ID   NADB_BACSU              Reviewed;         531 AA.
AC   P38032;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-NOV-2008, entry version 64.
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=BSU27870;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=93186710; PubMed=8444804;
RA   Sun D., Setlow P.L.;
RT   "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis
RT   nadB gene and a nifS-like gene, both of which are essential for NAD
RT   biosynthesis.";
RL   J. Bacteriol. 175:1423-1432(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; M98822; AAA21614.1; -; Genomic_DNA.
DR   EMBL; Z99118; CAB14747.1; -; Genomic_DNA.
DR   PIR; C47071; C47071.
DR   RefSeq; NP_390665.1; -.
DR   HSSP; P10902; 1CHU.
DR   GeneID; 938051; -.
DR   GenomeReviews; AL009126_GR; BSU27870.
DR   KEGG; bsu:BSU27870; -.
DR   NMPDR; fig|224308.1.peg.2790; -.
DR   SubtiList; BG10867; nadB.
DR   HOGENOM; P38032; -.
DR   BioCyc; BSUB224308:BSU2783-MON; -.
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; IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
DR   InterPro; IPR005288; NadB.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    531       L-aspartate oxidase.
FT                                /FTId=PRO_0000184380.
FT   NP_BIND       7     21       FAD (Potential).
FT   ACT_SITE    226    226       By similarity.
FT   ACT_SITE    245    245       By similarity.
SQ   SEQUENCE   531 AA;  58239 MW;  AF592AC55EC51259 CRC64;
     MSKKTIAVIG SGAAALSLAA AFPPSYEVTV ITKKSVKNSN SVYAQGGIAA AYAKDDSIEA
     HLEDTLYAGC GHNNLAIVAD VLHDGKMMVQ SLLERGFPFD RNERGGVCLG REGAHSYNRI
     FHAGGDATGR LLIDYLLKRI NSKIKLIENE TAADLLIEDG RCIGVMTKDS KGRLKVRHAD
     EVVLAAGGCG NLFLHHTNDL TVTGDGLSLA YRAGAELTDL EFTQFHPTLL VKNGVSYGLV
     SEAVRGEGGC LVDENGRRIM AERHPLGDLA PRDIVSRVIH EEMAKGNRVY IDFSAISDFE
     TRFPTITAIC EKAGIDIHSG KIPVAPGMHF LMGGVSVNRW GETTVPGLYA IGETACSGLH
     GANRLASNSL LEALVFGKRA AEHIIQKPVY NRQYQSGLET SVFYEVPDIE GHELQSKMTS
     HMSILREQSS LIELSIWLHT LPFQEVNVKD ITIRQMELSH LWQTAKLMTF SALLREESRG
     AHFRTDFPHA EVSWQGRQIV HTKKGTKIRK NEGIWNNESF TAEKITESLF S
//