ID   ASPD_RALN1              Reviewed;         268 AA.
AC   Q8XRV9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 124.
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=RSp0722; ORFNames=RS01727;
OS   Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646053; CAD17873.1; -; Genomic_DNA.
DR   RefSeq; WP_011004020.1; NC_003296.1.
DR   AlphaFoldDB; Q8XRV9; -.
DR   SMR; Q8XRV9; -.
DR   STRING; 267608.RSp0722; -.
DR   EnsemblBacteria; CAD17873; CAD17873; RSp0722.
DR   GeneID; 60503637; -.
DR   KEGG; rso:RSp0722; -.
DR   eggNOG; COG1712; Bacteria.
DR   HOGENOM; CLU_089550_0_0_4; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid; Pyridine nucleotide biosynthesis.
FT   CHAIN           1..268
FT                   /note="L-aspartate dehydrogenase"
FT                   /id="PRO_0000144891"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
SQ   SEQUENCE   268 AA;  28259 MW;  9195BAB7EAA9AAE9 CRC64;
     MLHVSMVGCG AIGQGVLELL KSDPDLCFDT VIVPEHGMDR ARAAIAPFAP RTRVMTRLPA
     QADRPDLLVE CAGHDALREH VVPALEQGID CLVVSVGALS EPGLAERLEA AARRGHAQMQ
     LLSGAIGAID ALAAARVGGL DAVVYTGRKP PRAWKGTPAE RQFDLDALDR TTVIFEGKAS
     DAALLFPKNA NVAATLALAG LGMERTHVRL LADPTIDENI HHVEARGAFG GFELIMRGKP
     LAANPKTSAL TVFSVVRALG NRAHAVSI
//