AC   MF_01265;
DC   Protein; auto
TR   HAMAP; MF_01265; -; 1; level=0
XX
Names: NadX
XX
ID   ASPD
DE   RecName: Full=L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX;
XX
CC   -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC       dehydrogenation of L-aspartate to iminoaspartate.
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   -!- 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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (dehydrogenase route): step 1/1.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
XX
DR   Pfam; PF01958; DUF108; 1; trigger=no
DR   Pfam; PF03447; NAD_binding_3; 1; trigger=no
DR   NCBIfam; TIGR03855; NAD_NadX; 1; trigger=no
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1; trigger=no
XX
KW   NAD
KW   NADP
KW   Oxidoreductase
KW   Pyridine nucleotide biosynthesis
XX
GO   GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
GO   GO:0050661; F:NADP binding
GO   GO:0051287; F:NAD binding
GO   GO:0009435; P:NAD biosynthetic process
XX
FT   From: ASPD_THEMA (Q9X1X6)
FT   ACT_SITE        193
FT   Condition: H
FT   BINDING         109
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: A
FT   BINDING         164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: N
XX
Size: 236-280;
Related: None;
Template: Q9X1X6; O28440;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BORBR, BORPA, BORPE
Plasmid: in RALN1
Comments: None
XX
# Revision 1.24 2023/11/28
//