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Database: UniProt/TrEMBL
Entry: Q7WL13_BORBR
LinkDB: Q7WL13_BORBR
Original site: Q7WL13_BORBR 
ID   Q7WL13_BORBR            Unreviewed;       469 AA.
AC   Q7WL13;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   14-MAY-2014, entry version 61.
DE   SubName: Full=Putative oxidoreductase;
GN   OrderedLocusNames=BB1937;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- SIMILARITY: Contains FAD-binding PCMH-type domain.
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DR   EMBL; BX640442; CAE32434.1; -; Genomic_DNA.
DR   RefSeq; NP_888482.1; NC_002927.3.
DR   ProteinModelPortal; Q7WL13; -.
DR   STRING; 257310.BB1937; -.
DR   EnsemblBacteria; CAE32434; CAE32434; BB1937.
DR   GeneID; 2659536; -.
DR   KEGG; bbr:BB1937; -.
DR   PATRIC; 21137170; VBIBorBro124907_1962.
DR   HOGENOM; HOG000230995; -.
DR   KO; K00102; -.
DR   OMA; GQGFEWA; -.
DR   OrthoDB; EOG6RZB40; -.
DR   BioCyc; BBRO257310:BB1937-MONOMER; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Complete proteome.
SQ   SEQUENCE   469 AA;  50946 MW;  BA5F88FF0135900C CRC64;
     MNAPQPAEAL RRPVPPACLD ALKARFGDRL STAHAVREHH GRDESPYPPM LPDAVVFAHS
     TEDVAEVARL CNEHRVPLIP YGAGSSLEGH LLAIQGGISL DLSQMNQVLA VNAEDLTVTV
     QAGVTRKQLN EEIRDTGLFF PIDPGADASL GGMAATRASG TNAVRYGTMR ENVMALTVVT
     ADGRVLRTAG RARKSSAGYD LTRIFVGSEG TLGIITEVTV RLYPQPEAVS AAICNFPSLD
     AAVQSVIEII QMGVPVARVE FMDEASVRAV NMHSKLTLRE TPLLLFEFHG SPAGVQEQAE
     TVQAITAEHG GMDFEWAERP EDRSRLWTAR HNAYFAGLQL RPGCRASTTD VCVPISRLAD
     CVRETVDELE RASFPYTIVG HVGDGNFHVL MLLDADSPQE WQESETINHN LVRRAIAADG
     TCTGEHGVGL HKMQFMAEEH GEEALALMRS LKHAFDPNNI LNPGKIIAW
//
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