ID A0A1M7ND07_9FLAO Unreviewed; 195 AA.
AC A0A1M7ND07;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=SAMN05216269_110131 {ECO:0000313|EMBL:SHN01549.1};
OS Flavobacterium xinjiangense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=178356 {ECO:0000313|EMBL:SHN01549.1, ECO:0000313|Proteomes:UP000184092};
RN [1] {ECO:0000313|EMBL:SHN01549.1, ECO:0000313|Proteomes:UP000184092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.2749 {ECO:0000313|EMBL:SHN01549.1,
RC ECO:0000313|Proteomes:UP000184092};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRCL01000010; SHN01549.1; -; Genomic_DNA.
DR RefSeq; WP_073210013.1; NZ_FRCL01000010.1.
DR AlphaFoldDB; A0A1M7ND07; -.
DR STRING; 178356.SAMN05216269_110131; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000184092; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..195
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012432645"
FT DOMAIN 34..195
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 72
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 195 AA; 22135 MW; 96D9AB7064DD62C5 CRC64;
MKNLLLLTCS IMFLFSCQNQ AQTKKTKLNK SNTVMAKETI YQFKVEDLSG KIFDFASLKG
KKVMIVNTAS KCGLTPQYKD LEAIYKEYKD KGFVIVGFPA NNFASQEPGT NEEIATFCQL
NYGVTFPMMD KVSVKGDDMC AVYQFLTQKS KNGLQDSQVE WNFQKYLINE KGELEKVIAP
RTLVTDPEVL NWIKA
//