ID   NADB_CLOPE              Reviewed;         439 AA.
AC   Q8XNE2;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=L-aspartate oxidase {ECO:0000250|UniProtKB:P10902};
DE            Short=LASPO {ECO:0000250|UniProtKB:P10902};
DE            EC=1.4.3.16 {ECO:0000250|UniProtKB:P10902};
DE   AltName: Full=Quinolinate synthase B;
GN   Name=nadB; OrderedLocusNames=CPE0395;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the
CC       first step in the de novo biosynthesis of NAD(+).
CC       {ECO:0000250|UniProtKB:P10902}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC         Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC         Evidence={ECO:0000250|UniProtKB:P10902};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC         Evidence={ECO:0000250|UniProtKB:P10902};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P10902};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P10902};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000250|UniProtKB:P10902}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10902}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BA000016; BAB80101.1; -; Genomic_DNA.
DR   RefSeq; WP_003471363.1; NC_003366.1.
DR   AlphaFoldDB; Q8XNE2; -.
DR   SMR; Q8XNE2; -.
DR   STRING; 195102.gene:10489651; -.
DR   EnsemblBacteria; BAB80101; BAB80101; BAB80101.
DR   KEGG; cpe:CPE0395; -.
DR   HOGENOM; CLU_014312_3_1_9; -.
DR   OMA; DSPDIHY; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR005288; NadB.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR42716; PTHR42716; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..439
FT                   /note="L-aspartate oxidase"
FT                   /id="PRO_0000184383"
FT   ACT_SITE        267
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         12..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         41..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         204
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         352
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         368..369
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   SITE            111
FT                   /note="Important in orienting the L-aspartate substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
SQ   SEQUENCE   439 AA;  49236 MW;  D89A50E494E5F5C7 CRC64;
     MKRVADVLIV GSGVAGLYAS LNLREDLEII MVSKKSVNLC NSSLAQGGIA VARGKEDFQS
     FIEDTLKAGK YENNIDSVRV LVEESMDNIN KLIDLGANFE KDENGVLFTK EGAHEINRIV
     YHKDITGKHV EDILLENVKR RKNIKIIEDC EMVDIYHRGN RCIGALFNKD GQDLSIYAKV
     VILATGGIGG LFKKSTNERI ITGDSIGVAI RNNIEIKDLS YIQIHPTAFF SKKSEEKRFL
     ISESVRGEGG KLLNCNGERF VDELLPRDIV SKKIYEEMKK TNSNNVFLDV SFMEKSFLQN
     RFPNIYNKCL EEGIDISKEP IPVAPAQHYF MGGIKVDLNG KTSMENLYAF GETSCTGVHG
     ANRLASNSLL EALVFSRRGA LEINSYIDNL ELIIEERECE DLDKYRLLNR KILIDEICRL
     RGDIKDELVT CGGECKKSS