ID   ASPD_RALEH              Reviewed;         266 AA.
AC   Q0K391;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=H16_B0736;
OS   Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
OS   (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier
OS   337)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
RA   Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E.,
RA   Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
RA   Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium
RT   Ralstonia eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC       dehydrogenation of L-aspartate to iminoaspartate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate
CC       + NH(3) + NAD(P)H.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
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DR   EMBL; AM260480; CAJ95533.1; -; Genomic_DNA.
DR   RefSeq; YP_728898.1; -.
DR   GeneID; 4454967; -.
DR   GenomeReviews; AM260480_GR; H16_B0736.
DR   KEGG; reh:H16_B0736; -.
DR   HOGENOM; Q0K391; -.
DR   OMA; Q0K391; ECAGHSA.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:HAMAP.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-N...; IEA:HAMAP.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006742; P:NADP catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01265; -; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR011182; Asp_DH_NAD_syn.
DR   Pfam; PF01958; DUF108; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR   ProDom; PD017325; Asp_dh; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; NADP; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    266       Probable L-aspartate dehydrogenase.
FT                                /FTId=PRO_1000067312.
FT   ACT_SITE    219    219       By similarity.
FT   BINDING     123    123       NAD; via amide nitrogen (By similarity).
FT   BINDING     189    189       NAD (By similarity).
SQ   SEQUENCE   266 AA;  27776 MW;  81190186F4F9E17B CRC64;
     MLHVSMVGCG AIGRGVMELL KSDPEVVFDV VIVPEHTMDE ARDAVTALAP GARVATHLDD
     QRPDLLVECA GHHALEEHIV PALERGIPCM VVSVGALSEP GMAERLEAAA RRGGTQVQLL
     SGAIGAIDAL AAARVGGLDE VIYTGRKPAR AWAGTPAEQL FDLDALTEAT VIFEGTARDA
     ARLYPKNANV AATVSLAGLG LDRTSVKLLA DPHAVENVHH VEARGAFGGF ELTMRGKPLA
     ANPKTSALTV FSVVRALGNR AHAVSI
//