Summary: Transferase family
Transferase family Provide feedback
This family includes a number of transferase enzymes. These include anthranilate N-hydroxycinnamoyl/benzoyltransferase that catalyses the first committed reaction of phytoalexin biosynthesis . Deacetylvindoline 4-O-acetyltransferase EC:220.127.116.11 catalyses the last step in vindoline biosynthesis is also a member of this family . The motif HXXXD is probably part of the active site. The family also includes trichothecene 3-O-acetyltransferase.
Yang Q, Reinhard K, Schiltz E, Matern U; , Plant Mol Biol 1997;35:777-789.: Characterization and heterologous expression of hydroxycinnamoyl/benzoyl-CoA:anthranilate N-hydroxycinnamoyl/benzoyltransferase from elicited cell cultures of carnation, Dianthus caryophyllus L. PUBMED:9426598 EPMC:9426598
St-Pierre B, Laflamme P, Alarco AM, De Luca V; , Plant J 1998;14:703-713.: The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer. PUBMED:9681034 EPMC:9681034
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003480This family includes a number of transferase enzymes. These include anthranilate N-hydroxycinnamoyl/benzoyltransferase that catalyzes the first committed reaction of phytoalexin biosynthesis [PUBMED:9426598]. Deacetylvindoline 4-O-acetyltransferase (EC) catalyzes the last step in vindoline biosynthesis is also a member of this family [PUBMED:9681034]. The motif HXXXD is probably part of the active site. The family also includes trichothecene 3-O-acetyltransferase.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
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All characterised families in this clan are involved in CoA-dependent acyltransferase. All families have a characteristic HXXXD motif.
The clan contains the following 7 members:2-oxoacid_dh AATase Carn_acyltransf CAT Condensation Transferase WES_acyltransf
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_1540 (release 5.4)|
|Number in seed:||11|
|Number in full:||3130|
|Average length of the domain:||327.00 aa|
|Average identity of full alignment:||17 %|
|Average coverage of the sequence by the domain:||84.89 %|
|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:||10|
|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 Transferase domain has been found. There are 17 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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