ID   NADB_AQUAE              Reviewed;         510 AA.
AC   O66973;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
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=aq_777;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to
CC       iminoaspartate.
CC   -!- CATALYTIC ACTIVITY: L-aspartate + O(2) = iminosuccinate +
CC       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; AE000657; AAC06932.1; -; Genomic_DNA.
DR   PIR; B70368; B70368.
DR   RefSeq; NP_213534.1; -.
DR   HSSP; P10902; 1CHU.
DR   GeneID; 1193423; -.
DR   GenomeReviews; AE000657_GR; aq_777.
DR   KEGG; aae:aq_777; -.
DR   NMPDR; fig|224324.1.peg.549; -.
DR   HOGENOM; O66973; -.
DR   OMA; O66973; AGCHYNN.
DR   BioCyc; AAEO224324:AQ_777-MON; -.
DR   BRENDA; 1.4.3.16; 189781.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:EC.
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_DH_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    510       L-aspartate oxidase.
FT                                /FTId=PRO_0000184378.
FT   NP_BIND      20     34       FAD (Potential).
FT   ACT_SITE    234    234       By similarity.
FT   ACT_SITE    250    250       By similarity.
SQ   SEQUENCE   510 AA;  57793 MW;  B6D5AD83438D0C42 CRC64;
     MNYFLRFDTS LLPEEEAKVL ICGSGIGGLA TAISLKELGI EPLILTRGIG NTYYSQGGIA
     AAVLPDDSPY LHYCDTLRAG RYLNHELHTK LLTYEGIFRI LDLERWGVDF DKKNGFYETT
     LEGGHSKPRV LKVKDYTGRE IYTKLLKKTE ELGIKILHGE LQEIIIEENG VQGVIYSEEG
     SLKFIRTPLL ILATGGAASM YYYTSNPKKV RGDAIGIAFR MGATVKNPEF VQFHPTVLKG
     TNLLISEAVR GEGAILVNDR GERFVNELLP RDEVARAIYN QIKRGREVYL DLRPVAQKGI
     KIEERFPTIY SFLRERGYDP YREPVPIIPA AHYYIGGIEV DDRGRTSIQG LYAVGECSCT
     GIHGANRLAS NSLLEGVVFG HRTAYQVYLD LKILKPSKVN FRSERAGSDK PNLGIEELKK
     LMWNYVGLER DEEGLTYVKK RILSVLSQAK HWEPTPQNRQ LYDILLVALC TVEGALMRKE
     SRGVHYRKDY PTEREVYRRD TIITRDLFEL
//