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InterPro: IPR001330 Prenyltransferase/squalene oxidase

Protein matches Help

UniProtKB

Matches:

1502 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

IPR001330 Prenyltrans

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00432	Prenyltrans	1502
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006400 Hopene cyclase
IPR008930 Terpenoid cylases/protein prenyltransferase alpha-alpha toroid
IPR016648 Uncharacterised conserved protein UCP016175, prenyltransferase beta-subunit-related
IPR016731 Uncharacterised conserved protein UCP018649
IPR017826 2,3-oxidosqualene cyclase
IPR018333 Squalene cyclase

GO Term annotation Help

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

The beta subunit of the farnesyltransferases is responsible for peptide binding. Squalene-hopene cyclase is a bacterial enzyme that catalyzes the cyclization of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism [1]. Lanosterol synthase (EC:5.4.99.7) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi [2]. Cycloartenol synthase (EC: 5.4.99.8) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.

Structural links Help

PDB - click here

SCOP: a.102.4.2 , a.102.4.3

CATH: 1.50.10.20

Database links Help

PANDIT: PF00432

Blocks: IPB001330

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001330

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

B6EXY6 Beta-amyrin synthase

P18898 Geranylgeranyl transferase type-1 subunit beta

P41992 Probable geranylgeranyl transferase type-2 subunit beta

P48449 Lanosterol synthase

P53612 Geranylgeranyl transferase type-2 subunit beta

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002365	Terpene synthase, conserved site
IPR001330	Prenyltransferase/squalene oxidase
IPR018333	Squalene cyclase
IPR008930	Terpenoid cylases/protein prenyltransferase alpha-alpha toroid
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Wendt KU, Poralla K, Schulz GE. Structure and function of a squalene cyclase. Science 277 1811-5 1997 [PubMed: 9295270] http://dx.doi.org/10.1126/science.277.5333.1811
2.	Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G. A specific amino acid repeat in squalene and oxidosqualene cyclases. Trends Biochem. Sci. 19 157-8 1994 [PubMed: 8016864] http://dx.doi.org/10.1016/0968-0004(94)90276-3

Additional Reading Open in usermanual
	Njoroge FG, Vibulbhan B, Pinto P, Strickland C, Bishop WR, Nomeir A, Girijavallabhan V. Enhanced FTase activity achieved via piperazine interaction with catalytic zinc. Bioorg. Med. Chem. Lett. 16 2006 984-8 [PubMed: 16298128] http://dx.doi.org/10.1016/j.bmcl.2005.10.090
	Van Voorhis WC, Rivas KL, Bendale P, Nallan L, Horney C, Barrett LK, Bauer KD, Smart BP, Ankala S, Hucke O, Verlinde CL, Chakrabarti D, Strickland C, Yokoyama K, Buckner FS, Hamilton AD, Williams DK, Lombardo LJ, Floyd D, Gelb MH. Efficacy, pharmacokinetics, and metabolism of tetrahydroquinoline inhibitors of Plasmodium falciparum protein farnesyltransferase. Antimicrob. Agents Chemother. 51 2007 3659-71 [PubMed: 17606674] http://dx.doi.org/10.1128/AAC.00246-07
	Guo Z, Wu YW, Das D, Delon C, Cramer J, Yu S, Thuns S, Lupilova N, Waldmann H, Brunsveld L, Goody RS, Alexandrov K, Blankenfeldt W. Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation. EMBO J. 27 2008 2444-56 [PubMed: 18756270] http://dx.doi.org/10.1038/emboj.2008.164
	Guo Z, Wu YW, Tan KT, Bon RS, Guiu-Rozas E, Delon C, Nguyen TU, Wetzel S, Arndt S, Goody RS, Blankenfeldt W, Alexandrov K, Waldmann H. Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase-inhibitor complex. Angew. Chem. Int. Ed. Engl. 47 2008 3747-50 [PubMed: 18399557]
	Eastman RT, White J, Hucke O, Yokoyama K, Verlinde CL, Hast MA, Beese LS, Gelb MH, Rathod PK, Van Voorhis WC. Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase. Mol. Biochem. Parasitol. 152 2007 66-71 [PubMed: 17208314] http://dx.doi.org/10.1016/j.molbiopara.2006.11.012

InterPro 23.1