ID W0RW10_9BACT Unreviewed; 161 AA.
AC W0RW10;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=J421_6208 {ECO:0000313|EMBL:AHG93743.1};
OS Gemmatirosa kalamazoonensis.
OG Plasmid 2 {ECO:0000313|EMBL:AHG93743.1, ECO:0000313|Proteomes:UP000019151}.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG93743.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG93743.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG93743.1,
RC ECO:0000313|Proteomes:UP000019151};
RC PLASMID=Plasmid 2 {ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP007130; AHG93743.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RW10; -.
DR KEGG; gba:J421_6208; -.
DR PATRIC; fig|861299.3.peg.6270; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_0; -.
DR InParanoid; W0RW10; -.
DR OrthoDB; 9809733at2; -.
DR Proteomes; UP000019151; Plasmid 2.
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 Plasmid {ECO:0000313|EMBL:AHG93743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT DOMAIN 1..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 161 AA; 18084 MW; C9D9C1690210F725 CRC64;
MPLPNLELTT ITGDIIPLAD YRGQVLLVVN VASKCGFTPQ YEGLEALHRR FHMRGFTVLG
FPCDQFGHQE PGDADEIQRF CSLTYDVTFP LFAKTDVNGP NAHPLWRELK RAKRGLLGSR
AIKWNFTKFL VDRDGTVRAR FAPNTTPAEL EPEVEALLAG R
//
