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Database: UniProt
Entry: A0A0Q8A5P2_9ACTN
LinkDB: A0A0Q8A5P2_9ACTN
Original site: A0A0Q8A5P2_9ACTN 
ID   A0A0Q8A5P2_9ACTN        Unreviewed;       164 AA.
AC   A0A0Q8A5P2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=ASD66_07640 {ECO:0000313|EMBL:KQZ76136.1};
OS   Nocardioides sp. Root151.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ76136.1, ECO:0000313|Proteomes:UP000051274};
RN   [1] {ECO:0000313|EMBL:KQZ76136.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ76136.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ76136.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ76136.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQZ76136.1}.
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DR   EMBL; LMGG01000001; KQZ76136.1; -; Genomic_DNA.
DR   RefSeq; WP_056684399.1; NZ_LMGG01000001.1.
DR   AlphaFoldDB; A0A0Q8A5P2; -.
DR   Proteomes; UP000051274; 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; 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; 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:UP000051274}.
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   164 AA;  17535 MW;  FDD355F4B4DF5FF4 CRC64;
     MSILDAPIAR LDGTSATLGE ITGGKPALLV NVASKCGLTP QYTALEQLHE QYADRGFSVI
     GIPCNQFGGQ EPGTSDEIAE FCSATYGVTF PMTEKVEVNG DGRHPIYAEL AKVPDEEGEA
     GDVQWNFEKF LIAADGKVIS RFRPGVTPDD QRLVDGVERL TSGS
//
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