ID A0A0C1IGV7_9BACT Unreviewed; 170 AA.
AC A0A0C1IGV7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=HY58_15260 {ECO:0000313|EMBL:KIC89724.1};
OS Flavihumibacter sp. ZG627.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC89724.1, ECO:0000313|Proteomes:UP000031400};
RN [1] {ECO:0000313|EMBL:KIC89724.1, ECO:0000313|Proteomes:UP000031400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZG627 {ECO:0000313|EMBL:KIC89724.1,
RC ECO:0000313|Proteomes:UP000031400};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter carbonis ZG627.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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:KIC89724.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPHF01000008; KIC89724.1; -; Genomic_DNA.
DR RefSeq; WP_039133615.1; NZ_JPHF01000008.1.
DR AlphaFoldDB; A0A0C1IGV7; -.
DR STRING; 1463156.HY58_15260; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000031400; Unassembled WGS sequence.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000031400}.
FT DOMAIN 11..170
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 49
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 170 AA; 18969 MW; 8A196A43002CBA39 CRC64;
MLKTLLVSLM VLASTGIYDF KVNTLDGKPL DLAQFKGKKM LIVNTASKCG YTKQYSDLQE
LYEKYGNKIA VIGFPANNFG QQEPGSNAEI GEFCKKNYGV KFPMAEKVSV KGGDIHPLFK
YLTEEAAKLG VEDPIKWNFT KFLIDENGKL IAVFPSKVKP TDPEITKYLN
//
