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Database: UniProt
Entry: A0A3M0C5Z9_9PROT
LinkDB: A0A3M0C5Z9_9PROT
Original site: A0A3M0C5Z9_9PROT 
ID   A0A3M0C5Z9_9PROT        Unreviewed;       160 AA.
AC   A0A3M0C5Z9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Glutathione-dependent peroxiredoxin {ECO:0000256|RuleBase:RU366011};
DE            EC=1.11.1.27 {ECO:0000256|RuleBase:RU366011};
GN   ORFNames=BXY39_2923 {ECO:0000313|EMBL:RMB04652.1};
OS   Eilatimonas milleporae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Eilatimonas.
OX   NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB04652.1, ECO:0000313|Proteomes:UP000271227};
RN   [1] {ECO:0000313|EMBL:RMB04652.1, ECO:0000313|Proteomes:UP000271227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB04652.1,
RC   ECO:0000313|Proteomes:UP000271227};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMB04652.1}.
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DR   EMBL; REFR01000013; RMB04652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0C5Z9; -.
DR   InParanoid; A0A3M0C5Z9; -.
DR   OrthoDB; 9800621at2; -.
DR   Proteomes; UP000271227; 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: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   Peroxidase {ECO:0000256|RuleBase:RU366011};
KW   Redox-active center {ECO:0000256|RuleBase:RU366011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271227}.
FT   DOMAIN          3..160
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   160 AA;  16733 MW;  E9D828FFD8C9DD25 CRC64;
     MTIQVGETIP SAKLMTMTAD GPGPVDTDGY FKGRKVAVFS VPGAFTPTCS AKHLPGFVDQ
     ADALKAKGVD EIACFSVNDV FVMDAWGKGS SADGKVTMLA DGNGDFAKAL GLEMDASGFG
     MGTRSQRFSM LVDDGKVTAL YIEEPGAFQV SSAEHMLAHL
//
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