ID C3J8L3_POREA Unreviewed; 185 AA.
AC C3J8L3;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=POREN0001_0531 {ECO:0000313|EMBL:EEN83472.1};
OS Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 /
OS NCTC 13058 / HG 370).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=553175 {ECO:0000313|EMBL:EEN83472.1, ECO:0000313|Proteomes:UP000004295};
RN [1] {ECO:0000313|EMBL:EEN83472.1, ECO:0000313|Proteomes:UP000004295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370
RC {ECO:0000313|Proteomes:UP000004295};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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:EEN83472.1}.
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DR EMBL; ACNN01000007; EEN83472.1; -; Genomic_DNA.
DR RefSeq; WP_004332585.1; NZ_ACNN01000007.1.
DR AlphaFoldDB; C3J8L3; -.
DR STRING; 553175.POREN0001_0531; -.
DR GeneID; 84819338; -.
DR eggNOG; COG0386; Bacteria.
DR Proteomes; UP000004295; 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; 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:UP000004295}.
FT DOMAIN 1..185
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 185 AA; 21340 MW; 4755842848AC973C CRC64;
MTTIYDFSLT DAQGNDVSLS EYKGKVLLIV NTATKCGFTP QYEKLEEMYR DMRAEGFEII
DIPCNQFKNQ APGSDEEITQ FCRMNFGTEF PQFKKSDVNG ENELPLYTWL KSQKGFEGFD
KENSLSPKLE RMLDKADPNW RSKSDIKWNF TKFLIDRNGN VIARFEPTKD MGKVAELVKK
ALEAK
//
