ID   NADB_YERPE              Reviewed;         533 AA.
AC   Q8ZD80; Q0WDI1;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   24-JAN-2024, entry version 138.
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=YPO2710, y1289, YP_2514;
OS   Yersinia pestis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM84863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS62712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAL21329.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL590842; CAL21329.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE009952; AAM84863.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS62712.1; ALT_INIT; Genomic_DNA.
DR   PIR; AF0330; AF0330.
DR   RefSeq; YP_002347657.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZD80; -.
DR   SMR; Q8ZD80; -.
DR   STRING; 214092.YPO2710; -.
DR   PaxDb; 214092-YPO2710; -.
DR   DNASU; 1146236; -.
DR   EnsemblBacteria; AAS62712; AAS62712; YP_2514.
DR   KEGG; ype:YPO2710; -.
DR   KEGG; ypj:CH55_1456; -.
DR   KEGG; ypk:y1289; -.
DR   KEGG; ypl:CH46_2394; -.
DR   KEGG; ypm:YP_2514; -.
DR   KEGG; ypv:BZ15_818; -.
DR   KEGG; ypw:CH59_3595; -.
DR   PATRIC; fig|214092.21.peg.3151; -.
DR   eggNOG; COG0029; Bacteria.
DR   HOGENOM; CLU_014312_3_0_6; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IBA:GO_Central.
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:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
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-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   NCBIfam; TIGR00551; nadB; 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   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 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..533
FT                   /note="L-aspartate oxidase"
FT                   /id="PRO_0000184406"
FT   ACT_SITE        290
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         16..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         45..52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         375
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         391..392
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   SITE            121
FT                   /note="Important in orienting the L-aspartate substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
SQ   SEQUENCE   533 AA;  59294 MW;  909E8BFEB15BD2BD CRC64;
     MQSSSEHISD VLIIGSGAAG LSLALRLAPH CKVTVLSKGP LNEGATFYAQ GGIAAVFDET
     DSISSHVDDT LIAGAGLCDK EAVEFIASNA RSCVQWLIDQ GVLFDTETSA NGEERYHLTR
     EGGHSHRRIL HTADATGKEV ETTLVGKASN HPNISVKERC NAVDLITSNK IGLAGTKRVV
     GAYVWNRELE KVETFRAKAV VLATGGAAKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF
     NQFHPTCLFH PQARNFLLTE ALRGEGAYLK RPDGSRFMLD FDPRGELAPR DIVARAIDHE
     MKRLGADCMY LDISHKPTDF VMQHFPMIYE KLLSLGIDLT KEAIPIVPAA HYTCGGVMVD
     QHGRTDLDGL YAIGEVSYTG LHGANRMASN SLLECLVYGW SAAEDILTRL PTAKLAKHLP
     DWDESRVDNS DERVVIQHNW HELRLFMWDY VGIVRTTKRL ERALRRINTL QQEIDEYYAN
     FRISNNLLEL RNLVQVAELI VRCAMERKES RGLHYTLDYP DQIENPQPTI LHP
//