ID A0A0N0LZI7_9GAMM Unreviewed; 160 AA.
AC A0A0N0LZI7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=ADS77_11180 {ECO:0000313|EMBL:KPH62941.1};
OS Pseudoalteromonas porphyrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH62941.1, ECO:0000313|Proteomes:UP000037848};
RN [1] {ECO:0000313|EMBL:KPH62941.1, ECO:0000313|Proteomes:UP000037848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH62941.1,
RC ECO:0000313|Proteomes:UP000037848};
RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.;
RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14.";
RL Submitted (AUG-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:KPH62941.1}.
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DR EMBL; LHPH01000011; KPH62941.1; -; Genomic_DNA.
DR RefSeq; WP_054454461.1; NZ_LHPH01000011.1.
DR AlphaFoldDB; A0A0N0LZI7; -.
DR STRING; 187330.AMS58_11950; -.
DR PATRIC; fig|187330.3.peg.4365; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000037848; 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; 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}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 160 AA; 17941 MW; 3A5B6F17855EB8CE CRC64;
MNDFHQLSAT NLQGQTFDFS NLEGKVVLII NTASKCGFTP QYEGLQQLHA KYAEQGLVII
GFPCNQFGQQ EPGNAKDIEQ GCLINYGVDF VMMGKVDVNG EHAHPVFRHL KSALPGFLSR
KIKWNFTKFL IGRNGEPIKR FAPFTKPQQI ESTIIKALKN
//
