Summary: Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain
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Glycoside hydrolase family 89 Edit Wikipedia article
|Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain|
|Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain|
|Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain|
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 89 CAZY GH_89 includes enzymes with α-N-acetylglucosaminidase EC 18.104.22.168 activity. The enzyme consist of three structural domains, the N-terminal domain has an alpha-beta fold, the central domain has a TIM barrel fold, and the C-terminal domain has an all alpha helical fold.
Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterised by neurological dysfunction but relatively mild somatic manifestations.
- Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- Ficko-Blean E, Stubbs KA, Nemirovsky O, Vocadlo DJ, Boraston AB (2008). "Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB.". Proc Natl Acad Sci U S A 105 (18): 6560–5. doi:10.1073/pnas.0711491105. PMC 2373330. PMID 18443291.
- Li HH, Yu WH, Rozengurt N, Zhao HZ, Lyons KM, Anagnostaras S, Fanselow MS, Suzuki K, Vanier MT, Neufeld EF (December 1999). "Mouse model of Sanfilippo syndrome type B produced by targeted disruption of the gene encoding alpha-N-acetylglucosaminidase". Proc. Natl. Acad. Sci. U.S.A. 96 (25): 14505–10. doi:10.1073/pnas.96.25.14505. PMC 24466. PMID 10588735.
- Villani GR, Follenzi A, Vanacore B, Di Domenico C, Naldini L, Di Natale P (June 2002). "Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer". Biochem. J. 364 (Pt 3): 747–53. doi:10.1042/BJ20011872. PMC 1222624. PMID 12049639.
Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain Provide feedback
Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate . Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterised by neurological dysfunction but relatively mild somatic manifestations . The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold .
Li HH, Yu WH, Rozengurt N, Zhao HZ, Lyons KM, Anagnostaras S, Fanselow MS, Suzuki K, Vanier MT, Neufeld EF; , Proc Natl Acad Sci U S A 1999;96:14505-14510.: Mouse model of Sanfilippo syndrome type B produced by targeted disruption of the gene encoding alpha-N-acetylglucosaminidase. PUBMED:10588735 EPMC:10588735
Villani GR, Follenzi A, Vanacore B, Di Domenico C, Naldini L, Di Natale P; , Biochem J 2002;364:747-753.: Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer. PUBMED:12049639 EPMC:12049639
Ficko-Blean E, Stubbs KA, Nemirovsky O, Vocadlo DJ, Boraston AB;, Proc Natl Acad Sci U S A. 2008;105:6560-6565.: Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB. PUBMED:18443291 EPMC:18443291
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024733
Alpha-N-acetylglucosaminidase is a lysosomal enzyme that is required for the stepwise degradation of heparan sulphate [PUBMED:10588735]. Mutations on the alpha-N-acetylglucosaminidase gene can lead to mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B), characterised by neurological dysfunction but relatively mild somatic manifestations [PUBMED:12049639].
Alpha-N-acetylglucosaminidase is composed of three domains. This entry represents the central domain, which has a tim barrel fold [PUBMED:18443291].
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This large superfamily contains a range of glycosyl hydrolase enzymes that possess a TIM barrel fold. This CLAN merges clans GH-A, GH-D, GH-H and GH-K from CAZy.
The clan contains the following 50 members:Alpha-amylase Alpha_L_fucos Cellulase Cellulase-like DUF187 DUF4015 DUF4038 DUF4434 GHL1-3 GHL12 GHL13 GHL15 GHL5 GHL6 Glyco_hydr_30_2 Glyco_hydro_1 Glyco_hydro_10 Glyco_hydro_101 Glyco_hydro_114 Glyco_hydro_14 Glyco_hydro_17 Glyco_hydro_18 Glyco_hydro_20 Glyco_hydro_25 Glyco_hydro_26 Glyco_hydro_2_C Glyco_hydro_3 Glyco_hydro_30 Glyco_hydro_31 Glyco_hydro_35 Glyco_hydro_39 Glyco_hydro_42 Glyco_hydro_44 Glyco_hydro_53 Glyco_hydro_56 Glyco_hydro_59 Glyco_hydro_66 Glyco_hydro_70 Glyco_hydro_72 Glyco_hydro_77 Glyco_hydro_79n Glyco_hydro_97 Glyco_hydro_cc hDGE_amylase Lipid_bd Melibiase NAGidase NAGLU Raffinose_syn Xylanase
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Curation and family details
|Seed source:||Pfam-B_6295 (release 7.7)|
|Author:||Moxon SJ, Bateman A|
|Number in seed:||30|
|Number in full:||411|
|Average length of the domain:||304.40 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||38.80 %|
|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 NAGLU domain has been found. There are 5 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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