GenomeNet

Database: UniProt
Entry: M4S3J9_9SPHN
LinkDB: M4S3J9_9SPHN
Original site: M4S3J9_9SPHN 
ID   M4S3J9_9SPHN            Unreviewed;       202 AA.
AC   M4S3J9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=G432_14480 {ECO:0000313|EMBL:AGH50615.1};
OS   Sphingomonas sp. MM-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH50615.1, ECO:0000313|Proteomes:UP000011816};
RN   [1] {ECO:0000313|EMBL:AGH50615.1, ECO:0000313|Proteomes:UP000011816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM-1 {ECO:0000313|EMBL:AGH50615.1};
RX   PubMed=23682148;
RA   Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT   Bacterium Sphingomonas sp. Strain MM-1.";
RL   Genome Announc. 1:E00247-13(2013).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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; CP004036; AGH50615.1; -; Genomic_DNA.
DR   RefSeq; WP_015459592.1; NC_020561.1.
DR   AlphaFoldDB; M4S3J9; -.
DR   STRING; 745310.G432_14480; -.
DR   KEGG; sphm:G432_14480; -.
DR   PATRIC; fig|745310.14.peg.3015; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_1_0_5; -.
DR   Proteomes; UP000011816; 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; IPR036249; Thioredoxin-like_sf.
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; 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:UP000011816};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..202
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004057197"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   202 AA;  21615 MW;  954E68F28C5C1914 CRC64;
     MHKKWTLGGA AVIAIGAMAA VGYAQFPSVP DTPPMAAAEA QKHTAWDFDL TAIDGAPLPM
     KKFKGEVVLL VNTASMCGFT PQYEGLQKVQ DTYARRGFTI VGVPSGNFKN QEYGSNSEIA
     AFCKTKAVKF PLAEKSDVVG PNALPIYRWA AAKLGPQNTP KWNFHKYLIG RDGKLIAAFG
     TRTDPTDPKV TGAIEAALKA KG
//
DBGET integrated database retrieval system