ID Q6MQX6_BDEBA Unreviewed; 182 AA.
AC Q6MQX6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=btuE {ECO:0000313|EMBL:CAE77982.1};
GN OrderedLocusNames=Bd0326 {ECO:0000313|EMBL:CAE77982.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE77982.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE77982.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; BX842646; CAE77982.1; -; Genomic_DNA.
DR RefSeq; WP_011162923.1; NC_005363.1.
DR AlphaFoldDB; Q6MQX6; -.
DR STRING; 264462.Bd0326; -.
DR KEGG; bba:Bd0326; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_2_7; -.
DR Proteomes; UP000008080; Chromosome.
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: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; 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:UP000008080}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 182 AA; 19907 MW; F86B2794EDC0A831 CRC64;
MSTLNHIEFN TADGKKATLA DYSGKVLLVV NVASECGLTP QYEGLEKIHQ KYESQGLRVL
AFPANEFGAQ EPGSNEQIQE FCRTQFGVKF PVFAKMVVKG EGQHPLYQQL TTLQPAAQQV
PGGKLKSVLE EHGLLSGGPS DIMWNFEKFL IGKSGNVVAR FAPDMTPEDP TIVKAIEAEL
AR
//
