ID   ASPD_CUPNH              Reviewed;         266 AA.
AC   Q0K391;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=L-aspartate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01265};
DE            EC=1.4.1.21 {ECO:0000255|HAMAP-Rule:MF_01265};
GN   Name=nadX {ECO:0000255|HAMAP-Rule:MF_01265};
GN   OrderedLocusNames=H16_B0736;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   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. {ECO:0000255|HAMAP-
CC       Rule:MF_01265}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11784, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01265};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11788, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01265};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01265}.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia.
CC       {ECO:0000255|HAMAP-Rule:MF_01265}.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01265}.
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DR   EMBL; AM260480; CAJ95533.1; -; Genomic_DNA.
DR   RefSeq; WP_010811682.1; NZ_CP039288.1.
DR   AlphaFoldDB; Q0K391; -.
DR   SMR; Q0K391; -.
DR   STRING; 381666.H16_B0736; -.
DR   GeneID; 57646626; -.
DR   KEGG; reh:H16_B0736; -.
DR   eggNOG; COG1712; Bacteria.
DR   HOGENOM; CLU_089550_0_0_4; -.
DR   OrthoDB; 7056904at2; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000008210; Chromosome 2.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01265; NadX; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR020626; Asp_DH_prok.
DR   InterPro; IPR011182; L-Asp_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR31873:SF6; ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01958; Asp_DH_C; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..266
FT                   /note="L-aspartate dehydrogenase"
FT                   /id="PRO_1000067312"
FT   ACT_SITE        219
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT   BINDING         123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT   BINDING         189
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
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
//