ID V4P3J1_9CAUL Unreviewed; 181 AA.
AC V4P3J1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=ABENE_15995 {ECO:0000313|EMBL:ESQ88547.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ88547.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ88547.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ88547.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ88547.1}.
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DR EMBL; AWGB01000037; ESQ88547.1; -; Genomic_DNA.
DR RefSeq; WP_018081530.1; NZ_AWGB01000037.1.
DR AlphaFoldDB; V4P3J1; -.
DR STRING; 1121022.GCA_000376105_01863; -.
DR PATRIC; fig|1121022.4.peg.3253; -.
DR eggNOG; COG0386; Bacteria.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000017837; 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; 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:UP000017837}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 181 AA; 19887 MW; 9BCCCADB71394297 CRC64;
MTDIYNIPLK RIDGQPTTLE GFKGKVLLAV NVASKCGLTP QYEALEALYR EKSGDGLEIL
GFPANNFLSQ EPGTDEDIVS FCSTTYDVTF PLFSKISVVG ADKHPLYDVF TKAQPNAVSA
GPMRERLEKF GIPVSPEGEV LWNFEKFLIG KNGDVVERFA PDVTADDPRL VAAIERELAK
T
//
