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InterPro: IPR005835 Nucleotidyl transferase

Protein matches Help

UniProtKB

Matches:

10065 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

IPR005835 NTP_transferase

Secondary

IPR001825

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00483	NTP_transferase	10065
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005771 UTP--glucose-1-phosphate uridylyltransferase, bacterial/archaeal type
IPR005774 UTP-glucose pyrophosphorylase, regulatory subunit
IPR005882 Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
IPR005907 Glucose-1-phosphate thymidylyltransferase, long form
IPR005908 Glucose-1-phosphate thymidylyltransferase, short form
IPR006375 Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase
IPR011831 Glucose-1-phosphate adenylyltransferase
IPR011832 Glucose-1-phosphate adenylyltransferase, GlgD subunit
IPR013446 Glucose-1-phosphate cytidylyltransferase
IPR017189 CTP:phosphocholine cytidylyltransferase

Contains

IPR005836 ADP-glucose pyrophosphorylase, conserved site

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0016779 nucleotidyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

Nucleotidyl transferases transfer nucleotides from one compound to another. This domain is found in a number of enzymes that transfer nucleotides onto phosphosugars.

Structural links Help

PDB - click here

SCOP: c.68.1.13 , c.68.1.20 , c.68.1.5 , c.68.1.6

CATH: 3.90.550.10

Database links Help

Enzyme: EC:2.7.7

PANDIT: PF00483

Blocks: IPB005835

Pfam Clan: CL0110.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005835

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A3QMC8 Mannose-1-phosphate guanyltransferase beta

P41940 Mannose-1-phosphate guanyltransferase

Q7JZB4 Mannose-1-phosphate guanyltransferase beta

Q8BTZ7 Mannose-1-phosphate guanyltransferase beta

Q96IJ6 Mannose-1-phosphate guanyltransferase alpha

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018357	Hexapeptide transferase, conserved site
IPR001451	Bacterial transferase hexapeptide repeat
IPR005835	Nucleotidyl transferase
IPR011004	Trimeric LpxA-like
	SWISS-MODEL
	ModBase

Publications Help

Additional Reading Open in usermanual
	Koropatkin NM, Holden HM. Molecular structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi. J. Biol. Chem. 279 2004 44023-9 [PubMed: 15292268] http://dx.doi.org/10.1074/jbc.M407755200
	Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L. Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 16 2007 2657-66 [PubMed: 18029420] http://dx.doi.org/10.1110/ps.073135107
	Jin X, Ballicora MA, Preiss J, Geiger JH. Crystal structure of potato tuber ADP-glucose pyrophosphorylase. EMBO J. 24 2005 694-704 [PubMed: 15692569] http://dx.doi.org/10.1038/sj.emboj.7600551
	Mochalkin I, Lightle S, Narasimhan L, Bornemeier D, Melnick M, Vanderroest S, McDowell L. Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site. Protein Sci. 17 2008 577-82 [PubMed: 18218712] http://dx.doi.org/10.1110/ps.073271408
	Koropatkin NM, Cleland WW, Holden HM. Kinetic and structural analysis of alpha-D-Glucose-1-phosphate cytidylyltransferase from Salmonella typhi. J. Biol. Chem. 280 2005 10774-80 [PubMed: 15634670] http://dx.doi.org/10.1074/jbc.M414111200
	Jensen SO, Reeves PR. Domain organisation in phosphomannose isomerases (types I and II). Biochim. Biophys. Acta 1382 1998 5-7 [PubMed: 9507048] http://dx.doi.org/10.1016/S0167-4838(97)00122-2

InterPro 23.1