ID   PRX5_RHIET              Reviewed;         179 AA.
AC   O69777;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Peroxiredoxin;
DE            Short=Prx;
DE            EC=1.11.1.27 {ECO:0000250|UniProtKB:P44758};
DE   AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305};
OS   Rhizobium etli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=29449;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNPAF512;
RX   PubMed=9658006; DOI=10.1128/jb.180.14.3620-3628.1998;
RA   Michiels J., Moris M., Dombrecht B., Verreth C., Vanderleyden J.;
RT   "Differential regulation of the Rhizobium etli rpoN2 gene expression during
RT   symbiosis and free-living growth.";
RL   J. Bacteriol. 180:3620-3628(1998).
RN   [2]
RP   SEQUENCE REVISION TO 30-31; 34 AND 72.
RA   Michiels J.;
RL   Submitted (APR-2003) 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:0000250|UniProtKB:P44758}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione
CC         disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297; EC=1.11.1.27;
CC         Evidence={ECO:0000250|UniProtKB:P44758};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A9PCL4}.
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 1-Cys
CC       peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC       with a cysteine from another protein or with a small thiol molecule.
CC       {ECO:0000250|UniProtKB:A9PCL4}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ005696; CAA06680.3; -; Genomic_DNA.
DR   RefSeq; WP_004678566.1; NZ_JACJNQ010000026.1.
DR   AlphaFoldDB; O69777; -.
DR   SMR; O69777; -.
DR   GeneID; 58692214; -.
DR   PATRIC; fig|29449.15.peg.5173; -.
DR   OMA; SFCAKAK; -.
DR   BRENDA; 1.11.1.24; 5340.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd03013; PRX5_like; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PTHR10430; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Oxidoreductase; Peroxidase; Redox-active center.
FT   CHAIN           1..179
FT                   /note="Peroxiredoxin"
FT                   /id="PRO_0000056614"
FT   DOMAIN          2..152
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        56
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate (for
FT                   peroxiredoxin activity)"
FT                   /evidence="ECO:0000250|UniProtKB:P44758"
SQ   SEQUENCE   179 AA;  20080 MW;  AB0F934B749116FC CRC64;
     MTMEKQVPIV TFRTRVRDES ISGPNPYRWE DKTTDDYFSG KRVILFSLPG AFTPICSTFQ
     LPDFESLYVE FKKNGIDDIY CLSVNDAFVM NAWGKSQGLK NVKLIPDGSG EFTRKMGMLV
     AKDNLGFGLR SWRYAAVINN GVVEGWFEEE GFGDNCATDP YGVSSPQNIL KCLKAPAFV