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InterPro: IPR017437 ATP-NAD kinase, PpnK-type, all-beta

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2127 proteins

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Accession

IPR017437 ATP-NAD_kinase_PpnK-typ_all-b

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.200.30	ATP-NAD_kinase_PpnK-typ	2127
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002504 ATP-NAD/AcoX kinase
IPR012355 ATP-NAD kinase-like, eukaryotic
IPR016064 ATP-NAD kinase, PpnK-type

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0003951 NAD+ kinase activity

InterPro annotation

Entry Details in BioMart

Abstract

ATP-NAD kinases (EC:2.7.1.23) catalyse the phosphorylation of NAD to NADP utilizing ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. ATP-NAD kinase contains two domains, where domain 1 has an alpha/beta topology that is related in structure to the N-terminal of phosphofructokinase, and domain 2 has an atypical beta-sandwich topology made of four structural repeats of beta(3) units [1, 2]. This entry represents the all-beta domain 2.

Structural links Help

PDB - click here

SCOP: e.52.1.1

CATH: 2.60.200.30

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Enzyme: EC:2.7.1.23

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017437

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O95544 NAD kinase

P21373 NAD(+) kinase

P58058 NAD kinase

Q53NI2 Probable NAD kinase 2, chloroplastic

Q56YN3 NAD(H) kinase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017437	ATP-NAD kinase, PpnK-type, all-beta
IPR017438	ATP-NAD kinase, PpnK-type, alpha/beta
IPR002504	ATP-NAD/AcoX kinase
IPR016064	ATP-NAD kinase, PpnK-type
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH. Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP. J. Mol. Biol. 354 289-303 2005 [PubMed: 16242716] http://dx.doi.org/10.1016/j.jmb.2005.09.026
2.	Garavaglia S, Raffaelli N, Finaurini L, Magni G, Rizzi M. A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis. J. Biol. Chem. 279 40980-6 2004 [PubMed: 15269221] http://dx.doi.org/10.1074/jbc.M406586200

Additional Reading Open in usermanual
	Mori S, Yamasaki M, Maruyama Y, Momma K, Kawai S, Hashimoto W, Mikami B, Murata K. NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex. Biochem. Biophys. Res. Commun. 327 2005 500-8 [PubMed: 15629142] http://dx.doi.org/10.1016/j.bbrc.2004.11.163

InterPro 23.1