ID R0I0T4_9BRAS Unreviewed; 162 AA.
AC R0I0T4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013016, ECO:0000256|RuleBase:RU366011};
DE EC=1.11.1.25 {ECO:0000256|ARBA:ARBA00013016, ECO:0000256|RuleBase:RU366011};
GN ORFNames=CARUB_v10021068mg {ECO:0000313|EMBL:EOA35809.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA35809.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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 -!- 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:0000256|ARBA:ARBA00001711};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
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DR EMBL; KB870806; EOA35809.1; -; Genomic_DNA.
DR RefSeq; XP_006302911.1; XM_006302849.1.
DR AlphaFoldDB; R0I0T4; -.
DR STRING; 81985.R0I0T4; -.
DR GeneID; 17895683; -.
DR KEGG; crb:17895683; -.
DR eggNOG; KOG0541; Eukaryota.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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:SF8; PEROXIREDOXIN-2A-RELATED; 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:UP000029121}.
FT DOMAIN 4..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 162 AA; 17502 MW; 6B95D3B7D9151866 CRC64;
MAPITVGDVV PDGSISFFDE NDQLQTVSVH SIAAGKKVIL FGVPGAFTPT CSMSHVPGFI
EKAEELKSKG IDEIICFSVN DPFVMKAWGK TYPENKHVKF VADGSGEYTH LLGLELDLKD
KGLGIRSRRF AMLLDNLKVT VANIESGGEF TVSGVEDILK AL
//
