ID   A7NN76_ROSCS            Unreviewed;       167 AA.
AC   A7NN76;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 80.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   OrderedLocusNames=Rcas_2947 {ECO:0000313|EMBL:ABU59008.1};
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Roseiflexineae; Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU59008.1, ECO:0000313|Proteomes:UP000000263};
RN   [1] {ECO:0000313|EMBL:ABU59008.1, ECO:0000313|Proteomes:UP000000263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00691}.
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DR   EMBL; CP000804; ABU59008.1; -; Genomic_DNA.
DR   RefSeq; WP_012121432.1; NC_009767.1.
DR   AlphaFoldDB; A7NN76; -.
DR   STRING; 383372.Rcas_2947; -.
DR   KEGG; rca:Rcas_2947; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_2_2_0; -.
DR   OrthoDB; 9809733at2; -.
DR   Proteomes; UP000000263; Chromosome.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   FunFam; 3.40.30.10:FF:000010; Glutathione 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   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF78; 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.
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:UP000000263}.
FT   DOMAIN          1..159
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   167 AA;  18916 MW;  96BC0D81BA04B76A CRC64;
     MGIYDITANR IDGTPQPLSD YRNRVLLIVN VASKCGFAPQ YAGLETLYRR YRDEGFVVLG
     FPCDQFAGQE YDDPNAIQQF CTRNYGVSFP IFEKVDVNGP NTHPLFALLK AEKPGLLGIQ
     TIPWNFTKFL VDRQGKVRRR YAPTDTPEKI ERDIAALLRQ PTAITAQ
//