ID A0A0N1BVH8_9PROT Unreviewed; 179 AA.
AC A0A0N1BVH8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=IP70_04690 {ECO:0000313|EMBL:KPF87530.1};
OS alpha proteobacterium AAP38.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF87530.1, ECO:0000313|Proteomes:UP000037884};
RN [1] {ECO:0000313|EMBL:KPF87530.1, ECO:0000313|Proteomes:UP000037884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP38 {ECO:0000313|EMBL:KPF87530.1,
RC ECO:0000313|Proteomes:UP000037884};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF87530.1}.
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DR EMBL; LJHR01000005; KPF87530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1BVH8; -.
DR STRING; 1523418.IP70_04690; -.
DR PATRIC; fig|1523418.3.peg.4016; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000037884; 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 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..179
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005867470"
FT DOMAIN 19..177
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 179 AA; 19296 MW; D668E4904E6B8B9D CRC64;
MLALAGGLAM MGVMGMTGTA QAANAYDFGF TAIEGSPLKF DAYRGKTVLV VNTASMCGYT
PQYKGLQALW EKYKDKGLVV LGVPSNDFGG QEPGSAKEIK EFCEVNFAID FPMTTKEPVK
GPNAHPMYKW LADQKGEPKW NFHKYLIGTD GKLIEAYGSK VTPDSAELTA AIEKALPKG
//
