Summary: Polyketide synthesis cyclase
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This is the Wikipedia entry entitled "Polyketide synthesis cyclase family". More...
Polyketide synthesis cyclase family Edit Wikipedia article
| structural and functional analysis of tetracenomycin f2 cyclase from streptomyces glaucescens: a type-ii polyketide cyclase | |||||||||
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| Symbol | Cyclase_polyket | ||||||||
| Pfam | PF04673 | ||||||||
| InterPro | IPR006765 | ||||||||
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In molecular biology, the polyketide synthesis cyclase family of proteins includes a number of cyclases involved in polyketide synthesis in a number of actinobacterial species.
Aromatic polyketides are assembled by a type II (iterative) polyketide synthase in bacteria. Iterative type II polyketide synthases produce polyketide chains of variable but defined length from a specific starter unit and a number of extender units. They also specify the initial regiospecific folding and cyclisation pattern of nascent polyketides either through the action of a cyclase (CYC) subunit or through the combined action of site-specific ketoreductase and CYC subunits. Additional CYCs and other modifications may be necessary to produce linear aromatic polyketides.
The Tetracenomycin polyketide synthesis protein, tcmI, from Streptomyces glaucescens catalyses an aromatic rearrangement in the biosynthetic pathaway of tetracenomycin C from Streptomyces coelicolor. The protein is a homodimer where each subunit forms a beta-alpha-beta fold belonging to the ferrodoxin fold superfamily.[1] Four strands of antiparallel sheets and a layer of alpha helices create a cavity which was proposed to be the active site. This structure shows strong topological similarity to a polyketide monoxygenase from Streptomyces coelicolor which functions in the actinorhodin biosynthesic pathway.[2] It was suggested, therefore, that this fold is well suited to serve as a framework for rearrangements and chemical modification of polyaromatic substrates.
[edit] References
- ^ Thompson TB, Katayama K, Watanabe K, Hutchinson CR, Rayment I (September 2004). "Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase". J. Biol. Chem. 279 (36): 3795663. doi:10.1074/jbc.M406144200. PMID 15231835.
- ^ Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B (January 2003). "The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis". EMBO J. 22 (2): 20515. doi:10.1093/emboj/cdg031. PMC 140106. PMID 12514126. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140106.
This article incorporates text from the public domain Pfam and InterPro IPR006765
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This family represents a number of cyclases involved in polyketide synthesis in a number of actinobacterial species.
External database links
| PANDIT: | PF04673 |
| Pseudofam: | PF04673 |
| SYSTERS: | Cyclase_polyket |
This tab holds annotation information from the InterPro database.
InterPro entry IPR006765
Aromatic polyketides are assembled by a type II (iterative) polyketide synthase in bacteria. Iterative type II polyketide synthases produce polyketide chains of variable but defined length from a specific starter unit and a number of extender units. They also specify the initial regiospecific folding and cyclization pattern of nascent polyketides either through the action of a cyclase (CYC) subunit or through the combined action of site-specific ketoreductase and CYC subunits. Additional CYCs and other modifications may be necessary to produce linear aromatic polyketides.
This family represents a number of cyclases involved in polyketide synthesis in a number of actinobacterial species.
TcmI (SWISSPROT) catalyses an aromatic rearrangement in the biosynthetic pathaway of tetracenomycin C from Streptomyces coelicolor. The protein is a homodimer where each subunit forms a beta-alpha-beta fold belonging to the ferrodoxin fold superfamily [PUBMED:15231835]. Four strands of antiparallel sheets and a layer of alpha helices create a cavity which was proposed to be the active site. This structure shows strong topological similarity to a polyketide monoxygenase (SWISSPROT) from S. coelicolor which functions in the actinorhodin biosynthesic pathway [PUBMED:12514126]. It was suggested, therefore, that this fold is well suited to serve as a framework for rearrangements and chemical modification of polyaromatic substrates.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Biological process | polyketide biosynthetic process (GO:0030639) |
Domain organisation
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Alignments
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| Seed (23) |
Full (122) |
Representative proteomes | NCBI (120) |
Meta (0) |
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| RP15 (10) |
RP35 (30) |
RP55 (38) |
RP75 (40) |
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| PP/heatmap | 1 | |||||||
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| Seed (23) |
Full (122) |
Representative proteomes | NCBI (120) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (10) |
RP35 (30) |
RP55 (38) |
RP75 (40) |
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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.
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Trees
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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_5596 (release 7.5) |
| Previous IDs: | cyclase_polyket; |
| Type: | Family |
| Author: | Mifsud W |
| Number in seed: | 23 |
| Number in full: | 122 |
| Average length of the domain: | 96.20 aa |
| Average identity of full alignment: | 46 % |
| Average coverage of the sequence by the domain: | 87.19 % |
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: | 97 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Cyclase_polyketStructures
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 Cyclase_polyket domain has been found. There are 1 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