; CLU_042529_2_2_1; -.
DR InParanoid; O94561; -.
DR OMA; QVCGFQK; -.
DR PhylomeDB; O94561; -.
DR PRO; PR:O94561; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:PomBase.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IC:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IC:PomBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IC:PomBase.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cytoplasm; Disulfide bond; Nucleus; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..195
FT /note="Peroxiredoxin bcp1"
FT /id="PRO_0000314635"
FT DOMAIN 46..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 89
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P40553"
FT DISULFID 89..94
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P40553"
SQ SEQUENCE 195 AA; 21164 MW; 53D832E58A686741 CRC64;
MDAPRRSSRL AAKIANVLDS KGTIIPEAAP VMLKKPAKDE SVDSTIQVGD VIPDITLPDE
DGTSIRLRDI TANKGLVIFA YPKASTPGCT KQGCGFRDNY PKIQASDYEV LGLSFDTSKA
QKAFKDKQNF PYHLLSDPKG ELIKKLGAEK PGGGKLFRSH WIFEKGTGKC IVKEIDISPL
VSVDKAFAVI TDSEP
