ID F0SL40_RUBBR Unreviewed; 205 AA.
AC F0SL40;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=Plabr_3326 {ECO:0000313|EMBL:ADY60923.1};
OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Rubinisphaera.
OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY60923.1, ECO:0000313|Proteomes:UP000006860};
RN [1] {ECO:0000313|Proteomes:UP000006860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC {ECO:0000313|Proteomes:UP000006860};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL Submitted (FEB-2011) 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; CP002546; ADY60923.1; -; Genomic_DNA.
DR AlphaFoldDB; F0SL40; -.
DR STRING; 756272.Plabr_3326; -.
DR KEGG; pbs:Plabr_3326; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_0; -.
DR Proteomes; UP000006860; 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:UP000006860};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..205
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003260549"
FT DOMAIN 40..204
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 205 AA; 22935 MW; 3187D8804CF112E1 CRC64;
MIYDGATRFS TSFTSPERRP MKYFALCTLL SCLTFLSADA AEKSEVLDHK AQTLAGKEVD
LSKYDGKVVL IVNVASRCGA TPQYEALQRL HETYKDRGLV VLGFPCNQFG RQEPGTAAEI
REFCTANYGV TFDMFSKIDV NGPDASPLYQ HLTSEETNPE FAGNVRWNFE KFLISKDGKI
VNRFRTGVQP NSDVVIAAIE KELRK
//
