Summary: GlcNAc-PI de-N-acetylase
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GlcNAc-PI de-N-acetylase Provide feedback
Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase ( EC:126.96.36.199) that catalyses the second step in GPI biosynthesis [1,2].
Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T; , Biochem J 1999;339:185-192.: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. PUBMED:10085243 EPMC:10085243
Handa N, Terada T, Kamewari Y, Hamana H, Tame JR, Park SY, Kinoshita K, Ota M, Nakamura H, Kuramitsu S, Shirouzu M, Yokoyama S;, Protein Sci. 2003;12:1621-1632.: Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8. PUBMED:12876312 EPMC:12876312
Internal database links
|SCOOP:||PGM_PMM_II iPGM_N PglZ|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003737
Members of this family include N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase (EC) that catalyses the second step in glycosylphosphatidylinositol (GPI) biosynthesis [PUBMED:10085243, PUBMED:12958317] and 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase (EC), involved in the biosynthesis of mycothiol (an unusual thiol compound found in Actinobacteria) [PUBMED:11092856].
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Curation and family details
|Author:||Mian N, Bateman A|
|Number in seed:||70|
|Number in full:||20129|
|Average length of the domain:||135.20 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||49.60 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|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 PIG-L domain has been found. There are 29 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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