ID A0A1U7WVR3_NICSY Unreviewed; 170 AA.
AC A0A1U7WVR3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=LOC104227728 {ECO:0000313|RefSeq:XP_009778335.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009778335.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009778335.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009778335.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR RefSeq; XP_009778335.1; XM_009780033.1.
DR AlphaFoldDB; A0A1U7WVR3; -.
DR STRING; 4096.A0A1U7WVR3; -.
DR GeneID; 104227728; -.
DR KEGG; nsy:104227728; -.
DR eggNOG; KOG1651; Eukaryota.
DR OrthoDB; 177208at2759; -.
DR Proteomes; UP000189701; Unplaced.
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; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF17; GLUTATHIONE PEROXIDASE 5-RELATED; 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; PS00763; GLUTATHIONE_PEROXID_2; 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:UP000189701}.
FT DOMAIN 6..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 170 AA; 19096 MW; 69E1B3C1AADBAC50 CRC64;
MGASKSVPQK SIHEFTVKDI KGKDVDLSMY KGKVLLVVNV ASKCGFTSTN YTQLTQLYNQ
YKDKGFEVLA FPCNQFLKQE PGTSQEAQEF ACTRFQAEYP IFQKVRVNGP DTAPVYKFLK
ASKGGFLGSR IKWNFTKFLV DKDGKVIRRY GSTTPPLSIK ADIEKAISEN
//
