ID   NADB_CAUCR              Reviewed;         511 AA.
AC   Q9A4C3;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 52.
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=CC_2913;
OS   Caulobacter crescentus (Caulobacter vibrioides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=155892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24875.1; -; Genomic_DNA.
DR   PIR; G87609; G87609.
DR   RefSeq; NP_421707.1; -.
DR   HSSP; P83223; 1D4D.
DR   GeneID; 942841; -.
DR   GenomeReviews; AE005673_GR; CC_2913.
DR   KEGG; ccr:CC_2913; -.
DR   NMPDR; fig|190650.1.peg.2887; -.
DR   TIGR; CC_2913; -.
DR   HOGENOM; Q9A4C3; -.
DR   OMA; Q9A4C3; AGCHYNN.
DR   BRENDA; 1.4.3.16; 2191.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   InterPro; IPR004112; Fum_Rdtase/Succ_DH_flav_C.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    511       L-aspartate oxidase.
FT                                /FTId=PRO_0000184381.
FT   NP_BIND      15     29       FAD (Potential).
FT   ACT_SITE    236    236       By similarity.
FT   ACT_SITE    255    255       By similarity.
SQ   SEQUENCE   511 AA;  51598 MW;  46B565ABC80B5EAF CRC64;
     MTQYRITFEG PVILGAGLAG LTAALSATTG AAKTALVLSP TPLASGCSSA WAQGGMAAAL
     SGDDSPALHA ADTIAAGAGL CDPQAVDLLT REGPQAVRDL AALGAPFDRK ADDGFVLSLE
     AAHSAARVAR VGGDGAGAAI MAAVIAAVRA TPGIEVRENA RARRLLQDAN GRVVGVLADV
     DGALVEIRST AVILATGGVG GLYAVTTTPA QVRGEGLGLA ALAGAMIADP EFVQFHPTAI
     DIGRDPAPLA TEALRGEGAI LRNADGKAFM ADYHPAKELA PRDVVARALH AERAAGRGAF
     LDATAAVGAH FPHEFPAVFE ACMSAGIDPR RQMIPVTPAV HYHMGGVATD LDGRASLPGL
     YAAGECASTG VQGANRLASN SLLEAAVFGA RAGRAAAAEG ATGGPPVSLE PLPDLPDAAL
     QGLRKAMSRD AGVIRDADGL TRLLGEIETL EAGHGQGPIL VAARLIVTAA LAREESRGGH
     CRIDFPATDP VGVRTFVTLD GREPGLRYAA E
//