ID I3C1B4_9FLAO Unreviewed; 170 AA.
AC I3C1B4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=JoomaDRAFT_0350 {ECO:0000313|EMBL:EIJ37407.1};
OS Galbibacter orientalis DSM 19592.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ37407.1, ECO:0000313|Proteomes:UP000004690};
RN [1] {ECO:0000313|EMBL:EIJ37407.1, ECO:0000313|Proteomes:UP000004690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ37407.1,
RC ECO:0000313|Proteomes:UP000004690};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL Submitted (FEB-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; JH651380; EIJ37407.1; -; Genomic_DNA.
DR RefSeq; WP_008616288.1; NZ_JH651380.1.
DR AlphaFoldDB; I3C1B4; -.
DR STRING; 926559.JoomaDRAFT_0350; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_1_10; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000004690; 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; 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:UP000004690}.
FT ACT_SITE 50
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 170 AA; 19336 MW; 33E338163385B0C1 CRC64;
MISFFGKAQE PVNPSASIYD ISINNIDGDK IDLGTYKGKK ILFVNVASEC GFTGQYEDLQ
KLYETYQENL MIIGVPCNQF GGQEPGTADE IKTFCEKNYG VEFLITEKVA VKGENQHPLY
AWLTKKSING LKDSTVKWNF QKYLVDEQGR FIDYYMSTTK PMSSKITKYL
//
