(data stored in ACNUC7421 zone)

SWISSPROT: Q13RU6_PARXL

ID   Q13RU6_PARXL            Unreviewed;       212 AA.
AC   Q13RU6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   SubName: Full=1-Cys peroxiredoxin {ECO:0000313|EMBL:ABE33193.1};
DE            EC=1.11.1.15 {ECO:0000313|EMBL:ABE33193.1};
GN   ORFNames=Bxe_B2802 {ECO:0000313|EMBL:ABE33193.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33193.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33193.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33193.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR   EMBL; CP000271; ABE33193.1; -; Genomic_DNA.
DR   RefSeq; WP_011490567.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13RU6; -.
DR   STRING; 266265.Bxe_B2802; -.
DR   EnsemblBacteria; ABE33193; ABE33193; Bxe_B2802.
DR   GeneID; 4006599; -.
DR   KEGG; bxb:DR64_5131; -.
DR   KEGG; bxe:Bxe_B2802; -.
DR   PATRIC; fig|266265.5.peg.4891; -.
DR   eggNOG; ENOG4105D3R; Bacteria.
DR   eggNOG; COG0450; LUCA.
DR   HOGENOM; HOG000022346; -.
DR   OMA; IRFHAWL; -.
DR   OrthoDB; POG091H026G; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
DR   PRODOM; Q13RU6.
DR   SWISS-2DPAGE; Q13RU6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE33193.1};
KW   Peroxidase {ECO:0000313|EMBL:ABE33193.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        3    159       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   212 AA;  23802 MW;  1FE81049ED95ED52 CRC64;
     MSLRLGDIAP DFERQSSVGP IRFHEWLGDS WGVLFSHPAD FTPVCTTELG LTAKLAGEFE
     KRNVKTIALS VDSAESHKEW IKDINETQAA NVGFPILADG DRKVSELYDM IHPNANETLT
     VRSLFVIDPK KKVRLIITYP ASTGRNFDEV LRVIDSLQLT DSHSVATPGN WKQGDDVVIV
     PSLKDEEIIK QKFPKGYKAL RPYLRMTPQP NK
//

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