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Database: UniProt
Entry: J6HD84_9FIRM
LinkDB: J6HD84_9FIRM
Original site: J6HD84_9FIRM 
ID   J6HD84_9FIRM            Unreviewed;       180 AA.
AC   J6HD84;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=HMPREF1152_1714 {ECO:0000313|EMBL:EJU23040.1};
OS   Mogibacterium sp. CM50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX   NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU23040.1, ECO:0000313|Proteomes:UP000003142};
RN   [1] {ECO:0000313|EMBL:EJU23040.1, ECO:0000313|Proteomes:UP000003142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM50 {ECO:0000313|EMBL:EJU23040.1,
RC   ECO:0000313|Proteomes:UP000003142};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-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:EJU23040.1}.
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DR   EMBL; ALNL01000012; EJU23040.1; -; Genomic_DNA.
DR   RefSeq; WP_009643370.1; NZ_ALNL01000012.1.
DR   AlphaFoldDB; J6HD84; -.
DR   STRING; 936375.HMPREF1152_1714; -.
DR   eggNOG; COG0386; Bacteria.
DR   OrthoDB; 9809733at2; -.
DR   Proteomes; UP000003142; 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; 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; 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:UP000003142}.
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   180 AA;  20391 MW;  6660BEE25D74A709 CRC64;
     MSFYDYTVPA ADGSEISMKA YEGKVVLVVN TATGCGFTPQ YEPIEDMYEK YHDRGLEVLD
     IPCNQFAGQA PGSDDEIHEF CTLHYNTKFP QMKKSDVNGE NQLELYRFLK QEQGFQGLGK
     GLKATGLSLV VKKMDKDYKN NPDIKWNFTK FVVDRNGNVV ARFEPTAKME EVEKCVASLM
//
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