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InterPro: IPR013792 RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta

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4946 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR013792 RNA3'P_cycl/enolpyr_Trfase_a/b

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SuperFamily	SSF55205	RNA3'_cycl/enolpyr_transf_A/B	4946
Signatures in BioMart

InterPro Relationships Help

Children

IPR001986 3-phosphoshikimate 1-carboxyvinyltransferase, core

Found in

IPR000228 RNA 3'-terminal phosphate cyclase-like
IPR016443 RNA 3'-terminal phosphate cyclase-like, eukaryotic
IPR017770 RNA 3'-terminal phosphate cyclase, subgroup
IPR020723 RNA 3'-terminal phosphate cyclase predicted

Contains

IPR020719 RNA 3'-terminal phosphate cyclase-like, conserved site

GO Term annotation Help

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents an alpha/beta domain consisting of alternating beta-strands and alpha helices in two layer. This domain is found in RNA 3'-terminal phosphate cyclase (RPTC), where it occurs as a duplication of three repeats of this fold packed together around a pseudo three-fold axis [1]. RNA cyclases are a family of RNA-modifying enzymes that catalyse the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA. These cyclases contain an insert alpha/beta domain with a thioredoxin topology (IPR013791).

This domain is also found in enolpyruvate transferase, where it occurs as a duplication of six repeats of this fold organised into two RPTC-like domains [2, 3]. Enolpyruvate transferase is the first enzyme in bacterial peptidoglycan biosynthesis, catalysing the transfer of enolpyruvate from phosphoenolpyruvate to UDP-N-acetyl-glucosamine.

Structural links Help

PDB - click here

SCOP: d.68.2.1 , d.68.2.2

CATH: 3.65.10.10 , 3.65.10.20

Database links Help

Enzyme: EC:2.5.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013792

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O77264 RNA 3'-terminal phosphate cyclase

P08566 Pentafunctional AROM polypeptide

Q23400 Probable RNA 3'-terminal phosphate cyclase-like protein

Q8R5H1 Ubiquitin carboxyl-terminal hydrolase 15

Q9Y4E8 Ubiquitin carboxyl-terminal hydrolase 15

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR016443	RNA 3'-terminal phosphate cyclase-like, eukaryotic
IPR000228	RNA 3'-terminal phosphate cyclase-like
IPR002658	3-dehydroquinate synthase AroB
IPR017770	RNA 3'-terminal phosphate cyclase, subgroup
IPR013708	Shikimate dehydrogenase substrate binding, N-terminal
IPR018200	Peptidase C19, ubiquitin carboxyl-terminal hydrolase 2, conserved site
IPR016037	3-dehydroquinate synthase AroB, subgroup
IPR001394	Peptidase C19, ubiquitin carboxyl-terminal hydrolase 2
IPR018508	3-dehydroquinate dehydratase, active site
IPR016040	NAD(P)-binding domain
IPR006264	3-phosphoshikimate 1-carboxyvinyltransferase, subgroup
IPR001986	3-phosphoshikimate 1-carboxyvinyltransferase, core
IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
IPR013791	RNA 3'-terminal phosphate cyclase, subset, insert domain
IPR013796	RNA 3'-terminal phosphate cyclase, insert domain
IPR010110	Shikimate-5-dehydrogenase
IPR008289	Pentafunctional AroM protein
IPR020719	RNA 3'-terminal phosphate cyclase-like, conserved site
IPR006615	Peptidase C19, ubiquitin-specific peptidase, DUSP domain
IPR000623	Shikimate kinase
IPR001381	Dehydroquinase class I
IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
	ModBase
	SWISS-MODEL
	PDB Chain
	SCOP Domain

Publications Open in usermanual
1.	Palm GJ, Billy E, Filipowicz W, Wlodawer A. Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology. Structure 8 13-23 2000 [PubMed: 10673421] http://dx.doi.org/10.1016/S0969-2126(00)00076-9
2.	Skarzynski T, Kim DH, Lees WJ, Walsh CT, Duncan K. Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA. Biochemistry 37 2572-7 1998 [PubMed: 9485407] http://dx.doi.org/10.1021/bi9722608
3.	Yoon HJ, Ku MJ, Ahn HJ, Lee BI, Mikami B, Suh SW. Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin. Mol. Cells 19 398-401 2005 [PubMed: 15995357]

Additional Reading Open in usermanual
	Yoon HJ, Lee SJ, Mikami B, Park HJ, Yoo J, Suh SW. Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin. Proteins 71 2008 1032-7 [PubMed: 18247346] http://dx.doi.org/10.1002/prot.21959
	Funke T, Han H, Healy-Fried ML, Fischer M, Schonbrunn E. Molecular basis for the herbicide resistance of Roundup Ready crops. Proc. Natl. Acad. Sci. U.S.A. 103 2006 13010-5 [PubMed: 16916934] http://dx.doi.org/10.1073/pnas.0603638103
	Eschenburg S, Priestman M, Schonbrunn E. Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. J. Biol. Chem. 280 2005 3757-63 [PubMed: 15531591] http://dx.doi.org/10.1074/jbc.M411325200
	Healy-Fried ML, Funke T, Priestman MA, Han H, Schonbrunn E. Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase. J. Biol. Chem. 282 2007 32949-55 [PubMed: 17855366] http://dx.doi.org/10.1074/jbc.M705624200
	Funke T, Healy-Fried ML, Han H, Alberg DG, Bartlett PA, Schonbrunn E. Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-phosphate synthases by tetrahedral reaction intermediate analogues. Biochemistry 46 2007 13344-51 [PubMed: 17958399] http://dx.doi.org/10.1021/bi701095u

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