ID A0A2V4X7D1_9FLAO Unreviewed; 212 AA.
AC A0A2V4X7D1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peroxiredoxin (Alkyl hydroperoxide reductase subunit C) {ECO:0000313|EMBL:PYE81509.1};
GN ORFNames=DFQ11_10283 {ECO:0000313|EMBL:PYE81509.1};
OS Winogradskyella epiphytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=262005 {ECO:0000313|EMBL:PYE81509.1, ECO:0000313|Proteomes:UP000248054};
RN [1] {ECO:0000313|EMBL:PYE81509.1, ECO:0000313|Proteomes:UP000248054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7945 {ECO:0000313|EMBL:PYE81509.1,
RC ECO:0000313|Proteomes:UP000248054};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-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|ARBA:ARBA00037420}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:PYE81509.1}.
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DR EMBL; QJTD01000002; PYE81509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4X7D1; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000248054; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000248054}.
FT DOMAIN 2..179
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 212 AA; 23613 MW; 4DC8D175C99DCBBF CRC64;
MALVGRQFPD LEVNAMNEMG ETFRVNVLEE AKNNNKKVVL FWYPKDFTFV CPTELHAFQE
ALGEFEKRNT IVIGASCDTA EVHFAWLNTA KDDGGIEGVT YPILADSNRN LASALGILDI
FNESYDEETG LLTVEGDNVT YRATYIIDEE GTIQHESINN MPLGRNVNEY LRIVDALTHV
QQKGEVCPAN WEEGKDAMEA SAKGTAAYLS TH
//
