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Database: UniProt
Entry: A0A172Y0G2_9FLAO
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Original site: A0A172Y0G2_9FLAO 
ID   A0A172Y0G2_9FLAO        Unreviewed;       210 AA.
AC   A0A172Y0G2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Alkyl hydroperoxide reductase {ECO:0000313|EMBL:ANF52748.1};
GN   ORFNames=A0O34_20510 {ECO:0000313|EMBL:ANF52748.1};
OS   Chryseobacterium glaciei.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1685010 {ECO:0000313|EMBL:ANF52748.1, ECO:0000313|Proteomes:UP000077824};
RN   [1] {ECO:0000313|EMBL:ANF52748.1, ECO:0000313|Proteomes:UP000077824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 10212 {ECO:0000313|EMBL:ANF52748.1,
RC   ECO:0000313|Proteomes:UP000077824};
RA   Pal M., Swarnkar M.K., Kaushal K., Chhibber S., Singh A.K., Gulati A.;
RT   "Complete Genome Sequence of Chryseobacterium sp. IHBB 10212.";
RL   Submitted (APR-2016) 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|ARBA:ARBA00037420}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
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DR   EMBL; CP015199; ANF52748.1; -; Genomic_DNA.
DR   RefSeq; WP_066758845.1; NZ_CP015199.1.
DR   AlphaFoldDB; A0A172Y0G2; -.
DR   STRING; 1685010.A0O34_20510; -.
DR   KEGG; chh:A0O34_20510; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000077824; Chromosome.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        51
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   210 AA;  23872 MW;  6B116AE4ABCD6ADF CRC64;
     MSLVGKKFPN VAIDAMSEMG DDLRINIFEE TTKNQQKVIL FWYPKDFTFV CPTELHAFQE
     ALGEFEKRNT KVIGASCDTN EVHFAWLNVS KDNGGIEGVT YPLLADTHRQ LANMLGIVDQ
     DFEYNDEGEE VFTGSNVTYR ATYLIDETGK VFHESVNDMP LGRNVKEYLR LIDAYTHVQK
     HGEVCPANWE EGKDAMKADR NSTAEYLAKN
//
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