ID A0A1P8UX02_9RHOB Unreviewed; 171 AA.
AC A0A1P8UX02;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
DE Flags: Precursor;
GN ORFNames=Ga0080574_TMP3573 {ECO:0000313|EMBL:APZ53907.1};
OS Salipiger abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1250539 {ECO:0000313|EMBL:APZ53907.1, ECO:0000313|Proteomes:UP000187059};
RN [1] {ECO:0000313|EMBL:APZ53907.1, ECO:0000313|Proteomes:UP000187059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2014 {ECO:0000313|EMBL:APZ53907.1,
RC ECO:0000313|Proteomes:UP000187059};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (APR-2016) 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; CP015093; APZ53907.1; -; Genomic_DNA.
DR RefSeq; WP_076702918.1; NZ_CP015093.1.
DR AlphaFoldDB; A0A1P8UX02; -.
DR STRING; 1250539.Ga0080574_TMP3573; -.
DR KEGG; paby:Ga0080574_TMP3573; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000187059; 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; 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:UP000187059};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..171
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013134472"
FT DOMAIN 14..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 171 AA; 18719 MW; FDA693BEAD9F07F1 CRC64;
MIRILATLAA LTLALPALAA QSFAFDSIDG GTLSLDRWTG QPVLVVNTAS RCGFTPQYDG
LQALYDRYRD RGLVVLAVPS DDFRQELGSE EEVKAFCELN FALDLPMTTI TRVTGEDAHP
LYRWLAAQGF EPGWNFNKAL IGPDGGFVEG WGATTRPLSE PIVTRIEALL E
//
