(data stored in SCRATCH zone)

SWISSPROT: Q13RP6_PARXL

ID   Q13RP6_PARXL            Unreviewed;       418 AA.
AC   Q13RP6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   SubName: Full=Terephthalate 1,2-dioxygenase, alpha subunit {ECO:0000313|EMBL:ABE33243.1};
GN   ORFNames=Bxe_B2752 {ECO:0000313|EMBL:ABE33243.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33243.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33243.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33243.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., 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; ABE33243.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_B2752; -.
DR   DNASU; 4006532; -.
DR   EnsemblBacteria; ABE33243; ABE33243; Bxe_B2752.
DR   KEGG; bxe:Bxe_B2752; -.
DR   PATRIC; fig|266265.5.peg.4942; -.
DR   eggNOG; ENOG4105IS1; Bacteria.
DR   eggNOG; COG4638; LUCA.
DR   HOGENOM; HOG000150534; -.
DR   KO; K16319; -.
DR   OMA; FCKEEHG; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0044237; P:cellular metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   4: Predicted;
DR   PRODOM; Q13RP6.
DR   SWISS-2DPAGE; Q13RP6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Dioxygenase {ECO:0000313|EMBL:ABE33243.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE33243.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       43    157       Rieske. {ECO:0000259|PROSITE:PS51296}.
SQ   SEQUENCE   418 AA;  46337 MW;  90369D1D7D2779C4 CRC64;
     MRARRASITW PSEGLTRVPY ALFQDEGVYA DEQDAIFRGP NWSYLCLEAE VPNQGDFRST
     FVGDAPVVVT RDTDGEIYAF ENRCAHRGAM VCLEDQGNAR DFSCVYHAWT YSLQGDLVGV
     AFKDGIDGKG GMKPDFCTGD HGLRKLRVAT LHGLVFGSFS DDVPPLDEYL GEEIVERIAR
     VLENRKPVVL GRFTQMLPNN WKLYFENVKD SYHASILHLF FTTFQLNRLS QRGGIIVDPS
     GGHHVSYSAV DHAAEAAAQR KATSDYADQK IRSESEHRLE DTSVLAGVDE FGDGVTLQIL
     SVFPGFVLQQ IQNAIAVRQI LPRGTQQTEL NWTYLGFEDD TPELREMRLR QSNLVGPAGY
     VSMEDGCVGG FVQRGIEGAG DGRSVIEMGG DSAESSASRV TEASIRGFWK AYRNAMGY
//

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