ID A0A1I7EGC6_9BURK Unreviewed; 267 AA.
AC A0A1I7EGC6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=L-aspartate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01265};
DE EC=1.4.1.21 {ECO:0000256|HAMAP-Rule:MF_01265};
GN Name=nadX {ECO:0000256|HAMAP-Rule:MF_01265};
GN ORFNames=SAMN05192563_1019140 {ECO:0000313|EMBL:SFU22963.1};
OS Paraburkholderia aspalathi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1324617 {ECO:0000313|EMBL:SFU22963.1, ECO:0000313|Proteomes:UP000198844};
RN [1] {ECO:0000313|EMBL:SFU22963.1, ECO:0000313|Proteomes:UP000198844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27731 {ECO:0000313|EMBL:SFU22963.1,
RC ECO:0000313|Proteomes:UP000198844};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01265};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01265}.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008331, ECO:0000256|HAMAP-Rule:MF_01265}.
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DR EMBL; FPBH01000019; SFU22963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7EGC6; -.
DR UniPathway; UPA00253; UER00456.
DR Proteomes; UP000198844; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01265};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01265};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01265};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_01265}.
FT DOMAIN 7..120
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 167..254
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
FT ACT_SITE 219
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
SQ SEQUENCE 267 AA; 27727 MW; 8125AC88229A6BFD CRC64;
MNVGLIGCGA IGSLLYDLLS RYVPAVRVVA IYERDTHREG ARKALDAGAP IVDSVGDFLE
SDLDLVVECA GHEALRNLGP SALAAGHDML VASVGALADP TLETLLIDSA TAAGARLRIP
SGALGGLDAL GAAKFAGLRE VRYESHKAPG AWRGTPAEAL VVLDDIERPT AFYEGTARDA
ARLFPQNANV AAAVALAGVG FDRTRVVLYV DPLATGNTHR IKAEGDFGHI DIAVTGKTLP
SNPKTSMLAP CSLVRAIADL NQTLVVA
//