ID A0A2D1U457_9SPHI Unreviewed; 170 AA.
AC A0A2D1U457;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=CPT03_07845 {ECO:0000313|EMBL:ATP56390.1};
OS Pedobacter ginsengisoli.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=363852 {ECO:0000313|EMBL:ATP56390.1, ECO:0000313|Proteomes:UP000223749};
RN [1] {ECO:0000313|EMBL:ATP56390.1, ECO:0000313|Proteomes:UP000223749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T01R-27 {ECO:0000313|EMBL:ATP56390.1,
RC ECO:0000313|Proteomes:UP000223749};
RA Weon H.-Y., Lee S.A., Sang M.K., Song J.;
RT "Whole genome of Pedobacter ginsengisoli T01R-27 isolated from tomato
RT rhizosphere.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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; CP024091; ATP56390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D1U457; -.
DR KEGG; pgs:CPT03_07845; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000223749; Chromosome.
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 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.
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:UP000223749}.
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 170 AA; 19301 MW; F593718CF09ECC2E CRC64;
MNTLLILLSL LFTPPTKNVY DFSFKTIDGK EIKLSKFKGK KILIVNTASK CGFTPQYEDL
EKLQKQYGKN VVLIGFPAGN FGGQELATNS EIKEFCTGKY NVTFLLSEKS SVKGDDISPL
FKYLTSQENP DFTGDIQWNF EKFLINEKGQ LVHRFRSKVK PLDEAITKNL
//
