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InterPro: IPR003737 N-acetylglucosaminyl phosphatidylinositol deacetylase

Protein matchesHelp
UniProtKB
Matches:
1755 proteins
AccessionHelp IPR003737 GlcNAc_PIno_de-acetylase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR017810 Mycothiol biosynthesis protein, MshB
IPR017811 Mycothiol conjugate amidase, Mca
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

A number of the members of this family have been characterised as a probable N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase, (EC:3.5.1.89) that catalyses the second step in glycosylphosphatidylinositol (GPI) biosynthesis [1, 2].

Structural linksHelp
SCOP: c.134.1.1
Database linksHelp
Enzyme: EC:3
PANDIT: PF02585
Blocks: IPB003737

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003737 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O31857 Uncharacterized deacetylase yojG

P23797 N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase

Q5SX19 N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase

Q5UQW3 Uncharacterized protein L374

Q9Y2B2 N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003737 N-acetylglucosaminyl phosphatidylinositol deacetylase
SWISS-MODEL
ModBase

PublicationsHelp
1. Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T.
Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis.
Biochem. J. 339 ( Pt 1) 185-92 1999 [PubMed: 10085243]
http://dx.doi.org/10.1042/0264-6021:3390185
2. Maynes JT, Garen C, Cherney MM, Newton G, Arad D, Av-Gay Y, Fahey RC, James MN.
The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold.
J. Biol. Chem. 278 47166-70 2003 [PubMed: 12958317]
http://dx.doi.org/10.1074/jbc.M308914200

Additional ReadingHelp
Fadouloglou VE, Kotsifaki D, Gazi AD, Fellas G, Meramveliotaki C, Deli A, Psylinakis E, Bouriotis V, Kokkinidis M.
Purification, crystallization and preliminary characterization of a putative LmbE-like deacetylase from Bacillus cereus.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 261-4 [PubMed: 16511317]
Fadouloglou VE, Deli A, Glykos NM, Psylinakis E, Bouriotis V, Kokkinidis M.
Crystal structure of the BcZBP, a zinc-binding protein from Bacillus cereus.
FEBS J. 274 2007 3044-54 [PubMed: 17501983]
http://dx.doi.org/10.1111/j.1742-4658.2007.05834.x
Aggarwal VK, Grainger RS, Newton GK, Spargo PL, Hobson AD, Adams H.
Highly diastereoselective 1,3-dipolar cycloaddition reactions of trans-2-methylene-1,3-dithiolane 1,3-dioxide with 3-oxidopyridinium and 3-oxidopyrylium betaines: a route to the tropane skeleton.
Org. Biomol. Chem. 1 2003 1884-93 [PubMed: 12945769]
http://dx.doi.org/10.1039/b302834h
Handa N, Terada T, Kamewari Y, Hamana H, Tame JR, Park SY, Kinoshita K, Ota M, Nakamura H, Kuramitsu S, Shirouzu M, Yokoyama S.
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.
Protein Sci. 12 2003 1621-32 [PubMed: 12876312]
http://dx.doi.org/10.1110/ps.g03104003
McCarthy AA, Peterson NA, Knijff R, Baker EN.
Crystal structure of MshB from Mycobacterium tuberculosis, a deacetylase involved in mycothiol biosynthesis.
J. Mol. Biol. 335 2004 1131-41 [PubMed: 14698305]
http://dx.doi.org/10.1016/j.jmb.2003.11.034
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InterPro 23.1