ID ASPD_BURP1 Reviewed; 271 AA. AC Q3JFK2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 89. 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=BURPS1710b_A2501; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000125; ABA53762.1; -; Genomic_DNA. DR RefSeq; WP_004528162.1; NC_007435.1. DR AlphaFoldDB; Q3JFK2; -. DR SMR; Q3JFK2; -. DR EnsemblBacteria; ABA53762; ABA53762; BURPS1710b_A2501. DR KEGG; bpm:BURPS1710b_A2501; -. DR HOGENOM; CLU_089550_0_0_4; -. DR UniPathway; UPA00253; UER00456. DR Proteomes; UP000002700; Chromosome II. 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. FT CHAIN 1..271 FT /note="L-aspartate dehydrogenase" FT /id="PRO_1000067298" FT ACT_SITE 224 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265" FT BINDING 128 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265" FT BINDING 194 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265" SQ SEQUENCE 271 AA; 27761 MW; 4FB855C9F3D2D311 CRC64; MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA LGERVDVVSS VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG ALSDLALLDA LSNAADAGGA TLTLLSGAIG GIDALAAARQ GGLDEVRYIG RKPPLGWLGT PAEAICDLRA MAAEQTIFEG SARDAAQLYP RNANVAATIA LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS GKPLPDNPKT SALTAFSAIR ALRNRASHCV I //