ID Q7WL13_BORBR Unreviewed; 469 AA.
AC Q7WL13;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 58.
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 1 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; VAILIDP; -.
DR ProtClustDB; CLSK920881; -.
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; FAD-binding_2; 1.
DR SUPFAM; SSF56176; FAD-binding_2; 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
//
