ID A0A1Q8YGC2_9BURK Unreviewed; 161 AA.
AC A0A1Q8YGC2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=BLL52_1696 {ECO:0000313|EMBL:OLP06950.1};
OS Rhodoferax antarcticus ANT.BR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP06950.1, ECO:0000313|Proteomes:UP000185911};
RN [1] {ECO:0000313|EMBL:OLP06950.1, ECO:0000313|Proteomes:UP000185911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANT.BR {ECO:0000313|EMBL:OLP06950.1,
RC ECO:0000313|Proteomes:UP000185911};
RA Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M.,
RA Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J.,
RA Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J.,
RA Sattley M.;
RT "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple
RT nonsulfur bacterium from an Antarctic microbial mat.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLP06950.1}.
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DR EMBL; MSYM01000011; OLP06950.1; -; Genomic_DNA.
DR RefSeq; WP_075586098.1; NZ_MSYM01000011.1.
DR AlphaFoldDB; A0A1Q8YGC2; -.
DR STRING; 81479.RA876_02920; -.
DR Proteomes; UP000185911; 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 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; PS00763; GLUTATHIONE_PEROXID_2; 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:UP000185911}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 161 AA; 17171 MW; 310DB88A5174B0E2 CRC64;
MTTIYDFDAL SIDGKPVPLK NFEGKAMLIV NTASACGFTP QFAGLETLHE TYGAKGLVVL
GFPCNQFGAQ DSGTNGEIAQ FCQRNYGVSF PMMAKIEVNG SAAHPLYQWL SAEAPGLLGS
KSIKWNFTKF LVGKNGAVIK RYAPTDTPAG MAKDIKAALA L
//
