(data stored in ACNUC7421 zone)

SWISSPROT: Q0SKG6_RHOJR

ID   Q0SKG6_RHOJR            Unreviewed;       330 AA.
AC   Q0SKG6;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   SubName: Full=Xanthine dehydrogenase FAD-binding subunit {ECO:0000313|EMBL:ABG91970.1};
DE            EC=1.17.1.4 {ECO:0000313|EMBL:ABG91970.1};
GN   Name=xdhB {ECO:0000313|EMBL:ABG91970.1};
GN   OrderedLocusNames=RHA1_ro00134 {ECO:0000313|EMBL:ABG91970.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG91970.1, 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).
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DR   EMBL; CP000431; ABG91970.1; -; Genomic_DNA.
DR   RefSeq; WP_011593455.1; NC_008268.1.
DR   STRING; 101510.RHA1_ro00134; -.
DR   PRIDE; Q0SKG6; -.
DR   EnsemblBacteria; ABG91970; ABG91970; RHA1_ro00134.
DR   GeneID; 4217573; -.
DR   KEGG; rha:RHA1_ro00134; -.
DR   PATRIC; fig|101510.16.peg.159; -.
DR   eggNOG; ENOG4105DIP; Bacteria.
DR   eggNOG; COG1319; LUCA.
DR   HOGENOM; HOG000244727; -.
DR   KO; K11178; -.
DR   OMA; AFTYERA; -.
DR   OrthoDB; POG091H0E2Y; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; SSF55447; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; Q0SKG6.
DR   SWISS-2DPAGE; Q0SKG6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Oxidoreductase {ECO:0000313|EMBL:ABG91970.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN        1    222       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   330 AA;  34960 MW;  0A6A6FFE7C11A171 CRC64;
     MIPFDYERAT DVDSAVATVT GDPRASFLAG GTNLVDHMKL GVARPHLLVD VSRLPLGDVV
     ELPDGGLRIG AAVRNSDLAA HDVVRARYPM LSRALLSGAS GQLRNLATTA GNLLQRTRCV
     YFQDVTTPCN KREPGTGCSA IGGYVRYHAI LGASEHCVAV HPSDMAVAMT ALDGVVVVRG
     ADGERRIPLS EFYRLPGDRP DRDTVLAHGD LVTAVELPPP PSGNRSAYRK VRDRASFAFA
     VVSVAAELTI GDTSITSARV ALGGVAHRPW RATLAEEVLV GSPPTEATYT EAAAAELAAA
     QPLPGNEFKV ALTRRVLASV LRSLAEEARR
//

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