ID A0A164C4G8_9MICO Unreviewed; 167 AA.
AC A0A164C4G8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=gpx1 {ECO:0000313|EMBL:KZE90949.1};
GN ORFNames=AVP41_00477 {ECO:0000313|EMBL:KZE90949.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE90949.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE90949.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE90949.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-2016) 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:KZE90949.1}.
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DR EMBL; LQGV01000001; KZE90949.1; -; Genomic_DNA.
DR RefSeq; WP_067160211.1; NZ_LQGV01000001.1.
DR AlphaFoldDB; A0A164C4G8; -.
DR STRING; 1775956.AVP41_00477; -.
DR PATRIC; fig|1775956.3.peg.477; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000076535; 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; 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; 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:UP000076535}.
FT ACT_SITE 41
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 167 AA; 18375 MW; 508C2DA2B519020A CRC64;
MADSSSVEIR SIPFHDAEGA EKTLADFGDG PVLIVNVASK CGLTPQYEQL EQLQREYGDR
GLRVLGFPCN QFMGQEPGSM EEILDYCAVT WGVSFPIMDK IRVNGSHAAP LYKALKKARN
HEGAKGPVMW NFEKFLLTPS GEVHRFRPQT KPDAPEVIAA IEASLPA
//
