ID   ASPD_METMP              Reviewed;         267 AA.
AC   Q6LZ92;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=MMP0737;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF30293.1; -; Genomic_DNA.
DR   RefSeq; WP_011170681.1; NC_005791.1.
DR   AlphaFoldDB; Q6LZ92; -.
DR   SMR; Q6LZ92; -.
DR   STRING; 267377.MMP0737; -.
DR   EnsemblBacteria; CAF30293; CAF30293; MMP0737.
DR   GeneID; 37875269; -.
DR   KEGG; mmp:MMP0737; -.
DR   PATRIC; fig|267377.15.peg.755; -.
DR   eggNOG; arCOG00254; Archaea.
DR   HOGENOM; CLU_089550_0_0_2; -.
DR   OMA; ECAGHSA; -.
DR   OrthoDB; 50102at2157; -.
DR   BioCyc; MMAR267377:MMP_RS03855-MON; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000000590; Chromosome.
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; IPR022487; Asp_DH_arc.
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.
DR   TIGRFAMs; TIGR03855; NAD_NadX; 1.
PE   3: Inferred from homology;
KW   NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..267
FT                   /note="L-aspartate dehydrogenase"
FT                   /id="PRO_0000144899"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT   BINDING         124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
SQ   SEQUENCE   267 AA;  28593 MW;  061F6D2566E0E33A CRC64;
     MLKIGLVGCG AIASLITKAL MSDRLNKAEV LAFYDGNLEK AEKLAMETGA DFCKSLDELV
     SKDLDLIVEC ASVNAVEDTV IKSLNNDKDV IIMSVGAFAD KDLFVKLYKL AEKLGKKIYV
     PSGAVAGIDA VKSGSLGKIS EVSLTTTKPV HGLKSALEEQ GLNTDEIKEP KIVFEGTVFD
     AISKFPQNIN VSVVLSLASR YPAKVKIIAD PNAVVNRHEI LVKGSIGTIK TCVENNPCRD
     NPKTSALAAY SVIRLIKDLS EPVRIGT