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39  structures 98  species 0  interactions 146  sequences 2  architectures

Family: PTase_Orf2 (PF11468)

Summary: Aromatic prenyltransferase Orf2

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This is the Wikipedia entry entitled "Pt-barrel". More...

Pt-barrel Edit Wikipedia article

Orf2-like Prenyltransferase
Orf2 anim1X.gif
Crystal structure of a PT-barrel protein.

The PT-barrel, is a novel protein fold that was discovered in the crystal structure of the prenyltransferase, Orf2 from Streptomyces sp. strain CL190.[1]


The PT-barrel consists of a closed β-sheet comprising ten anti-parallel β-strands arranged around a central β-barrel core, itself surrounded by a ring of α-helices forming the outer, solvent exposed surface of the barrel.

The secondary connectivity nearly conforms to an (ααββ)5 classification, but is more specifically described using the (ααββ)4-(αββ)−α nomenclature, where helices 6 and 8, both involved in inter-protein contacts in the crystal lattice, display a helical “kink”. The most hydrophobic section of the PT-barrel is the region residing between the outer surface of the cylindrical β-barrel and the belt of surrounding α-helices. Additionally, a number of hydrophobic residues located inside the barrel accommodate the prenyl tail of the Geranyl-diPhosphate (GPP) and GSPP molecules, while the diphosphate or the thio-diphosphate head groups of substrate and substrate analogs, respectively, point toward the “upper”, more polar end of the barrel where a Mg2+ ion is coordinated. Finally, the bottom of the barrel is capped by a short C-terminal helix (α11).


  1. ^ Kuzuyama T, Noel JP, Richard SB (June 2005). "Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products". Nature. 435 (7044): 983–7. doi:10.1038/nature03668. PMC 2874460. PMID 15959519.

Press Releases

Promiscuous Catalytic Activity Possessed by Novel Enzyme Structure, June 15, 2005
SSRL Science Highlight July 2005 Press Release Number: PR-SSRL-05-3

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Aromatic prenyltransferase Orf2 Provide feedback

In vivo Orf2 attaches a geranyl group to a 1,3,6,8-tetrahydroxynaphthalene-derived polyketide during naphterpin biosynthesis [1]. In vitro, Orf2 catalyses carbon-carbon based and carbon-oxygen based prenylation of hydroxyl-containing aromatic acceptors of synthetic, microbial and plant origin [1].

Literature references

  1. Kuzuyama T, Noel JP, Richard SB;, Nature. 2005;435:983-987.: Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products. PUBMED:15959519 EPMC:15959519

This tab holds annotation information from the InterPro database.

InterPro entry IPR020965

This entry includes prenyltransferase-like proteins, including:

  • Aromatic prenyltransferases NovQ from Streptomyces niveus and CloQ from Streptomyces roseochromogenes. They catalyse the transfer of a dimethylallyl group to 4-hydroxyphenylpyruvate to produce the ring A structure in the novobiocin and clorobiocin biosynthesis pathways, respectively [ PUBMED:19557032 , PUBMED:12618544 ].
  • Flaviolin linalyltransferase from Streptomyces cinnamonensis. It is involved in the biosynthesis of furanonaphthoquinone I (FNQ I). It catalyses C- and O-prenylations of different phenolic substrates [ PUBMED:17103476 , PUBMED:17543953 ].
  • 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase from Streptomyces anulatus. It is involved in the biosynthesis of prenylated phenazines. It catalyses the transfer of a dimethylallyl moiety to C-9 of 5,10-dihydrophenazine 1-carboxylate (dihydro-PCA). It is specific for both dimethylallyl diphosphate and dihydro-PCA [ PUBMED:19339241 ].

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Domain organisation

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Seed source: pdb_1zb6
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Pollington J
Number in seed: 5
Number in full: 146
Average length of the domain: 275.30 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 91.98 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.0 22.0
Trusted cut-off 30.1 30.0
Noise cut-off 20.4 20.0
Model length: 287
Family (HMM) version: 10
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PTase_Orf2 domain has been found. There are 39 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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