(data stored in SCRATCH zone)

SWISSPROT: Q3IDD8_PSEHT

ID   Q3IDD8_PSEHT            Unreviewed;       163 AA.
AC   Q3IDD8;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   OrderedLocusNames=PSHAa0062 {ECO:0000313|EMBL:CAI85171.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85171.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85171.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; CR954246; CAI85171.1; -; Genomic_DNA.
DR   RefSeq; WP_011326789.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDD8; -.
DR   STRING; 326442.PSHAa0062; -.
DR   EnsemblBacteria; CAI85171; CAI85171; PSHAa0062.
DR   GeneID; 32565748; -.
DR   KEGG; pha:PSHAa0062; -.
DR   eggNOG; ENOG4108V06; Bacteria.
DR   eggNOG; COG0386; LUCA.
DR   HOGENOM; HOG000277054; -.
DR   KO; K00432; -.
DR   OMA; VDRYYPT; -.
DR   OrthoDB; POG091H02C9; -.
DR   BioCyc; PHAL326442:GJIU-64-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
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   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 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;
DR   PRODOM; Q3IDD8.
DR   SWISS-2DPAGE; Q3IDD8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000499,
KW   ECO:0000313|EMBL:CAI85171.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU000499,
KW   ECO:0000313|EMBL:CAI85171.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   ACT_SITE     36     36       {ECO:0000256|PIRSR:PIRSR000303-1}.
SQ   SEQUENCE   163 AA;  18344 MW;  EEC0A91CCBA66A60 CRC64;
     MHKFHQLSAT SLQGNTINFS EFAGKVVLIV NTASKCGFTY QYESLQALHN KYASQGLVIL
     GFPCNQFNQQ EPGDAQQIEQ GCLINYGVNF LMAAKVEVNG EHAHPVFRYL KSTQPGFLTR
     KIKWNFTKFL IAADGSPIKR YAPFTKPEKL ELTIQKALQQ SNK
//

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