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HAMAP rule MF_01265

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General rule information [?]

Accession MF_01265
Dates 29-JUL-2005 (Created)
28-NOV-2023 (Last updated, Version 24)
Name NadX
Scope(s) Bacteria
Template(s) Q9X1X6 (ASPD_THEMA); O28440 (ASPD_ARCFU); [ Recover all ]
Triggered by HAMAP; MF_01265 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier ASPD
Protein name RecName: Full=L-aspartate dehydrogenase;
Gene name Name=nadX;

Comments [?]

FUNCTIONSpecifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
CATALYTIC ACTIVITY Reaction=H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:11784, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=;
CATALYTIC ACTIVITY Reaction=H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:11788, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=;
PATHWAYCofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
MISCELLANEOUSThe iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.
SIMILARITYBelongs to the L-aspartate dehydrogenase family.

Keywords [?]

Gene Ontology [?]

GO:0016639; Molecular function:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
GO:0050661; Molecular function:NADP binding
GO:0051287; Molecular function:NAD binding
GO:0009435; Biological process:NAD biosynthetic process

Cross-references [?]

Pfam PF01958; DUF108; 1;
Pfam PF03447; NAD_binding_3; 1;
NCBIfam TIGR03855; NAD_NadX; 1;
PIRSF PIRSF005227; Asp_dh_NAD_syn; 1;

Features [?]

Key From To Description Tag Condition FTGroup
ACT_SITE 193 193 H
BINDING 109 109 /ligand="NAD(+)"
BINDING 164 164 /ligand="NAD(+)"

Additional information [?]

Size range 236-280 amino acids
Related rules None
Fusion Nter: None Cter: None

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