ID A1AK90_PELPD Unreviewed; 161 AA.
AC A1AK90;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=Ppro_0123 {ECO:0000313|EMBL:ABK97760.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK97760.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK97760.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP000482; ABK97760.1; -; Genomic_DNA.
DR RefSeq; WP_011734074.1; NC_008609.1.
DR AlphaFoldDB; A1AK90; -.
DR STRING; 338966.Ppro_0123; -.
DR KEGG; ppd:Ppro_0123; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_7; -.
DR OrthoDB; 9809733at2; -.
DR Proteomes; UP000006732; Chromosome.
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; IPR029760; GPX_CS.
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; PS00763; GLUTATHIONE_PEROXID_2; 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:UP000006732}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 161 AA; 17739 MW; C448A447AB521A33 CRC64;
MPCMYDFEVQ TAGGECTSLA EYRGQVMLIV NTASKCGFTP QYKGLEALYR KYASRGFVVL
GFPCNQFGAQ EPGDMTEIKN FCSLTYDVTF PLFAKINVNG SDASPLFQYL KSAAKGVLGS
EAIKWNFTKF LVDRHGTVVG RYAPTTTPES LEKDIEAALH C
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