GenomeNet

Database: UniProt
Entry: A0A1I5GR30_9FLAO
LinkDB: A0A1I5GR30_9FLAO
Original site: A0A1I5GR30_9FLAO 
ID   A0A1I5GR30_9FLAO        Unreviewed;       194 AA.
AC   A0A1I5GR30;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=SAMN05421741_1483 {ECO:0000313|EMBL:SFO38377.1};
OS   Paenimyroides ummariense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Paenimyroides.
OX   NCBI_TaxID=913024 {ECO:0000313|EMBL:SFO38377.1, ECO:0000313|Proteomes:UP000199036};
RN   [1] {ECO:0000313|Proteomes:UP000199036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-12 {ECO:0000313|Proteomes:UP000199036};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOVI01000048; SFO38377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5GR30; -.
DR   STRING; 913024.SAMN05421741_1483; -.
DR   OrthoDB; 9789406at2; -.
DR   Proteomes; UP000199036; 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; 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; 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}.
FT   DOMAIN          32..194
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   194 AA;  22108 MW;  12E781B1ED21147A CRC64;
     MKYIFIASAV LALSCTKNQP ITEKPEVIME QQKNVDPIYQ FKVKDITGGE FNLADLKGKK
     VLIVNTASKC GLTPQFEQLE ELYQKYKDQN FVIIGFPTND FMSQDPGTNE EIAEFCKLNY
     GVTFPMMSKI VVKGDNKEPL YQYLTQKDKN GLGDFDVEWN FQKFLINEEG KLAKVINPKV
     SPTDAEITNW IEGK
//
DBGET integrated database retrieval system