ID   NADB_PYRHO              Reviewed;         464 AA.
AC   O57765;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=PH0015;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA29083.1; -; Genomic_DNA.
DR   PIR; D71219; D71219.
DR   AlphaFoldDB; O57765; -.
DR   SMR; O57765; -.
DR   STRING; 70601.3256400; -.
DR   EnsemblBacteria; BAA29083; BAA29083; BAA29083.
DR   KEGG; pho:PH0015; -.
DR   eggNOG; arCOG00572; Archaea.
DR   OMA; DSPDIHY; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000000752; 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; 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.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN           1..464
FT                   /note="L-aspartate oxidase"
FT                   /id="PRO_0000184410"
FT   ACT_SITE        251
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         11..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         40..47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         332
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   BINDING         348..349
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
FT   SITE            105
FT                   /note="Important in orienting the L-aspartate substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10902"
SQ   SEQUENCE   464 AA;  51296 MW;  6D5504A7EFAD738D CRC64;
     MMEMRVGIVG GGLAGLTAAI ALAEKGFDVS IIGPRSTDSN SYLAQAGIAL PLLEGDSIRI
     HVLDTIKAGK YINDEEIVWN VISKSSEAHD FLTSHGVTFT GNELEGGHSY PRIFTIKSET
     GKHIIPILEK HARELDVNFI RGFVEEIGIN NGKLAGVFLQ GELLKFDAVV IAAGGFSGLY
     RFTAGVKNNI GLLIGDVALK GVPLRDMEFV QFHPTGFIGK RTYLITEAVR GAGAKLVTGD
     GERFVNELET RDIVARAIYM KMLEGKGVFL DARGIENFKD RFPYIYSVLR GEGINPEKDL
     IPITPVAHYT IGGISVDAFY RTRIKGLYAI GESACNGFHG ANRLASNSLL ECVVSGLEVA
     RTISREKPKR EVNDAPYSFN ELGDVDSIRE VLWNHAGIVR DEWSLREGLR KLKEIEVDER
     LKLVAKAVII SALKREESRG AHYRKDYPFM RKEFEHSSFF YPNV