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IPR012080

Description

IPR012080 is a Aspartate-semialdehyde dehydrogenase.

<p>This entry represents the entire asparate-semialdehyde dehydrogenase family.</p> <p>Aspartate-semialdehyde dehydrogenase ([ec:1.2.1.11]), the second enzyme in the aspartate pathway, converts aspartyl phosphate to aspartate-semialdehyde, the branch point intermediate between the lysine and threonine/methionine pathways. Based on sequence alignments, the aspartate-semialdehyde dehydrogenase family appears to have at least three distinct subfamilies. Most studies have been performed on enzymes isolated from Gram-negative bacteria [[cite:PUB00034673], [cite:PUB00029242], [cite:PUB00029661], [cite:PUB00034674]]. The N-terminal domain forms the active site and NADP-binding pocket, while C-terminal domain is primarily involved in hydrophobic intersubunit contacts. The catalytic mechanism involves the formation of a covalent thioester acyl-enzyme intermediate mediated through nucleophilic attack by an active site cysteine residue on the substrate aspartyl phosphate. Release of inorganic phosphate is followed by hydride transfer from NADPH to yield the product. The recently described archaeal structure suggests that the two subgroups of aspartate semi-aldehyde dehydrogenase share similar structures and have an identical catalytic mechanism, despite their relatively low sequence identity [[cite:PUB00034675]]. Unlike the bacterial enzymes, the archaeal enzyme utilised both NAD and NADP as cofactor.</p> <p>Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids -lysine, threonine, methionine and isoleucine -in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential component of bacterial cell wall biosynthesis, and dipicolinic acid, which is involved in sporulation in Gram-positive bacteria. Members of the animal kingdom do not posses this pathway and must therefore acquire these essential amino acids through their diet. Research into improving the metabolic flux through this pathway has the potential to increase the yield of the essential amino acids in important crops, thus improving their nutritional value. Additionally, since the enzymes are not present in animals, inhibitors of them are promising targets for the development of novel antibiotics and herbicides. For more information see [[cite:PUB00034672]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function Aspartate-semialdehyde dehydrogenase activity Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH.
Biological process Methionine biosynthetic process The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
Biological process Threonine biosynthetic process The chemical reactions and pathways resulting in the formation of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
Biological process Lysine biosynthetic process via diaminopimelate The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
Biological process Isoleucine biosynthetic process The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
Molecular function NADP binding Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

Associated Lotus transcripts 2

Transcript Name Description Predicted domains Domain count
PREDICTED: aspartate-semialdehyde dehydrogenase-like [Glycine max] gi|356524624|ref|XP_003530928.1| 18
Aspartate-semialdehyde dehydrogenase, N-acetyl-gamma-glutamyl-phosphate reductase; TAIR: AT1G14810.1 semialdehyde dehydrogenase family protein; Swiss-Prot: sp|P49420|DHAS_PROMA Aspartate-semialdehyde dehydrogenase; TrEMBL-Plants: tr|I1KQD8|I1KQD8_SOYBN Uncharacterized protein; Found in the gene: LotjaGi4g1v0458700 18

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
TIGR01296 TIGRFAM 1 50.00