ID B2AT30_PODAN Unreviewed; 166 AA.
AC B2AT30;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Peroxisomal prx5-like peroxiredoxin {ECO:0000313|EMBL:CDP23814.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 4 {ECO:0000313|EMBL:CAP67553.1};
GN ORFNames=PODANS_1_14500 {ECO:0000313|EMBL:CAP67553.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP67553.1};
RN [1] {ECO:0000313|EMBL:CAP67553.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP67553.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP67553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67553.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP23814.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU366011}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
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; CU633899; CAP67553.1; -; Genomic_DNA.
DR EMBL; FO904936; CDP23814.1; -; Genomic_DNA.
DR RefSeq; XP_001906882.1; XM_001906847.1.
DR AlphaFoldDB; B2AT30; -.
DR STRING; 515849.B2AT30; -.
DR GeneID; 6191506; -.
DR KEGG; pan:PODANSg3915; -.
DR VEuPathDB; FungiDB:PODANS_1_14500; -.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_1_1_1; -.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000001197; Chromosome 1.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|RuleBase:RU366011};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366011};
KW Peroxidase {ECO:0000256|RuleBase:RU366011};
KW Redox-active center {ECO:0000256|RuleBase:RU366011};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 4..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 60
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 166 AA; 17647 MW; 366EFCFF4F24C068 CRC64;
MSGLKAGDSF PPNVTFTYVP PTGDLNVTAC GIGIQYDASK EFASKKVVLV AVPGAFTPTC
QVSHVTSYLA KLDDLKAKGV DQVIFIASND HWVMAAWGKA NGVKDDSILF MSDAGLEFSK
SIGWTQGDRT LRYAIVVDHG KVTYAEVDSV RGSIENTGAE GVLAKL
//
