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13  structures 68  species 1  interaction 97  sequences 1  architecture

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.
Identifiers
Symbol PTase_Orf2
Pfam PF11468
InterPro IPR020965
SCOP 1zb6
SUPERFAMILY 1zb6

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]

Structure

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).

References

  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 2874460Freely accessible. PMID 15959519. 

Press Releases

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

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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].

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].

Gene Ontology

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Domain organisation

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Alignments

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(5)
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NCBI
(335)
Meta
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RP15
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RP35
(50)
RP55
(95)
RP75
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  Seed
(5)
Full
(97)
Representative proteomes UniProt
(185)
NCBI
(335)
Meta
(0)
RP15
(9)
RP35
(50)
RP55
(95)
RP75
(129)
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Curation and family details

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Curation View help on the curation process

Seed source: pdb_1zb6
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Pollington J
Number in seed: 5
Number in full: 97
Average length of the domain: 267.40 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 92.80 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.0 22.0
Trusted cut-off 22.8 30.0
Noise cut-off 21.4 20.6
Model length: 287
Family (HMM) version: 8
Download: download the raw HMM for this family

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Interactions

There is 1 interaction for this family. More...

PTase_Orf2

Structures

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 13 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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