ID A0A0M2H0R3_9MICO Unreviewed; 167 AA.
AC A0A0M2H0R3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=gpx1 {ECO:0000313|EMBL:KJL39787.1};
GN ORFNames=RS82_03996 {ECO:0000313|EMBL:KJL39787.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL39787.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL39787.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL39787.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL39787.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYJA01000041; KJL39787.1; -; Genomic_DNA.
DR RefSeq; WP_045302659.1; NZ_JYJA01000041.1.
DR AlphaFoldDB; A0A0M2H0R3; -.
DR PATRIC; fig|69370.6.peg.4054; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000034098; 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 PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 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.
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:UP000034098}.
FT ACT_SITE 41
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 167 AA; 18358 MW; CC37BC7C46B622E5 CRC64;
MTEATITDLR EIPFTTADGG TATLSEYGDQ VLLVVNVASK CGLTPQYEQL EQLQRAYADR
GFTVLGFPCN QFMGQEPGSM DEILEYCSVT WGVTFPVFDK VKVNGPGAAA VYKALKKSRD
AEGKKGPIVW NFEKFVLTPE GGVHRFRPNV KPDDPAIVEV IEANLPR
//