ID A0A0U5IFC0_9GAMM Unreviewed; 180 AA.
AC A0A0U5IFC0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=THIOKS12130013 {ECO:0000313|EMBL:CRI64821.1};
OS Thiocapsa sp. KS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=610332 {ECO:0000313|EMBL:CRI64821.1, ECO:0000313|Proteomes:UP000198608};
RN [1] {ECO:0000313|Proteomes:UP000198608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|Proteomes:UP000198608};
RA Luecker S.;
RL Submitted (MAY-2015) 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; CVPF01000128; CRI64821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5IFC0; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000198608; 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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF44; 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; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..180
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006859963"
FT DOMAIN 13..180
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 180 AA; 20177 MW; 9B0A46E8A0CA3F7F CRC64;
MRMFVLLPML GALLLPAAAS AACAPALDFE MRRLAGDETV RLCDAYQGKV ILAVNTASKC
GFTGQYEGLE ALYREYGERG LVVLGFPSND FANQEPGSEK EIRDFCRLTY SVEFPMFEKV
QVKKGAAAPF FEYLAAETGV YPEWNFYKYL IDRDGKVVEV FPSRTGPESE KMIQVIERLL
//
