ID A0A0R2DVL5_9LACO Unreviewed; 155 AA.
AC A0A0R2DVL5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=FC86_GL000018 {ECO:0000313|EMBL:KRN04570.1};
OS Holzapfeliella floricola DSM 23037 = JCM 16512.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Holzapfeliella.
OX NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN04570.1, ECO:0000313|Proteomes:UP000051378};
RN [1] {ECO:0000313|EMBL:KRN04570.1, ECO:0000313|Proteomes:UP000051378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN04570.1,
RC ECO:0000313|Proteomes:UP000051378};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN04570.1}.
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DR EMBL; AYZL01000008; KRN04570.1; -; Genomic_DNA.
DR RefSeq; WP_056974210.1; NZ_BBAW01000008.1.
DR AlphaFoldDB; A0A0R2DVL5; -.
DR STRING; 1423744.FC86_GL000018; -.
DR PATRIC; fig|1423744.4.peg.20; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000051378; 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 InterPro; IPR013766; Thioredoxin_domain.
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; 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:UP000051378}.
FT DOMAIN 1..155
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 155 AA; 17603 MW; B16703F4C2643177 CRC64;
MATIYDFSLT EMNGQPINLS DYKEKVLLIV NTASKCGLAP QLETIEQLYQ SYKDTGFAVI
GLPSNQFHQE LENDQETSDY CQRHYGVTFP MTQKVKLNGD DADPLINYLK EQSGKGAIKW
NFTKFLIGKD GQLIHRYAPM TSPKKMETEI VKALE
//
