ID M3GVC5_9LEPT Unreviewed; 142 AA.
AC M3GVC5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=LEP1GSC188_3618 {ECO:0000313|EMBL:EMF80841.1};
OS Leptospira weilii serovar Topaz str. LT2116.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1088540 {ECO:0000313|EMBL:EMF80841.1, ECO:0000313|Proteomes:UP000011770};
RN [1] {ECO:0000313|EMBL:EMF80841.1, ECO:0000313|Proteomes:UP000011770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2116 {ECO:0000313|EMBL:EMF80841.1,
RC ECO:0000313|Proteomes:UP000011770};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMF80841.1}.
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DR EMBL; AHOR02000046; EMF80841.1; -; Genomic_DNA.
DR AlphaFoldDB; M3GVC5; -.
DR Proteomes; UP000011770; 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 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.
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:UP000011770}.
FT ACT_SITE 18
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 142 AA; 16295 MW; 24C8C280F7F734D8 CRC64;
MEDYKGKVLL IVNTASECAF TPQYAGLQSL YGKYKTEGLE ILGFPCDQFK HQEPGSDETI
KNFCQKNYGV EFPIFKKIDV NGDNAHPVFR FLRKKASGFF GNSIKWNFTK FLVDKQGNVI
KRYSPITTPE KIEKVIQDLL KK
//
