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Database: UniProt
Entry: Q2CAL3_OCEGH
LinkDB: Q2CAL3_OCEGH
Original site: Q2CAL3_OCEGH 
ID   Q2CAL3_OCEGH            Unreviewed;       162 AA.
AC   Q2CAL3;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Glutathione-dependent peroxiredoxin {ECO:0000256|RuleBase:RU366011};
DE            EC=1.11.1.27 {ECO:0000256|RuleBase:RU366011};
GN   ORFNames=OG2516_12371 {ECO:0000313|EMBL:EAR49700.1};
OS   Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS   HTCC2516).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceanicola.
OX   NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR49700.1, ECO:0000313|Proteomes:UP000003635};
RN   [1] {ECO:0000313|EMBL:EAR49700.1, ECO:0000313|Proteomes:UP000003635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC   {ECO:0000313|Proteomes:UP000003635};
RX   PubMed=20418400; DOI=10.1128/JB.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
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:EAR49700.1}.
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DR   EMBL; AAOT01000051; EAR49700.1; -; Genomic_DNA.
DR   RefSeq; WP_007255992.1; NZ_CH724107.1.
DR   AlphaFoldDB; Q2CAL3; -.
DR   STRING; 314256.OG2516_12371; -.
DR   eggNOG; COG0678; Bacteria.
DR   HOGENOM; CLU_072440_1_2_5; -.
DR   OMA; TCSARHV; -.
DR   OrthoDB; 9800621at2; -.
DR   Proteomes; UP000003635; 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: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:UP000003635}.
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;  16596 MW;  677AF913AA70A033 CRC64;
     MALTTGDTLP DATLLRIGND GPETVDLGAM LAGRKVVIFG LPGAYTGTCT SAHVPSFIRS
     MDALGAKGVD AVVCTAVNDP FVMKAWGEST GAAEAGIEML ADASGQFAKA IGLDFDNPAV
     GFYGRSKRYA LMAEDGVVKV LNVEDSPGVC DMSGGETMVD AL
//
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