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Database: UniProt
Entry: A0A223NTW0_9SPHI
LinkDB: A0A223NTW0_9SPHI
Original site: A0A223NTW0_9SPHI 
ID   A0A223NTW0_9SPHI        Unreviewed;       166 AA.
AC   A0A223NTW0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=MuYL_1405 {ECO:0000313|EMBL:ASU33303.1};
OS   Mucilaginibacter xinganensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU33303.1, ECO:0000313|Proteomes:UP000215002};
RN   [1] {ECO:0000313|EMBL:ASU33303.1, ECO:0000313|Proteomes:UP000215002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU33303.1,
RC   ECO:0000313|Proteomes:UP000215002};
RG   Henan University of Science and Technology;
RA   You X.;
RT   "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; CP022743; ASU33303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223NTW0; -.
DR   KEGG; muc:MuYL_1405; -.
DR   OrthoDB; 9789406at2; -.
DR   Proteomes; UP000215002; Chromosome.
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   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; 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:UP000215002}.
FT   DOMAIN          1..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   166 AA;  18925 MW;  15C0C13E11234D0F CRC64;
     MVDNSIYQFN IKQLNGEELN LSEYKDKVLL IVNTASQCGF TPQLSELAAL KSEFAGKDFE
     ILAFPSNDFG GQEPLDGKEL VTFCERQNVN YPVFEKIRVR GPYADPLYKF FADKKQNGKL
     SSVPRWNFHK FLINKSGQVT DFFYPFTKPN ASKIKKQIAR LLAPGK
//
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