(data stored in ACNUC7421 zone)

SWISSPROT: Q0SK30_RHOJR

ID   Q0SK30_RHOJR            Unreviewed;       454 AA.
AC   Q0SK30;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   SubName: Full=Probable dibenzothiophene desulfurziation enzyme {ECO:0000313|EMBL:ABG92106.1};
GN   OrderedLocusNames=RHA1_ro00270 {ECO:0000313|EMBL:ABG92106.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92106.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000337-1};
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DR   EMBL; CP000431; ABG92106.1; -; Genomic_DNA.
DR   RefSeq; WP_011593559.1; NC_008268.1.
DR   ProteinModelPortal; Q0SK30; -.
DR   STRING; 101510.RHA1_ro00270; -.
DR   PRIDE; Q0SK30; -.
DR   EnsemblBacteria; ABG92106; ABG92106; RHA1_ro00270.
DR   GeneID; 4217982; -.
DR   KEGG; rha:RHA1_ro00270; -.
DR   PATRIC; fig|101510.16.peg.298; -.
DR   eggNOG; ENOG4105CPU; Bacteria.
DR   eggNOG; ENOG410XNPZ; LUCA.
DR   HOGENOM; HOG000190807; -.
DR   OMA; CWNVVTS; -.
DR   OrthoDB; POG091H089O; -.
DR   BioCyc; RJOS101510:GJJ1-270-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR016215; NTA_MOA.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   PIRSF; PIRSF000337; NTA_MOA; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
PE   4: Predicted;
DR   PRODOM; Q0SK30.
DR   SWISS-2DPAGE; Q0SK30.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000337-1};
KW   FMN {ECO:0000256|PIRSR:PIRSR000337-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN       15    386       Bac_luciferase. {ECO:0000259|Pfam:
FT                                PF00296}.
FT   NP_BIND     225    228       FMN binding. {ECO:0000256|PIRSR:
FT                                PIRSR000337-1}.
FT   BINDING      56     56       FMN; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000337-
FT                                1}.
FT   BINDING     103    103       FMN. {ECO:0000256|PIRSR:PIRSR000337-1}.
SQ   SEQUENCE   454 AA;  50096 MW;  2BF5B24C1E9AEAA1 CRC64;
     MSPSRMHLAA FVTAGPGRPG GWRYPGSVPG WLSAGYYQNI ARTLEDARFD LVFFADILSV
     PDRFGGSPDS QLRNGALGSM RLDPLHVLSS MGAVTSHLGL AATVSTTYAQ PFTVARSFAT
     LDHLTEGRAA WNVVTSFQES EARNFNRDEQ FPRDQRYERA DEFLEVAGKL WDSWEDDALV
     LDTEQPLFAD PDRVHPIRHK GDWFTVQGPL NVPRPPQGYP VVIQAGASAK GKDFAARWSD
     VIFCSHASLE SAQDFYKEIK ERAAAHGRDP ESVKILPSIA PVVGATTAIA QQTFEELFDL
     VPPLGGLSTL AYHLDVDLST FPLDERLPDV EVPGVEGHYQ EVREMTEREG LTLRELGKRY
     GGRVEGGFIG TATEVADGLG EWFGQGACDG FMVQAPYQPG GFEDFTRHVV PELQKRGLFR
     KEYEGSNLRE NLGLPRVQSG EWANRVRRGA EAAL
//

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