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InterPro: IPR004788 Ribose 5-phosphate isomerase

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UniProtKB

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1468 proteins

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Accession

IPR004788 Ribose-5-phosphate_isomerase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF06026	Rib_5-P_isom_A	1460
PANTHER	PTHR11934	RpiA	1457
TIGRFAMs	TIGR00021	rpiA	1398
Signatures in BioMart

InterPro Relationships Help

Children

IPR020672 Ribose-5-phosphate isomerase, subgroup

GO Term annotation Help

Process

GO:0009052 pentose-phosphate shunt, non-oxidative branch

Function

GO:0004751 ribose-5-phosphate isomerase activity

InterPro annotation

Entry Details in BioMart

Abstract

Ribose 5-phosphate isomerase, also known as phosphoriboisomerase, catalyses the conversion of D-ribose 5-phosphate to D-ribulose 5-phosphate in the non-oxidative branch of the pentose phosphate pathway. The pentose phosphate pathway is a target for chemotherapy against Chagas disease [1]. This family of enzymes is coded for by two genes and is found in Viridiplantae, Fungi and Metazoa. It is a highly conserved enzyme [2].

Structural links Help

PDB - click here

SCOP: c.124.1.4 , d.58.40.1

CATH: 3.30.70.260 , 3.40.50.1360

Database links Help

Enzyme: EC:5.3.1.6

PANDIT: PF06026

CluSTr: ALLvsALL:3438:41.5

Pfam Clan: CL0246.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004788

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P41994 Probable-ribose 5-phosphate isomerase

P47968 Ribose-5-phosphate isomerase

P49247 Ribose-5-phosphate isomerase

Q12189 Ribose-5-phosphate isomerase

Q9ZU38 Probable ribose-5-phosphate isomerase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004788	Ribose 5-phosphate isomerase
IPR020672	Ribose-5-phosphate isomerase, subgroup
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Igoillo-Esteve M, Maugeri D, Stern AL, Beluardi P, Cazzulo JJ. The pentose phosphate pathway in Trypanosoma cruzi: a potential target for the chemotherapy of Chagas disease. An. Acad. Bras. Cienc. 79 649-63 2007 [PubMed: 18066434] http://dx.doi.org/10.1590/S0001-37652007000400007
2.	Zhang R, Andersson CE, Savchenko A, Skarina T, Evdokimova E, Beasley S, Arrowsmith CH, Edwards AM, Joachimiak A, Mowbray SL. Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle. Structure 11 31-42 2003 [PubMed: 12517338] http://dx.doi.org/10.1016/S0969-2126(02)00933-4

Additional Reading Open in usermanual
	Holmes MA, Buckner FS, Van Voorhis WC, Verlinde CL, Mehlin C, Boni E, DeTitta G, Luft J, Lauricella A, Anderson L, Kalyuzhniy O, Zucker F, Schoenfeld LW, Earnest TN, Hol WG, Merritt EA. Structure of ribose 5-phosphate isomerase from Plasmodium falciparum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 427-31 [PubMed: 16682767] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=16682767
	Hamada K, Ago H, Sugahara M, Nodake Y, Kuramitsu S, Miyano M. Oxyanion hole-stabilized stereospecific isomerization in ribose-5-phosphate isomerase (Rpi). J. Biol. Chem. 278 2003 49183-90 [PubMed: 13679361] http://dx.doi.org/10.1074/jbc.M309272200
	Rangarajan ES, Sivaraman J, Matte A, Cygler M. Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli. Proteins 48 2002 737-40 [PubMed: 12211039] http://dx.doi.org/10.1002/prot.10203
	Graille M, Meyer P, Leulliot N, Sorel I, Janin J, Van Tilbeurgh H, Quevillon-Cheruel S. Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes. Biochimie 87 2005 763-9 [PubMed: 16054529] http://dx.doi.org/10.1016/j.biochi.2005.03.001

InterPro 23.1