ASPD_CUPNH
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 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=H16_B0736;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; 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 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 EnsemblBacteria; CAJ95533; CAJ95533; H16_B0736.
DR GeneID; 57646626; -.
DR KEGG; reh:H16_B0736; -.
DR eggNOG; COG1712; Bacteria.
DR HOGENOM; CLU_089550_0_0_4; -.
DR OMA; ECAGHSA; -.
DR OrthoDB; 1670363at2; -.
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 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 Pfam; PF01958; DUF108; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR SUPFAM; SSF51735; SSF51735; 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
