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Database: UniProt
Entry: A0A0T5P2R1_9RHOB
LinkDB: A0A0T5P2R1_9RHOB
Original site: A0A0T5P2R1_9RHOB 
ID   A0A0T5P2R1_9RHOB        Unreviewed;       162 AA.
AC   A0A0T5P2R1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glutathione-dependent peroxiredoxin {ECO:0000256|RuleBase:RU366011};
DE            EC=1.11.1.27 {ECO:0000256|RuleBase:RU366011};
GN   ORFNames=RIdsm_04572 {ECO:0000313|EMBL:QEW28733.1}, XM52_24410
GN   {ECO:0000313|EMBL:KRS15395.1};
OS   Roseovarius indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS15395.1, ECO:0000313|Proteomes:UP000051401};
RN   [1] {ECO:0000313|EMBL:KRS15395.1, ECO:0000313|Proteomes:UP000051401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B108 {ECO:0000313|EMBL:KRS15395.1,
RC   ECO:0000313|Proteomes:UP000051401};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius indicus B108T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEW28733.1, ECO:0000313|Proteomes:UP000325785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW28733.1,
RC   ECO:0000313|Proteomes:UP000325785};
RA   Vollmers J., Petersen J.;
RT   "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT   geographic distances.";
RL   Submitted (AUG-2018) 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   -!- 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:0000256|RuleBase:RU366011};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000256|RuleBase:RU366011}.
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DR   EMBL; LAXI01000023; KRS15395.1; -; Genomic_DNA.
DR   EMBL; CP031598; QEW28733.1; -; Genomic_DNA.
DR   RefSeq; WP_057820500.1; NZ_LXYQ01000004.1.
DR   AlphaFoldDB; A0A0T5P2R1; -.
DR   STRING; 540747.SAMN04488031_11612; -.
DR   KEGG; rid:RIdsm_04572; -.
DR   PATRIC; fig|540747.5.peg.3234; -.
DR   OrthoDB; 9800621at2; -.
DR   Proteomes; UP000051401; Unassembled WGS sequence.
DR   Proteomes; UP000325785; Chromosome.
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   ECO:0000313|EMBL:QEW28733.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU366011, ECO:0000313|EMBL:KRS15395.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU366011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051401}.
FT   DOMAIN          3..162
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        49
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ   SEQUENCE   162 AA;  16948 MW;  45E3D08757FE9EF9 CRC64;
     MTITVGDKLP DATLVQMGGE GPEPVELSSK TDGRKVVIFA VPGAFTPTCH SAHVPSFIRT
     KDQFAEKGVD EIICVSVNDP FVMGNWGEAT GASDAGITML GDPEAKFTKA IGMDFSAPPA
     GLIDRSKRYA MLVEDGKVSV LNLEDSPGTC EVSAGEGLLA DM
//
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