(data stored in SCRATCH zone)

SWISSPROT: Q3KJ69_PSEPF

ID   Q3KJ69_PSEPF            Unreviewed;       144 AA.
AC   Q3KJ69;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:ABA72187.1};
DE            EC=1.8.1.8 {ECO:0000313|EMBL:ABA72187.1};
GN   OrderedLocusNames=Pfl01_0443 {ECO:0000313|EMBL:ABA72187.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72187.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72187.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72187.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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DR   EMBL; CP000094; ABA72187.1; -; Genomic_DNA.
DR   RefSeq; WP_011332109.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0443; -.
DR   EnsemblBacteria; ABA72187; ABA72187; Pfl01_0443.
DR   KEGG; pfo:Pfl01_0443; -.
DR   eggNOG; ENOG4105K63; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000292979; -.
DR   KO; K03672; -.
DR   OMA; QRVDMIN; -.
DR   BioCyc; PFLU205922:G1G4S-448-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
DR   PRODOM; Q3KJ69.
DR   SWISS-2DPAGE; Q3KJ69.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000077-4};
KW   Oxidoreductase {ECO:0000313|EMBL:ABA72187.1};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR000077-4}.
FT   DOMAIN       27    144       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     68     71       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000077-4}.
SQ   SEQUENCE   144 AA;  15794 MW;  9AA01AD88C989BC2 CRC64;
     MTDPLLIPCP SCNGLNRIPA ERLNDHPKCG RCKSEVLLNK PFELKQGDYA SQIKGDLPLL
     VDVWADWCGP CKSFAPVFEQ AAAQLAGKCR LAKLDSEANQ QLSAQLGIRS IPSLILLRNG
     REVARQSGAF PLPQLMAWLR SQGI
//

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