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InterPro: IPR000534 Semialdehyde dehydrogenase, NAD-binding
Protein matches
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UniProtKB Matches: 4385 proteins |
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Accession
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IPR000534 Semialdehyde_DH_NAD-bd |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR016040 NAD(P)-binding domain
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Found in
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IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase
IPR003361 Acetaldehyde dehydrogenase
IPR005676 Aspartate-semialdehyde dehydrogenase, peptidoglycan lacking
IPR005986 Aspartate-semialdehyde dehydrogenase, bacterial
IPR011534 Aspartate-semialdehyde dehydrogenase, proteobacteria
IPR012080 Aspartate-semialdehyde dehydrogenase
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GO Term annotation
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Process
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GO:0006520 cellular amino acid metabolic process
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Function
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GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0051287 NAD or NADH binding
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Component
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GO:0005737 cytoplasm
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase [1], 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.
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Structural links
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Database links
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Pfam Clan: CL0063.21
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Additional Reading
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Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr.
Ensemble refinement of protein crystal structures: validation and application.
Structure 15 2007 1040-52
[PubMed: 17850744]
http://dx.doi.org/10.1016/j.str.2007.06.019
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Nonaka T, Kita A, Miura-Ohnuma J, Katoh E, Inagaki N, Yamazaki T, Miki K.
Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa).
Proteins 61 2005 1137-40
[PubMed: 16240442]
http://dx.doi.org/10.1002/prot.20679
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Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK.
High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase.
J. Mol. Biol. 341 2004 797-806
[PubMed: 15288787]
http://dx.doi.org/10.1016/j.jmb.2004.05.073
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Blanco J, Moore RA, Faehnle CR, Coe DM, Viola RE.
The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 1388-95
[PubMed: 15272161]
http://dx.doi.org/10.1107/S0907444904012971
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Faehnle CR, Le Coq J, Liu X, Viola RE.
Examination of key intermediates in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase from a gram-positive infectious bacteria.
J. Biol. Chem. 281 2006 31031-40
[PubMed: 16895909]
http://dx.doi.org/10.1074/jbc.M605926200
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InterPro 23.1
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