ID A0A258AFQ0_9BACT Unreviewed; 145 AA.
AC A0A258AFQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=B7Z21_00725 {ECO:0000313|EMBL:OYW69763.1};
OS Verrucomicrobiales bacterium 32-60-5.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales.
OX NCBI_TaxID=1970610 {ECO:0000313|EMBL:OYW69763.1, ECO:0000313|Proteomes:UP000219220};
RN [1] {ECO:0000313|EMBL:OYW69763.1, ECO:0000313|Proteomes:UP000219220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-60-5 {ECO:0000313|EMBL:OYW69763.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYW69763.1}.
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DR EMBL; NCDH01000055; OYW69763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258AFQ0; -.
DR Proteomes; UP000219220; 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:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..145
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012965908"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 145 AA; 15152 MW; C9081E0D44CD5226 CRC64;
MKLLTLASSL LLAVALSAAD APKSVYDVPL KDIDGKDTTL KAYAGKVLLI VNVASECGYT
PQYAGLQALH EKMSGKGLAV LGFPCNDFGG QEPGSEAEIK SFCSLNYKVT FPMFAKVAIK
GDAKHPLYAA LQSAAGGEVG VLIQE
//
