ID I3UC15_ADVKW Unreviewed; 160 AA.
AC I3UC15;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=TKWG_11795 {ECO:0000313|EMBL:AFK62553.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62553.1};
RN [1] {ECO:0000313|EMBL:AFK62553.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WT001 {ECO:0000313|EMBL:AFK62553.1};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
RN [2] {ECO:0000313|EMBL:AFK62553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WT001 {ECO:0000313|EMBL:AFK62553.1};
RA Alam M., Pyne P., Roy C., Ali A., Mandal A., Chakraborty S., Ghosh W.;
RT "Whole genome sequence of Advenella kashmirensis and comparative genomics
RT of non-pathogenic and pathogenic members of Alcaligenaceae.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP003555; AFK62553.1; -; Genomic_DNA.
DR RefSeq; WP_014750644.1; NC_017964.1.
DR AlphaFoldDB; I3UC15; -.
DR STRING; 1036672.TKWG_11795; -.
DR KEGG; aka:TKWG_11795; -.
DR HOGENOM; CLU_029507_2_2_4; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000005267; 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; IPR029760; GPX_CS.
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; PS00763; GLUTATHIONE_PEROXID_2; 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}.
FT DOMAIN 1..160
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 160 AA; 18141 MW; D844A5C20179A84E CRC64;
MSDFYSMNVT LQDGSQLPLS SLRDKVVLVV NVASRCGFTP QYTGLQRLHE QYRDQGLVVL
AFPCNQFGSQ EPGTDQEIQD FCELNFGVTF ALARKTEVNG PHTHPVFAWL KKEKPGLLGI
QSIKWNFTKF LVGRDGQVRH RYAPTVKPQD IEQDIKEALK
//
