ID Q1GTX8_SPHAL Unreviewed; 158 AA.
AC Q1GTX8;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=Sala_1178 {ECO:0000313|EMBL:ABF52894.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF52894.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF52894.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF52894.1; -; Genomic_DNA.
DR RefSeq; WP_011541479.1; NC_008048.1.
DR AlphaFoldDB; Q1GTX8; -.
DR STRING; 317655.Sala_1178; -.
DR KEGG; sal:Sala_1178; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_5; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000006578; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006578}.
FT DOMAIN 1..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 158 AA; 17711 MW; 0C2337E0D89CB580 CRC64;
MGLYDLSAKL PGGGTQSLAD YRGKVLLIVN TASKCGFTPQ YEGLEELYRD YRDRGFEILA
FPCNQFGAQE PGDAEEIRTF CSLTYDVSFP LMAKIDVNGD DADPIFKHLK KEKTGLLGSA
IKWNFTKFLV DRDGKVVSRH APTTRPEQLR KEIEELLG
//
