ID A0A1A6C2R6_9GAMM Unreviewed; 158 AA.
AC A0A1A6C2R6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=Thpro_023112 {ECO:0000313|EMBL:OBS08862.1};
OS Acidihalobacter prosperus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS08862.1, ECO:0000313|Proteomes:UP000029273};
RN [1] {ECO:0000313|EMBL:OBS08862.1, ECO:0000313|Proteomes:UP000029273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS08862.1,
RC ECO:0000313|Proteomes:UP000029273};
RX PubMed=25342676;
RA Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S.,
RA Watkin E.;
RT "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and Halotolerant
RT 'Thiobacillus prosperus' Type Strain DSM 5130.";
RL Genome Announc. 2:0-0(2014).
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:OBS08862.1}.
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DR EMBL; JQSG02000006; OBS08862.1; -; Genomic_DNA.
DR RefSeq; WP_038091406.1; NZ_JQSG02000006.1.
DR AlphaFoldDB; A0A1A6C2R6; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000029273; 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:UP000029273}.
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 158 AA; 17673 MW; 552D0B8FBCD40E92 CRC64;
MDLYEIALRT IDGRACTLAD YRGRVLLVVN VASRCAFTPQ YAALEALYRR HVARGLSVLG
FPCDQFGQQE PGDEAAIADF CASRYAVSFP MFAKTTVNGE EAHPLFRCLT AAAPGWLGGP
VRWNFTKFLI DREGRVYRRY APQTAPARLE RAIRRLLG
//
