ID   PRX5_SINFN              Reviewed;         188 AA.
AC   Q53212;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Peroxiredoxin y4vD;
DE            Short=Prx;
DE            EC=1.11.1.27 {ECO:0000250|UniProtKB:P44758};
DE   AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305};
GN   OrderedLocusNames=NGR_a01200; ORFNames=y4vD;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8796346; DOI=10.1101/gr.6.7.590;
RA   Freiberg C., Perret X., Broughton W.J., Rosenthal A.;
RT   "Sequencing the 500-kb GC-rich symbiotic replicon of Rhizobium sp. NGR234
RT   using dye terminators and a thermostable 'sequenase': a beginning.";
RL   Genome Res. 6:590-600(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; Z68203; CAA92419.1; -; Genomic_DNA.
DR   EMBL; U00090; AAB91892.1; -; Genomic_DNA.
DR   RefSeq; NP_444105.1; NC_000914.2.
DR   RefSeq; WP_010875158.1; NC_000914.2.
DR   AlphaFoldDB; Q53212; -.
DR   SMR; Q53212; -.
DR   STRING; 394.NGR_a01200; -.
DR   EnsemblBacteria; AAB91892; AAB91892; NGR_a01200.
DR   KEGG; rhi:NGR_a01200; -.
DR   PATRIC; fig|394.7.peg.104; -.
DR   eggNOG; COG0678; Bacteria.
DR   HOGENOM; CLU_072440_2_0_5; -.
DR   OMA; HVPEYIQ; -.
DR   OrthoDB; 892697at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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; Plasmid; Redox-active center;
KW   Reference proteome.
FT   CHAIN           1..188
FT                   /note="Peroxiredoxin y4vD"
FT                   /id="PRO_0000056613"
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   188 AA;  21432 MW;  9F03D6DBE7B284BD CRC64;
     MPVKKRVPFV AFRTRVRDET IGGPNPYRWE VRTTEDYFSG KRVVLFSLPG AFTPTCSTQQ
     LPDFERLYDE FGKVGIEAVY CLSVNDAFVM NAWGKALGLE KVRLIPDGSG EFTRKMGMLV
     AKDNLGFGMR SWRYAAVVND SVVEQWFEEE GFSDNCESDP YWASSPQNIL ETLRTFDTAR
     LGRVPIKF