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   16-JUN-2009, entry version 56.
DE   RecName: Full=L-aspartate oxidase;
DE            Short=LASPO;
DE            EC=1.4.3.16;
DE   AltName: Full=Quinolinate synthetase B;
GN   Name=nadB; OrderedLocusNames=PH0015;
OS   Pyrococcus horikoshii.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=53953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT3;
RX   MEDLINE=98344137; PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   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
CC       iminoaspartate.
CC   -!- CATALYTIC ACTIVITY: L-aspartate + O(2) = iminosuccinate +
CC       H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (oxidase route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       NadB subfamily.
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DR   EMBL; BA000001; BAA29083.1; -; Genomic_DNA.
DR   PIR; D71219; D71219.
DR   RefSeq; NP_142038.1; -.
DR   HSSP; P10902; 1CHU.
DR   GeneID; 1443917; -.
DR   GenomeReviews; BA000001_GR; PH0015.
DR   KEGG; pho:PH0015; -.
DR   NMPDR; fig|70601.1.peg.17; -.
DR   HOGENOM; O57765; -.
DR   OMA; O57765; NENCETS.
DR   BRENDA; 1.4.3.16; 74679.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004112; Fum_Rdtase/Succ_DH_flav_C.
DR   InterPro; IPR005288; NadB.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    464       L-aspartate oxidase.
FT                                /FTId=PRO_0000184410.
FT   NP_BIND       7     21       FAD (Potential).
FT   ACT_SITE    213    213       By similarity.
FT   ACT_SITE    230    230       By similarity.
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
//