ID   NADB_XYLFT              Reviewed;         512 AA.
AC   Q87D19;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 37.
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=PD_0868;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22421331; PubMed=12533478;
RX   DOI=10.1128/JB.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B.,
RA   Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H.,
RA   Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R.,
RA   Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.,
RA   Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J.,
RA   Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E.,
RA   Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M.,
RA   Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V.,
RA   da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T.,
RA   Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D.,
RA   de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G.,
RA   Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C.,
RA   Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's
RT   disease and citrus variegated chlorosis strains of Xylella
RT   fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(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; AE009442; AAO28735.1; -; Genomic_DNA.
DR   RefSeq; NP_779086.1; -.
DR   HSSP; P10902; 1CHU.
DR   GeneID; 1143590; -.
DR   GenomeReviews; AE009442_GR; PD_0868.
DR   KEGG; xft:PD0868; -.
DR   HOGENOM; Q87D19; -.
DR   BioCyc; XFAS183190:PD_0868-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    512       L-aspartate oxidase.
FT                                /FTId=PRO_0000184405.
FT   NP_BIND      13     27       FAD (Potential).
FT   ACT_SITE    233    233       By similarity.
FT   ACT_SITE    252    252       By similarity.
SQ   SEQUENCE   512 AA;  53938 MW;  581222938C6BA53C CRC64;
     MAKIVDCFAD RPIIVGSGLA GLIAALTISP EPSVLVTRSA LGAETSSAWA QGGMSVSLSP
     DDNPSLHLAD TLAAGDGLCD AVAAESIILE ALDAFHVLQH FGIHFDQDSN GHLALGLEAA
     HSRRRIVHVG GDRSGTAIVQ ALTACVLNDP SITVLEGLEA RHILMADNVV CGLLLANPTS
     EIVLPSSRIL LATGGIGGLY DATTNPVNNF GQGIAMAARA GAVLADMEFV QFHPTALHCH
     NRPLALVSEA VRGEGAVLIN ERGERFMADI PGAELAARNI VAQAISAEIT RGGQVFLDAR
     QALGARFSTR FPTITALCHK VGIDPVHMPI PVCPAAHYHM GGIATDRQGR SSIPGLWVAG
     EAASTGLHGA NRLASNSLLE AVVMGTRAAR DITSHNTPHP LGTIPITPKK PDTTLIRPIV
     SQCLGVLRHA ADMHRAIAAL LPFVEGEEES SDPAIVALLI AIFAHLRTES RGAHARTDFP
     LKHDTTQRRN MTLEDVLEIA HSRIAQRKEK IS
//