ID L1MSM1_9BACT Unreviewed; 162 AA.
AC L1MSM1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 28-JUN-2023, entry version 36.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=HMPREF9999_00221 {ECO:0000313|EMBL:EKX93896.1};
OS Alloprevotella sp. oral taxon 473 str. F0040.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX93896.1, ECO:0000313|Proteomes:UP000010460};
RN [1] {ECO:0000313|EMBL:EKX93896.1, ECO:0000313|Proteomes:UP000010460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0040 {ECO:0000313|EMBL:EKX93896.1,
RC ECO:0000313|Proteomes:UP000010460};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKX93896.1}.
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DR EMBL; AMEK01000012; EKX93896.1; -; Genomic_DNA.
DR AlphaFoldDB; L1MSM1; -.
DR STRING; 1035197.HMPREF9999_00221; -.
DR PATRIC; fig|1035197.3.peg.188; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_10; -.
DR Proteomes; UP000010460; 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 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; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 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:UP000010460}.
FT DOMAIN 1..160
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 162 AA; 17892 MW; 82693BE196EEC911 CRC64;
MPHMIHDFST VTSKGAPYPL SQHKGQVLLI VNTASKCGFT PQFAELEQLY QQYKDQGLMI
LGFPCNQFAG QEPGSGSDAE AACQLNYGVT FPIMHKIKVN GSEADPIFQY LKSQAGGFLT
NAIKWNFTKF LISRDGTMIR RYAPITKPSK IAKDIEALLA QS
//
