SMART: Semialdhyde_dh domain annotation

Semialdhyde_dh Semialdehyde dehydrogenase, NAD binding domain

SMART accession number:	SM00859
Description:	The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.
Interpro abstract (IPR000534):	The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase [(PUBMED:10369777)], an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.
GO process:	oxidation-reduction process (GO:0055114), cellular amino acid metabolic process (GO:0006520)
GO component:	cytoplasm (GO:0005737)
GO function:	NAD binding (GO:0051287), oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620)
Family alignment:	View or

There are 3788 Semialdhyde_dh domains in 3788 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Semialdhyde_dh domain is also avaliable.

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Go to specific node: Arabidopsis thaliana, Caenorhabditis elegans, Saccharomyces cerevisiae
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R
- Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichiacoli, a key enzyme in the aspartate family of amino acid biosynthesis.
- J Mol Biol. 1999; 289: 991-1002
- Display abstract
- Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branchpoint in an essential aspartic biosynthetic pathway found in bacteria,fungi and the higher plants. Mutations in the asd gene encoding for ASADHthat produce an inactive enzyme are lethal, which suggests that ASADH maybe an effective target for antibacterial, herbicidal and fungicidalagents.We have solved the crystal structure of the Escherichia coli enzymeto 2.5 A resolution using single isomorphous replacement and 3-foldnon-crystallographic symmetry. Each monomer has an N-terminalnucleotide-binding domain and a dimerisation domain. The presence of anessential cysteine locates the active site in a cleft between the twodomains. The functional dimer has the appearance of a butterfly, with theNADP-binding domains forming the wings and the dimerisation domain formingthe body.A histidine residue is identified as a likely acid/base catalystin the enzymic reaction. Other amino acids implicated in the enzymicactivity by mutagenesis are found in the active site region and define thesubstrate binding pocket.
Structure (3D structures containing this domain)

3D Structures of Semialdhyde_dh domains in PDB

PDB code	Main view	Title
1brm		Aspartate beta-semialdehyde dehydrogenase from escherichia coli
1gl3		Aspartate beta-semialdehyde dehydrogenase in complex with nadp and substrate analogue s-methyl cysteine sulfoxide
1mb4		Crystal structure of aspartate semialdehyde dehydrogenase from vibrio cholerae with nadp and s-methyl-l-cysteine sulfoxide
1mc4		Crystal structure of aspartate-semialdehyde dehydrogenase from vibrio cholerae el tor
1nvm		Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate
1nwc		Crystal structure of aspartate-semialdehyde dehydrogenase from haemophilus influenzae
1nwh		Crystal structure of aspartate semialdehyde dehydrogenase from haemophilus influenzae as a tetrahedral hemithioacetal reaction intermediate at 2.0 a
1nx6		Crystal structure of aspartate semialdehyde dehydrogenase from haemophilus influenzae as a tetrahedral hemithiocetal reaction intermediate with phosphate at 2.15 a
1oza		Crystal structure of the r103l mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae
1pqp		Crystal structure of the c136s mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae bound with aspartate semialdehyde and phosphate
1pqu		Crystal structure of the h277n mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae bound with nadp, s-methyl cysteine sulfoxide and cacodylate
1pr3		Crystal structure of the r103k mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae
1ps8		Crystal structure of the r270k mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae
1pu2		Crystal structure of the k246r mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae
1q2x		Crystal structure of the e243d mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae bound with substrate aspartate semialdehyde
1t4b		1.6 angstrom structure of esherichia coli aspartate- semialdehyde dehydrogenase.
1t4d		Crystal structure of escherichia coli aspartate beta- semialdehyde dehydrogenase (ecasadh), at 1.95 angstrom resolution
1ta4		Crystal structure of aspartate-semialdehyde dehydrogenase from haemophilus influenzae with a bound arsenate
1tb4		Crystal structure of aspartate-semialdehyde dehydrogenase from haemophilus influenzae with a bound periodate
1vkn		Crystal structure of n-acetyl-gamma-glutamyl-phosphate reductase (tm1782) from thermotoga maritima at 1.80 a resolution
1xyg		X-ray structure of gene product from arabidopsis thaliana at2g19940
1ys4		Structure of aspartate-semialdehyde dehydrogenase from methanococcus jannaschii
2cvo		Crystal structure of putative n-acetyl-gamma-glutamyl- phosphate reductase (ak071544) from rice (oryza sativa)
2ep5		Structural study of project id st1242 from sulfolobus tokodaii strain7
2g17		The structure of n-acetyl-gamma-glutamyl-phosphate reductase from salmonella typhimurium.
2gyy		Structure of aspartate semialdehyde dehydrogenase (asadh) from streptococcus pneumoniae
2gz1		Structure of aspartate semialdehyde dehydrogenase (asadh) from streptococcus pneumoniae complexed with nadp
2gz2		Structure of aspartate semialdehyde dehydrogenase (asadh) from streptococcus pneumoniae complexed with 2',5'-adp
2gz3		Structure of aspartate semialdehyde dehydrogenase (asadh) from streptococcus pneumoniae complexed with nadp and aspartate-semialdehyde
2hjs		The structure of a probable aspartate-semialdehyde dehydrogenase from pseudomonas aeruginosa
2i3a		Crystal structure of n-acetyl-gamma-glutamyl-phosphate reductase (rv1652) from mycobacterium tuberculosis
2i3g		Crystal structure of n-acetyl-gamma-glutamyl-phosphate reductase (rv1652) from mycobacterium tuberculosis in complex with nadp+.
2nqt		Crystal structure of n-acetyl-gamma-glutamyl-phosphate reductase (rv1652) from mycobacterium tuberculosis at 1.58 a resolution
2ozp		Crystal structure of n-acetyl-gamma-glutamyl-phosphate reductase (ttha1904) from thermus thermophilus
2q49		Ensemble refinement of the protein crystal structure of gene product from arabidopsis thaliana at2g19940
2qz9		Crystal structure of aspartate semialdehyde dehydrogenase ii from vibrio cholerae
2r00		Crystal structure of aspartate semialdehyde dehydrogenase ii complexed with asa from vibrio cholerae
2yv3		Crystal structure of aspartate semialdehyde dehydrogenase from thermus thermophilus hb8
3dr3		Structure of idp00107, a potential n-acetyl-gamma- glutamylphosphate reductase from shigella flexneri

Links (links to other resources describing this domain)
PFAM Semialdhyde_dh
INTERPRO IPR000534