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Database: UniProt
Entry: A0A1Y0FYU5_9GAMM
LinkDB: A0A1Y0FYU5_9GAMM
Original site: A0A1Y0FYU5_9GAMM 
ID   A0A1Y0FYU5_9GAMM        Unreviewed;       178 AA.
AC   A0A1Y0FYU5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=CBR65_15085 {ECO:0000313|EMBL:ARU28662.1};
OS   Cellvibrio sp. PSBB006.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU28662.1, ECO:0000313|Proteomes:UP000196143};
RN   [1] {ECO:0000313|EMBL:ARU28662.1, ECO:0000313|Proteomes:UP000196143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB006 {ECO:0000313|EMBL:ARU28662.1,
RC   ECO:0000313|Proteomes:UP000196143};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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; CP021382; ARU28662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0FYU5; -.
DR   KEGG; cell:CBR65_15085; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000196143; 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:SF44; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000196143};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..178
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012440310"
FT   DOMAIN          11..178
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   178 AA;  19577 MW;  931A204F969E54E6 CRC64;
     MKPQAFLGGL ALLLLSGPLL AACPDYLQGE YRQLHSTKDI DLCKLTEGKP VLVVNTASHC
     GYTKQFTGLE ALSQKYRDEG LVVVGFASDD FNQEAKNEEE AATICFENFG VTFTMFAPTH
     VRGDEANPLF KSLAKATSEP KWNFNKYLLD KDGKIIEHFG SSVKPEDKAL TGAIEKLL
//
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