ID D7B7J7_NOCDD Unreviewed; 164 AA.
AC D7B7J7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=Ndas_3995 {ECO:0000313|EMBL:ADH69392.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH69392.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH69392.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP002040; ADH69392.1; -; Genomic_DNA.
DR RefSeq; WP_013154999.1; NC_014210.1.
DR AlphaFoldDB; D7B7J7; -.
DR STRING; 446468.Ndas_3995; -.
DR KEGG; nda:Ndas_3995; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_2_11; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000002219; Chromosome 1.
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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 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:UP000002219}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 164 AA; 18126 MW; 312B2DB4F1A51708 CRC64;
MSDLDEIPVT LIDGRETTFG EWSGKVRLVV NVASRCGYTP QYERLEKLQH RYGDRGFTVL
GVPSNQFLQE FGSEEKIAEY CSATWGVTFP MTAKAKLNGK QQHPLYAALS SAEDEDGKAG
KVKWNFEKFL VLPDGAVHRF RSSTEPDDPG ITALIEKALP GDAG
//
