ID A0A0E0MUD0_ORYRU Unreviewed; 198 AA.
AC A0A0E0MUD0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI01G11470.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI01G11470.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
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DR AlphaFoldDB; A0A0E0MUD0; -.
DR SMR; A0A0E0MUD0; -.
DR STRING; 4529.A0A0E0MUD0; -.
DR EnsemblPlants; ORUFI01G11470.1; ORUFI01G11470.1; ORUFI01G11470.
DR Gramene; ORUFI01G11470.1; ORUFI01G11470.1; ORUFI01G11470.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_2_1_1; -.
DR OMA; YTMNGWA; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblPlants.
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:SF34; PEROXIREDOXIN-2F, 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:UP000008022}.
FT DOMAIN 34..198
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 86
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 198 AA; 20874 MW; 21362AB6D2964CCD CRC64;
MASALLRKAT VGGSAAAAAA RWASRGLASV GSGSDIVSAA PGVSLQKARS WDEGVATNFS
TTPLKDIFHG KKVVIFGLPG AYTGVCSQAH VPSYKNNIDK LKAKGVDSVI CVSVNDPYAL
NGWAEKLQAK DAIEFYGDFD GSFHKSLDLE VDLSAALLGR RSHRWSAFVD DGKIKAFNVE
VAPSDFKVSG AEVILDQI
//
