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Database: UniProt
Entry: A0A0B2BTB4_9ACTN
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Original site: A0A0B2BTB4_9ACTN 
ID   A0A0B2BTB4_9ACTN        Unreviewed;       160 AA.
AC   A0A0B2BTB4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=CLV56_0669 {ECO:0000313|EMBL:PJJ56461.1};
OS   Mumia flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Mumia.
OX   NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ56461.1, ECO:0000313|Proteomes:UP000230842};
RN   [1] {ECO:0000313|EMBL:PJJ56461.1, ECO:0000313|Proteomes:UP000230842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ56461.1,
RC   ECO:0000313|Proteomes:UP000230842};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-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:PJJ56461.1}.
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DR   EMBL; PGEZ01000001; PJJ56461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2BTB4; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000230842; 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   Reference proteome {ECO:0000313|Proteomes:UP000230842}.
FT   DOMAIN          1..159
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   160 AA;  17998 MW;  17EDCB8D52DE5E1D CRC64;
     MTSAYDFSAV DIDGNERSLS EFQGKAVLVV NTASKCGFTP QYEGLEELHR KYAEEGLVVL
     GFPCDQFGHQ EPGDAEEIKS FCSLTYDVTF PMFAKIDVNG KDAHPLYQWL RSERTGVLGD
     RIKWNFTKFL LDSDGQVVKR YGSRTTPEAL TGDIERLLND
//
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