ID H8XU43_FLAIG Unreviewed; 211 AA.
AC H8XU43;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Probable peroxiredoxin {ECO:0000313|EMBL:CCG52826.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:CCG52826.1};
GN OrderedLocusNames=KQS_04230 {ECO:0000313|EMBL:CCG52826.1};
OS Flavobacterium indicum (strain DSM 17447 / CIP 109464 / GPTSA100-9).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1094466 {ECO:0000313|EMBL:CCG52826.1, ECO:0000313|Proteomes:UP000007599};
RN [1] {ECO:0000313|EMBL:CCG52826.1, ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RX PubMed=22582381; DOI=10.1128/JB.00420-12;
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.F., Touchon M.,
RA Duchaud E.;
RT "Complete Genome Sequence of Flavobacterium indicum GPSTA100-9T, Isolated
RT from Warm Spring Water.";
RL J. Bacteriol. 194:3024-3025(2012).
RN [2] {ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.-F., Touchon M.,
RA Duchaud E.;
RT "Complete genome sequence of Flavobacterium indicum GPTSA100-9T, isolated
RT from warm spring water.";
RL Submitted (MAR-2012) 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; HE774682; CCG52826.1; -; Genomic_DNA.
DR RefSeq; WP_014387968.1; NC_017025.1.
DR AlphaFoldDB; H8XU43; -.
DR STRING; 1094466.KQS_04230; -.
DR KEGG; fin:KQS_04230; -.
DR PATRIC; fig|1094466.5.peg.830; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_1_10; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000007599; Chromosome.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:RHEA.
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 ECO:0000313|EMBL:CCG52826.1}; Peroxidase {ECO:0000313|EMBL:CCG52826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007599}.
FT DOMAIN 2..178
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 211 AA; 23541 MW; 44DB5019E876E1CA CRC64;
MALVGKKFPN ITVDAISEMG DNLRINVLEE ATKNNKKVLL FWYPKDFTFV CPTELHAFQA
ALGEFEKRNT IVIGASCDTN EVHFAWLNTA KNNGGIEGVT YPLLADTTRN LSTALGILEA
EEVFNEETGD YLIEGSNVTY RATYLVDETG VIFHESVNHM PLGRNVNEYL RLIDAYTHVQ
TKGEVCPANW EEGKDAMKAD RSSTAEYLAS H
//
