ID A0A180F0F5_9BACT Unreviewed; 179 AA.
AC A0A180F0F5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=bsaA {ECO:0000313|EMBL:OAV65842.1};
GN ORFNames=Barb6XT_02225 {ECO:0000313|EMBL:OAV65842.1};
OS Bacteroidales bacterium Barb6XT.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1633202 {ECO:0000313|EMBL:OAV65842.1, ECO:0000313|Proteomes:UP000078346};
RN [1] {ECO:0000313|EMBL:OAV65842.1, ECO:0000313|Proteomes:UP000078346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barb6XT {ECO:0000313|EMBL:OAV65842.1,
RC ECO:0000313|Proteomes:UP000078346};
RA Tai V., Carpenter K.J., Weber P.K., Nalepa C.A., Perlman S.J.,
RA Keeling P.J.;
RT "Genomic and NanoSIMS analyses of nitrogen-fixing bacterial ectosymbionts
RT of a protist inhabiting a wood-eating cockroach.";
RL Submitted (DEC-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:OAV65842.1}.
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DR EMBL; LBCW01000179; OAV65842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180F0F5; -.
DR PATRIC; fig|1633202.3.peg.1117; -.
DR Proteomes; UP000078346; 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:UP000078346};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..179
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008108439"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 179 AA; 19882 MW; B9A52470A058A45C CRC64;
MKASLLLFAA AALSFSAAAQ NKNFHDFTVQ TIDGDNFSLS ELKGKKVLVV NVASKCGLTP
QYEDLQALYA KYGNDKFVVV GFPANNFGTQ EPGSNAEIKA FCADTYDVTF PMMAKISVKG
DDIAPLYQWL TKKGENGKED AEVTWNFQKF LIDEEGNWVA FFPPKTKPFA QEIIDRIEE
//