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InterPro: IPR005854 Amidophosphoribosyl transferase

Protein matches Help

UniProtKB

Matches:

2187 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

IPR005854 Amd_phspho_trans

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000485	Amd_phspho_trans	1749
PANTHER	PTHR11907	Amd_phspho_trans	2175
TIGRFAMs	TIGR01134	purF	1693
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000583 Glutamine amidotransferase, class-II
IPR000836 Phosphoribosyltransferase

GO Term annotation Help

Process

GO:0009113 purine base biosynthetic process

Function

GO:0004044 amidophosphoribosyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

Purine nucleotides are synthesised both via the de novo pathway and via the salvage pathway and are vital for cell functions and cell proliferation through DNA and RNA syntheses and ATP energy supply. Amidophosphoribosyltransferase (EC:2.4.2.14) is the rate-limiting enzyme in the de novo pathway of purine ribonucleotide synthesis and is regulated by feedback inhibition by AMP and GMP [1].

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O

This family contains sequences which are members of the MEROPS peptidase family C44 (glutamine phosphoribosylpyrophosphate amidotransferase precursor, clan PB(C)) and sequences which are classed as non-peptidase homologs. These are sequences either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity.

Structural links Help

PDB - click here

SCOP: c.61.1.1 , d.153.1.1

CATH: 3.40.50.2020 , 3.60.20.10

Database links Help

Enzyme: EC:2.4.2.14

MEROPS: C44

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005854

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00497 Amidophosphoribosyltransferase

P04046 Amidophosphoribosyltransferase

Q06203 Amidophosphoribosyltransferase

Q27601 Amidophosphoribosyltransferase

Q55621 Amidophosphoribosyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000583	Glutamine amidotransferase, class-II
IPR005854	Amidophosphoribosyl transferase
IPR000836	Phosphoribosyltransferase
IPR017932	Glutamine amidotransferase, type II
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Yamaoka T, Yano M, Kondo M, Sasaki H, Hino S, Katashima R, Moritani M, Itakura M. Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses. J. Biol. Chem. 276 21285-91 2001 [PubMed: 11290738] http://dx.doi.org/10.1074/jbc.M011103200

Additional Reading Open in usermanual
	Muchmore CR, Krahn JM, Kim JH, Zalkin H, Smith JL. Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Protein Sci. 7 1998 39-51 [PubMed: 9514258] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9514258&action=stream&blobtype=pdf
	Krahn JM, Kim JH, Burns MR, Parry RJ, Zalkin H, Smith JL. Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry 36 1997 11061-8 [PubMed: 9333323] http://dx.doi.org/10.1021/bi9714114
	Smith JL, Zaluzec EJ, Wery JP, Niu L, Switzer RL, Zalkin H, Satow Y. Structure of the allosteric regulatory enzyme of purine biosynthesis. Science 264 1994 1427-33 [PubMed: 8197456] http://www.sciencemag.org/cgi/content/abstract/264/5164/1427
	Kim JH, Krahn JM, Tomchick DR, Smith JL, Zalkin H. Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271 1996 15549-57 [PubMed: 8663035] http://dx.doi.org/10.1074/jbc.271.26.15549
	Chen S, Tomchick DR, Wolle D, Hu P, Smith JL, Switzer RL, Zalkin H. Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry 36 1997 10718-26 [PubMed: 9271502] http://dx.doi.org/10.1021/bi9711893

InterPro 23.1