ID   NADB_MYCBO              Reviewed;         527 AA.
AC   P65500; O06595;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 27.
DE   RecName: Full=L-aspartate oxidase;
DE            Short=LASPO;
DE            EC=1.4.3.16;
DE   AltName: Full=Quinolinate synthetase B;
GN   Name=nadB; OrderedLocusNames=Mb1621;
OS   Mycobacterium bovis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to
CC       iminoaspartate.
CC   -!- CATALYTIC ACTIVITY: L-aspartate + H(2)O + O(2) = oxaloacetate +
CC       NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (oxidase route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       NadB subfamily.
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DR   EMBL; BX248339; CAD96289.1; -; Genomic_DNA.
DR   RefSeq; NP_855274.1; -.
DR   HSSP; P10902; 1CHU.
DR   GeneID; 1092510; -.
DR   GenomeReviews; BX248333_GR; Mb1621.
DR   KEGG; mbo:Mb1621; -.
DR   HOGENOM; P65500; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
DR   InterPro; IPR005288; NadB.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    527       L-aspartate oxidase.
FT                                /FTId=PRO_0000184390.
FT   NP_BIND      13     27       FAD (Potential).
FT   ACT_SITE    233    233       By similarity.
FT   ACT_SITE    254    254       By similarity.
SQ   SEQUENCE   527 AA;  53785 MW;  5494D354B107E5DA CRC64;
     MAGPAWRDAA DVVVIGTGVA GLAAALAADR AGRSVVVLSK AAQTHVTATH YAQGGIAVVL
     PDNDDSVDAH VADTLAAGAG LCDPDAVYSI VADGYRAVTD LVGAGARLDE SVPGRWALTR
     EGGHSRRRIV HAGGDATGAE VQRALQDAAG MLDIRTGHVA LRVLHDGTAV TGLLVVRPDG
     CGIISAPSVI LATGGLGHLY SATTNPAGST GDGIALGLWA GVAVSDLEFI QFHPTMLFAG
     RAGGRRPLIT EAIRGEGAIL VDRQGNSITA GVHPMGDLAP RDVVAAAIDA RLKATGDPCV
     YLDARGIEGF ASRFPTVTAS CRAAGIDPVR QPIPVVPGAH YSCGGIVTDV YGQTELLGLY
     AAGEVARTGL HGANRLASNS LLEGLVVGGR AGKAAAAHAA AAGRSRATSS ATWPEPISYT
     ALDRGDLQRA MSRDASMYRA AAGLHRLCDS LSGAQVRDVA CRRDFEDVAL TLVAQSVTAA
     ALARTESRGC HHRAEYPCTV PEQARSIVVR GADDANAVCV QALVAVC
//