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InterPro: IPR000534 Semialdehyde dehydrogenase, NAD-binding

Protein matchesHelp
UniProtKB
Matches:
4385 proteins
AccessionHelp IPR000534 Semialdehyde_DH_NAD-bd
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR016040 NAD(P)-binding domain
Found in 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
GO Term annotationHelp
Process GO:0006520 cellular amino acid metabolic process
Function GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0051287 NAD or NADH binding
Component GO:0005737 cytoplasm
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
SCOP: c.2.1.3
CATH: 3.40.50.720
Database linksHelp
PANDIT: PF01118
Pfam Clan: CL0063.21

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000534 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O87014 USG-1 protein homolog

P13663 Aspartate-semialdehyde dehydrogenase

P54899 N-acetyl-gamma-glutamyl-phosphate reductase

Q6AV34 Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic

Q93Z70 Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005676 Aspartate-semialdehyde dehydrogenase, peptidoglycan lacking
IPR016040 NAD(P)-binding domain
IPR012280 Semialdehyde dehydrogenase, dimerisation domain
IPR000319 Aspartate-semialdehyde dehydrogenase, conserved site
IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase
IPR000534 Semialdehyde dehydrogenase, NAD-binding
IPR012080 Aspartate-semialdehyde dehydrogenase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R.
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J. Mol. Biol. 289 991-1002 1999 [PubMed: 10369777]
http://dx.doi.org/10.1006/jmbi.1999.2828

Additional ReadingHelp
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
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
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
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
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