ID   NADB_RHORU              Reviewed;         277 AA.
AC   Q59767;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
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;
DE   Flags: Fragment;
GN   Name=nadB;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UR1;
RX   PubMed=7721706; DOI=10.1128/jb.177.8.2157-2163.1995;
RA   Shelver D., Kerby R.L., He Y., Roberts G.P.;
RT   "Carbon monoxide-induced activation of gene expression in Rhodospirillum
RT   rubrum requires the product of cooA, a member of the cyclic AMP receptor
RT   protein family of transcriptional regulators.";
RL   J. Bacteriol. 177:2157-2163(1995).
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; U65510; AAC45129.1; -; Genomic_DNA.
DR   PIR; T51327; T51327.
DR   AlphaFoldDB; Q59767; -.
DR   SMR; Q59767; -.
DR   UniPathway; UPA00253; UER00326.
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; IMP:CACAO.
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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
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   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 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.
FT   CHAIN           <1..277
FT                   /note="L-aspartate oxidase"
FT                   /id="PRO_0000184398"
FT   REGION          142..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        23
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         122..123
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   NON_TER         1
SQ   SEQUENCE   277 AA;  28540 MW;  253364CE414F5204 CRC64;
     ILVDAQGRRF MTALDPAAEL APRDVVTRGV AAAIKAGKGA FLDARTALGA AFPQAFPTVY
     AACRASGIDP VRQPIPIAPA AHYHMGGVLT DSFGRTSIDG LWAVGEVACT GAHGANRLAS
     NSLLEAVVFA ARVAGDVGAA PLRRGWPPPA PPDLSPRPPP AEDAAAITRL RATMSARVGV
     IRDGQGLESA LATIETIAAG ARSPRLRAMT TAARLITAAA LARRESRGAH FRADYPATDP
     AQSHRATAPF GPLRTVPPHP AQSLGEGLAA PPMETRS