GenomeNet

Database: UniProt
Entry: A0A0L9UP79_PHAAN
LinkDB: A0A0L9UP79_PHAAN
Original site: A0A0L9UP79_PHAAN 
ID   A0A0L9UP79_PHAAN        Unreviewed;       170 AA.
AC   A0A0L9UP79;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=HKW66_Vig0161690 {ECO:0000313|EMBL:KAG2375677.1},
GN   LR48_Vigan06g001600 {ECO:0000313|EMBL:KOM44710.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM44710.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN   [2] {ECO:0000313|EMBL:KOM44710.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:KOM44710.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAG2375677.1, ECO:0000313|Proteomes:UP000743370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAG2375677.1};
RA   Xiang H.;
RT   "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL   Submitted (MAY-2020) 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; JABFOF010000010; KAG2375677.1; -; Genomic_DNA.
DR   EMBL; CM003376; KOM44710.1; -; Genomic_DNA.
DR   RefSeq; XP_017427734.1; XM_017572245.1.
DR   AlphaFoldDB; A0A0L9UP79; -.
DR   STRING; 3914.A0A0L9UP79; -.
DR   EnsemblPlants; KOM44710; KOM44710; LR48_Vigan06g001600.
DR   GeneID; 108335986; -.
DR   Gramene; KOM44710; KOM44710; LR48_Vigan06g001600.
DR   KEGG; var:108335986; -.
DR   OMA; ENTSPFY; -.
DR   OrthoDB; 177208at2759; -.
DR   Proteomes; UP000053144; Chromosome 6.
DR   Proteomes; UP000743370; 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; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF27; GLUTATHIONE PEROXIDASE 8-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:UP000053144}.
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;  19067 MW;  615F66FF08AC899C CRC64;
     MSTGSSKDPK SVYDFSVKDA KGDVVDLSTY EGKVLLIINV ASKCGLTNSN YTELNELYAK
     YKDEGLEILA FPCNQFGEQE PESNDKIVDF VCTRFKSEFP IFDKIEVNGG NSAPLYKFLK
     SGKWGIFGDD IQWNFAKFVV DKKGQVVGRY YPTTSPLSLE RDIRQLLGIS
//
DBGET integrated database retrieval system