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InterPro: IPR012280 Semialdehyde dehydrogenase, dimerisation domain

Protein matches Help

UniProtKB

Matches:

3512 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR012280 Semialdhyde_DH_dimer_dom

Secondary

IPR000534

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02774	Semialdhyde_dhC	3512
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005676 Aspartate-semialdehyde dehydrogenase, peptidoglycan lacking
IPR005986 Aspartate-semialdehyde dehydrogenase, bacterial
IPR011534 Aspartate-semialdehyde dehydrogenase, proteobacteria
IPR012080 Aspartate-semialdehyde dehydrogenase

Contains

IPR000319 Aspartate-semialdehyde dehydrogenase, conserved site

GO Term annotation Help

Process

GO:0008652 cellular amino acid biosynthetic process

Function

GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046983 protein dimerization activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

This domain contains 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. It also contains the 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 dimerisation domain of semialdehyde dehydrogenase.

Structural links Help

PDB - click here

SCOP: c.2.1.3 , d.81.1.1

CATH: 3.30.360.10 , 3.40.50.720

Database links Help

Enzyme: EC:1.2.1.38

PANDIT: PF02774

Blocks: IPB012280

Pfam Clan: CL0139.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012280

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

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

Publications Open in usermanual
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 Reading Open in usermanual
	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
	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, Blanco J, Viola RE. Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 2320-4 [PubMed: 15583380] http://dx.doi.org/10.1107/S0907444904026411
	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

InterPro 23.1