Summary: SnoaL-like polyketide cyclase
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SnoaL-like polyketide cyclase Provide feedback
This family includes SnoaL  a polyketide cyclase involved in nogalamycin biosynthesis. This family was formerly known as DUF1486. The proteins in this family adopt a distorted alpha-beta barrel fold . Structural data together with site-directed mutagenesis experiments have shown that SnoaL has a different mechanism to that of the classical aldolase for catalysing intramolecular aldol condensation .
Sultana A, Kallio P, Jansson A, Wang JS, Niemi J, Mantsala P, Schneider G; , EMBO J 2004;23:1911-1921.: Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation. PUBMED:15071504 EPMC:15071504
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR009959
This domain is found in SnoaL [PUBMED:15071504] a polyketide cyclase involved in nogalamycin biosynthesis. This domain was formerly known as DUF1486. It adopts a distorted alpha-beta barrel fold [PUBMED:15071504]. Structural data together with site-directed mutagenesis experiments have shown that SnoaL has a different mechanism to that of the classical aldolase for catalysing intramolecular aldol condensation [PUBMED:15071504].This entry represents a SnoaL-like domain that is found in SnoaL and a in large number of other sequences.
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This example describes an architecture with one
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This superfamily contains a variety of enzymes such as Scytalone dehydratase, Delta-5-3-ketosteroid isomerase, Limonene-1,2-epoxide hydrolase among others. The family also includes presumed non-enzymatic homologues such as NTF2.
The clan contains the following 24 members:CaMKII_AD DUF1348 DUF2358 DUF3225 DUF3804 DUF4440 DUF4467 LEH Lumazine_bd Lumazine_bd_2 MBA1 MecA_N Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL SnoaL_2 SnoaL_3 SnoaL_4 Tim44 VirB8 WI12
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_20348 (release 10.0), Pfam-B_4335 (release 18.0)|
|Author:||Moxon SJ, Bateman A|
|Number in seed:||29|
|Number in full:||1134|
|Average length of the domain:||122.50 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||66.56 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 SnoaL domain has been found. There are 23 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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