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Database: UniProt
Entry: A0A1M6Y4D5_9FLAO
LinkDB: A0A1M6Y4D5_9FLAO
Original site: A0A1M6Y4D5_9FLAO 
ID   A0A1M6Y4D5_9FLAO        Unreviewed;       210 AA.
AC   A0A1M6Y4D5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peroxiredoxin (Alkyl hydroperoxide reductase subunit C) {ECO:0000313|EMBL:SHL13082.1};
GN   ORFNames=SAMN05444407_102346 {ECO:0000313|EMBL:SHL13082.1};
OS   Chryseobacterium contaminans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1423959 {ECO:0000313|EMBL:SHL13082.1, ECO:0000313|Proteomes:UP000184069};
RN   [1] {ECO:0000313|EMBL:SHL13082.1, ECO:0000313|Proteomes:UP000184069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27621 {ECO:0000313|EMBL:SHL13082.1,
RC   ECO:0000313|Proteomes:UP000184069};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRBM01000002; SHL13082.1; -; Genomic_DNA.
DR   RefSeq; WP_066692332.1; NZ_MAYF01000045.1.
DR   AlphaFoldDB; A0A1M6Y4D5; -.
DR   STRING; 1423959.SAMN05444407_102346; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000184069; Unassembled WGS sequence.
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;  23817 MW;  62EB72098BA5755B CRC64;
     MSLVGKKFPN LTIDAMSEMG DDLRINILEE ATNNQQKVLL FWYPKDFTFV CPTELHAFQE
     ALGEFEKRNT KVIGASCDTN EVHFAWLNTP KDNGGIEGVT YPLLADTHRQ LANTLGIVDQ
     DFEYNEEGEE IFTGSNVTYR ATYLIDETGK IFHEAVNDMP LGRNVKEFLR LIDAYTHVQK
     HGEVCPANWE EGKDAMKADR TSTAEYLAKN
//
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