ID   NADB_MYCLE              Reviewed;         526 AA.
AC   Q49617; Q9CC64;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   16-JUN-2009, entry version 65.
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=ML1226; ORFNames=B1170_C1_167;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17059.1; Type=Frameshift; Positions=399;
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DR   EMBL; U00010; AAA17059.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL583921; CAC31607.1; ALT_INIT; Genomic_DNA.
DR   PIR; D87062; D87062.
DR   PIR; S72695; S72695.
DR   RefSeq; NP_301888.1; -.
DR   HSSP; P10902; 1CHU.
DR   GeneID; 910334; -.
DR   GenomeReviews; AL450380_GR; ML1226.
DR   KEGG; mle:ML1226; -.
DR   NMPDR; fig|272631.1.peg.760; -.
DR   Leproma; ML1226; -.
DR   HOGENOM; Q49617; -.
DR   OMA; Q49617; GAYIWNR.
DR   BioCyc; MLEP272631:ML1226-MON; -.
DR   BRENDA; 1.4.3.16; 808.
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; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
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   PRINTS; PR00368; FADPNR.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    526       L-aspartate oxidase.
FT                                /FTId=PRO_0000184388.
FT   NP_BIND      13     27       FAD (Potential).
FT   ACT_SITE    234    234       By similarity.
FT   ACT_SITE    257    257       By similarity.
SQ   SEQUENCE   526 AA;  54182 MW;  A90A6EC4332C248D CRC64;
     MAVPDWKHAA DVVVIGTGVA GLAAALAAHR AGRNVVVLTK ADQRRGETAT HYAQGGIAVV
     LPGSDDSVDA HASDTLAAGA GMCNLDTVYS IVAEGYHAVT ELVGYGARFD ESIPGRWAVT
     CEGGHSRRRI VHAGGDATGA EVQRALDHAA DVLDIRTSHL ALRVLHDGTV VNGVSVLNPN
     GWGIVSAPSV ILASGGLGHL YGATTNPEGS TGDGIALALW AGVAVSDLEF IQFHPTMLFA
     AGTGTGGRRP LVTEAIRGEG AILLDSKGNS VTSGVHPLGD LAPRDVVAAA IDARLKATGD
     SCVYLDARGI DGFASRFPTV TAACRTVGID PAREPIPVVP GAHYSCGGIV TDAYGQTELA
     GLFAAGEVAR TGMHGANRLA SNSLLEGLVV GGRAGRAAAA HAAAAGRAYV SKLEPVTHHA
     LKRRELQRVM SRDAAVMRNA AGLQRLSDTL AEAPIRHVTG RRDFEDVALT LTARAVAAAA
     LARNESRGCH HCTEYPDTAP EHARSTVIRL ADDQNLVRAE ALATVG
//