ID B8KSK9_9GAMM Unreviewed; 161 AA.
AC B8KSK9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=gshPx {ECO:0000313|EMBL:EED36756.1};
GN ORFNames=NOR51B_2708 {ECO:0000313|EMBL:EED36756.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED36756.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
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; DS999411; EED36756.1; -; Genomic_DNA.
DR RefSeq; WP_009021498.1; NZ_DS999411.1.
DR AlphaFoldDB; B8KSK9; -.
DR STRING; 565045.NOR51B_2708; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_6; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000004699; 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; 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:UP000004699}.
FT DOMAIN 1..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 161 AA; 17716 MW; BE95DF87A1D29484 CRC64;
MGDIYDFSAT TADGSDVNLA DYRGKVLLIV NTASKCGFTP QYEGLEALRS DFSDRGFEIL
AFPCNQFGNQ EPGTEEEIVE FCSLNFSTTF PLFAKIDVNG SDAHPLYEHL KEQAPGVLGT
KSIKWNFTKF LVNSNGEVVK RYASKDKPAS IAKDIEALLE A
//
