Summary: Mycobacterial cell wall arabinan synthesis protein
This is the Wikipedia entry entitled "Arabinosyltransferase". More...
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Arabinosyltransferase Edit Wikipedia article
In molecular biology, an arabinosyltransferase is a transferase enzyme acting upon arabinose. This enzyme is involved in polymerisation of arabinogalactan (an essential component of the mycobacterial cell wall). In terms of mycobacteria, the more precise term is arabinofuranosyltransferase, since the arabinose residues occur only in a furanose form.
- "Reconstitution of functional mycobacterial arabinosyltransferase AftC proteoliposome and assessment of decaprenylphosphorylarabinose analogues as arabinofuranosyl donors." US National Library. Retrieved 2014-3-11.
- Belanger AE, Besra GS, Ford ME, Mikusova K, Belisle JT, Brennan PJ, Inamine JM (October 1996). "The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the antimycobacterial drug ethambutol". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11919–24. doi:10.1073/pnas.93.21.11919. PMC 38159. PMID 8876238.
Mycobacterial cell wall arabinan synthesis protein Provide feedback
Arabinosyltransferase is involved in arabinogalactan (AG) biosynthesis pathway in mycobacteria. AG is a component of the macromolecular assembly of the mycolyl-AG-peptidoglycan complex of the cell wall. This enzyme has important clinical applications as it is believed to be the target of the antimycobacterial drug Ethambutol .
Belanger AE, Besra GS, Ford ME, Mikusova K, Belisle JT, Brennan PJ, Inamine JM; , Proc Natl Acad Sci U S A 1996;93:11919-11924.: The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the antimycobacterial drug ethambutol. PUBMED:8876238 EPMC:8876238
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007680
Arabinosyltransferases EmbA, EmbB and EmbC are known to be involved in arabinogalactan (AG) and lipoarabinomannan (LAM) biosynthesis in mycobacteria. Synthesis of LAM, but not AG, ceases after inactivation of EmbC, while the arabinan of AG is affected by EmbA or EmbB disruption [PUBMED:14507364]. The arabinans of the mycobacterial cell wall are key structural and immunological polymers.
These enzymes could have important clinical applications as they are believed to be the target of the antimycobacterial drug Ethambutol [PUBMED:8876238].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||arabinosyltransferase activity (GO:0052636)|
|Biological process||Actinobacterium-type cell wall biogenesis (GO:0071766)|
- 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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This is the GT-C clan that contains diverse glycosyltransferases that possess 8-13 predicted transmembrane segments .
The clan contains the following 21 members:ALG3 Alg6_Alg8 Arabinose_trans DIE2_ALG10 DUF1420 DUF2029 DUF2079 DUF2142 DUF2723 EpsG Glucan_synthase Glyco_transf_22 Mannosyl_trans Mannosyl_trans2 Oleosin PIG-U PMT PMT_2 PTPS_related STT3 YfhO
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Curation and family details
|Seed source:||Pfam-B_4670 (release 7.5)|
|Author:||Waterfield DI, Finn RD|
|Number in seed:||7|
|Number in full:||497|
|Average length of the domain:||565.40 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||61.09 %|
|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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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 Arabinose_trans domain has been found. There are 8 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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