Summary: Prenyltransferase and squalene oxidase repeat
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This is the Wikipedia entry entitled "Prenyltransferase". More...
Prenyltransferase Edit Wikipedia article
| Structure of a squalene cyclase.[1] | |||||||||
| Identifiers | |||||||||
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| Symbol | Prenyltrans | ||||||||
| Pfam | PF00432 | ||||||||
| Pfam clan | CL0059 | ||||||||
| InterPro | IPR001330 | ||||||||
| PROSITE | PDOC00825 | ||||||||
| SCOP | 1sqc | ||||||||
| SUPERFAMILY | 1sqc | ||||||||
| OPM superfamily | 38 | ||||||||
| OPM protein | 1w6k | ||||||||
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Prenyltransferases are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.[2]
Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereochemistry of the resulting products. Examples of trans-prenyltranferases include dimethylallyltranstransferase, and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to dolichol).
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.[3] 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.[4] 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.
Contents |
[edit] Human proteins containing this domain
[edit] References
- ^ Wendt KU, Poralla K, Schulz GE (September 1997). "Structure and function of a squalene cyclase". Science 277 (5333): 18115. doi:10.1126/science.277.5333.1811. PMID 9295270.
- ^ Takahashi S, Koyama T (2006). "Structure and function of cis-prenyl chain elongating enzymes". Chem Rec 6 (4): 194205. doi:10.1002/tcr.20083. PMID 16900467.
- ^ Schulz GE, Wendt KU, Poralla K (1997). "Structure and function of a squalene cyclase". Science 277 (5333): 18111815. doi:10.1126/science.277.5333.1811. PMID 9295270.
- ^ Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G (1994). "A specific amino acid repeat in squalene and oxidosqualene cyclases". Trends Biochem. Sci. 19 (4): 157158. doi:10.1016/0968-0004(94)90276-3. PMID 8016864.
[edit] Further reading
- Wendt KU, Poralla K, Schulz GE (September 1997). "Structure and function of a squalene cyclase". Science 277 (5333): 18115. doi:10.1126/science.277.5333.1811. PMID 9295270.
- Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G (April 1994). "A specific amino acid repeat in squalene and oxidosqualene cyclases". Trends Biochem. Sci. 19 (4): 1578. doi:10.1016/0968-0004(94)90276-3. PMID 8016864.
[edit] External links
This article incorporates text from the public domain Pfam and InterPro IPR001330
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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.
Prenyltransferase and squalene oxidase repeat Provide feedback
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Literature references
-
Wendt KU, Poralla K, Schulz GE; , Science 1997;277:1811-1815.: Structure and function of a squalene cyclase. PUBMED:9295270 EPMC:9295270
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Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G; , Trends Biochem Sci 1994;19:157-158.: A specific amino acid repeat in squalene and oxidosqualene cyclases. PUBMED:8016864 EPMC:8016864
Internal database links
| SCOOP: | A2M_comp Mago-bind Pec_lyase |
| Similarity to PfamA using HHSearch: | Prenyltrans_1 Prenyltrans_1 Prenyltrans_2 Prenyltrans_2 |
External database links
| HOMSTRAD: | prenyltrans |
| PANDIT: | PF00432 |
| PROSITE: | PDOC00825 |
| Pseudofam: | PF00432 |
| SCOP: | 1sqc |
| SYSTERS: | Prenyltrans |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001330
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 [PUBMED:9295270]. Lanosterol synthase (EC) (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 [PUBMED:8016864]. Cycloartenol synthase (EC) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | catalytic activity (GO:0003824) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan 6_Hairpin (CL0059), which contains the following 28 members:
A2M_comp Bac_rhamnosid C5-epim_C Cobalamin_bind DUF1237 DUF1680 DUF2807 DUF4097 DUF4098 DUF608 GDE_C GlcNAc_2-epim Glyco_hydro_100 Glyco_hydro_15 Glyco_hydro_47 Glyco_hydro_48 Glyco_hydro_63 Glyco_hydro_65m Glyco_hydro_76 Glyco_hydro_8 Glyco_hydro_88 Glyco_hydro_9 Glycoamylase Pec_lyase Prenyltrans Prenyltrans_1 Prenyltrans_2 TrehalaseAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (69) |
Full (2497) |
Representative proteomes | NCBI (6750) |
Meta (154) |
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| RP15 (520) |
RP35 (866) |
RP55 (1268) |
RP75 (1550) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (69) |
Full (2497) |
Representative proteomes | NCBI (6750) |
Meta (154) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (520) |
RP35 (866) |
RP55 (1268) |
RP75 (1550) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_130 (release 1.0) |
| Previous IDs: | prenyltrans; |
| Type: | Repeat |
| Author: | Bateman A, Finn RD |
| Number in seed: | 69 |
| Number in full: | 2497 |
| Average length of the domain: | 43.70 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 14.26 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 44 | ||||||||||||
| Family (HMM) version: | 16 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
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 Prenyltrans domain has been found. There are 411 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence