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InterPro: IPR003694 NAD+ synthase

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UniProtKB

Matches:

2222 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR003694 NAD_synthase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02540	NAD_synthase	2222
TIGRFAMs	TIGR00552	nadE	1924
Signatures in BioMart

InterPro Relationships Help

Parent

IPR014729 Rossmann-like alpha/beta/alpha sandwich fold

Found in

IPR014445 Glutamine-dependent NAD(+) synthetase, GAT domain-containing

GO Term annotation Help

Process

GO:0009435 NAD biosynthetic process

Function

GO:0003952 NAD+ synthase (glutamine-hydrolyzing) activity
GO:0005524 ATP binding

InterPro annotation

Entry Details in BioMart

Abstract

NAD+ synthase (EC:6.3.5.1) catalyzes the last step in the biosynthesis of nicotinamide adenine dinucleotide and is induced by stress factors such as heat shock and glucose limitation. The three-dimensional structure of NH3-dependent NAD+ synthetase from Bacillus subtilis, in its free form and in complex with ATP shows that the enzyme consists of a tight homodimer with alpha/beta subunit topology [1].

Structural links Help

PDB - click here

SCOP: c.26.2.1

CATH: 3.30.300.10 , 3.40.50.620

Database links Help

Enzyme: EC:6.3.1.5

PANDIT: PF02540

Blocks: IPB003694

Pfam Clan: CL0039.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003694

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P38795 Glutamine-dependent NAD(+) synthetase

P74292 Probable glutamine-dependent NAD(+) synthetase

Q6IA69 Glutamine-dependent NAD(+) synthetase

Q711T7 Glutamine-dependent NAD(+) synthetase

Q9VYA0 Probable glutamine-dependent NAD(+) synthetase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014445	Glutamine-dependent NAD(+) synthetase, GAT domain-containing
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR003694	NAD+ synthase
IPR003010	Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, Galizzi A. Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. EMBO J. 15 5125-34 1996 [PubMed: 8895556] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8895556&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Jauch R, Humm A, Huber R, Wahl MC. Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements. J. Biol. Chem. 280 2005 15131-40 [PubMed: 15699042] http://dx.doi.org/10.1074/jbc.M413195200
	Kang GB, Kim YS, Im YJ, Rho SH, Lee JH, Eom SH. Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori. Proteins 58 2005 985-8 [PubMed: 15645437] http://dx.doi.org/10.1002/prot.20377
	McDonald HM, Pruett PS, Deivanayagam C, Protasevich II, Carson WM, DeLucas LJ, Brouillette WJ, Brouillette CG. Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis. Acta Crystallogr. D Biol. Crystallogr. 63 2007 891-905 [PubMed: 17642516] http://dx.doi.org/10.1107/S0907444907029769
	Cantoni R, Branzoni M, Labo M, Rizzi M, Riccardi G. The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+ synthetase. J. Bacteriol. 180 1998 3218-21 [PubMed: 9620974] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=9620974&action=stream&blobtype=pdf
	Symersky J, Devedjiev Y, Moore K, Brouillette C, DeLucas L. NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution. Acta Crystallogr. D Biol. Crystallogr. 58 2002 1138-46 [PubMed: 12077433] http://dx.doi.org/10.1107/S0907444902006698
	Devedjiev Y, Symersky J, Singh R, Jedrzejas M, Brouillette C, Brouillette W, Muccio D, Chattopadhyay D, DeLucas L. Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis. Acta Crystallogr. D Biol. Crystallogr. 57 2001 806-12 [PubMed: 11375500] http://dx.doi.org/10.1107/S0907444901003523

InterPro 23.1