ID D3E061_METRM Unreviewed; 179 AA.
AC D3E061;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Glutathione peroxidase GpxA {ECO:0000313|EMBL:ADC47785.1};
DE EC=1.11.1.9 {ECO:0000313|EMBL:ADC47785.1};
GN Name=gpxA {ECO:0000313|EMBL:ADC47785.1};
GN OrderedLocusNames=mru_1935 {ECO:0000313|EMBL:ADC47785.1};
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC47785.1, ECO:0000313|Proteomes:UP000008680};
RN [1] {ECO:0000313|EMBL:ADC47785.1, ECO:0000313|Proteomes:UP000008680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1
RC {ECO:0000313|Proteomes:UP000008680};
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926}.
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DR EMBL; CP001719; ADC47785.1; -; Genomic_DNA.
DR RefSeq; WP_012956733.1; NC_013790.1.
DR AlphaFoldDB; D3E061; -.
DR SMR; D3E061; -.
DR STRING; 634498.mru_1935; -.
DR GeneID; 8771605; -.
DR KEGG; mru:mru_1935; -.
DR PATRIC; fig|634498.28.peg.1935; -.
DR eggNOG; arCOG00310; Archaea.
DR HOGENOM; CLU_029507_2_2_2; -.
DR OrthoDB; 74692at2157; -.
DR Proteomes; UP000008680; Chromosome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
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; 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; 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:0000313|EMBL:ADC47785.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ADC47785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008680}.
FT DOMAIN 1..179
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 179 AA; 20448 MW; D223D6DAB58CC40F CRC64;
MSIYDFEVKD INGNMVSLKE YEGQVLLIVN SATECGFTPQ YNELTQIFDE LNEEGFTILD
FPCNQFGKQA PGTGEEIAEA CRATFLVQYP IFEKIEVNGE NEEPLYTYLK SEQPFVDITG
EDAERLKGIL ESINPDYMDS NDIKWNFTKF LVDREGNVVA RFEPTQSLDD VKAQIKELL
//
