ID   NADB_XYLFA              Reviewed;         512 AA.
AC   Q9PC57;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 129.
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=XF_1924;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
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 = iminosuccinate + H2O2;
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; AE003849; AAF84730.1; -; Genomic_DNA.
DR   PIR; A82621; A82621.
DR   RefSeq; WP_010894390.1; NC_002488.3.
DR   AlphaFoldDB; Q9PC57; -.
DR   SMR; Q9PC57; -.
DR   STRING; 160492.XF_1924; -.
DR   KEGG; xfa:XF_1924; -.
DR   eggNOG; COG0029; Bacteria.
DR   HOGENOM; CLU_014312_3_2_6; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000000812; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; ISS:UniProtKB.
DR   GO; GO:0034628; P:'de novo' NAD+ biosynthetic process from L-aspartate; IEA:TreeGrafter.
DR   FunFam; 3.90.700.10:FF:000002; L-aspartate oxidase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-dep_OxRdtase_2_FAD-bd.
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   NCBIfam; TIGR00551; nadB; 1.
DR   NCBIfam; NF005701; PRK07512.1; 1.
DR   PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR   PANTHER; PTHR42716:SF2; L-ASPARTATE OXIDASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..512
FT                   /note="L-aspartate oxidase"
FT                   /id="PRO_0000184404"
FT   ACT_SITE        278
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         17..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         46..53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         377..378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   SITE            118
FT                   /note="Important in orienting the L-aspartate substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
SQ   SEQUENCE   512 AA;  53965 MW;  DD2C9C15FC7A61C6 CRC64;
     MAEIVDCFAD RPIIVGSGLA GLIAALTMSP EPSVLVTRSA LGAETSSAWA QGGMSVSLSP
     DDNPSLHLAD TLAAGDGLCD AVAAESIILE ALDAFHVLQH FGIHFDQDSN GHLALGLEAA
     HSRRRIVHVG GDRSGTAIVQ ALTACVLNDP SITVLEGLEA RHILMADNVV CGLLLANPTS
     EIVLPSSRIL LATGGIGGLY DATTNPVSNF GQGIAMAARA GAVLADMEFV QFHPTALHCH
     NRPLALVSEA VRGEGAVLIN ERGERFMADI PGAELAARNI VAQAISAEIT RGGQVFLDAR
     QALGARFSTR FPTITALCHK VGIDPVHMPI PVCPAAHYHM GGIAIDHQGR SSIPGLWVAG
     EAASTGLHGA NRLASNSLLE AVVMGTRAAR DITFHNTPHP LGTIPITPKK PDTTLIRPIV
     SQCLGVLRHA ADMHRAIAAL LPFVEGEEES SDPAIVALLI AIFAYLRTES RGAHARTDFP
     LKHDTTQRRH MTLEDVLEIA HSCVAQRKEK IS
//