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Information on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase and Organism(s) Drosophila melanogaster and UniProt Accession Q7KRR5

for references in articles please use BRENDA:EC3.5.1.52
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EC Tree
IUBMB Comments
Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(beta-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
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Select one or more organisms in this record: ?
This record set is specific for:
Drosophila melanogaster
UNIPROT: Q7KRR5
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
n-glycanase, pngase f, n-glycosidase f, pngase, peptide n-glycosidase f, ngly1, peptide-n-glycosidase f, glycopeptidase, peptide:n-glycosidase, peptide:n-glycanase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptide:N-glycanase
-
acid PNGase M
-
-
-
-
glycopeptidase
-
-
-
-
glycopeptide N-glycosidase
-
-
-
-
jackbean glycopeptidase
-
-
-
-
L-929 PNGase
-
-
-
-
N-glycanase
-
-
-
-
N-oligosaccharide glycopeptidase
-
-
-
-
neutral PNGase M
-
-
-
-
peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
-
-
-
-
peptide:N-glycanase
-
-
PNGase A
-
-
-
-
PNGase At
-
-
-
-
PNGase F
-
-
-
-
PNGase J
-
-
-
-
PNGase Os
-
-
-
-
PNGase Se
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic acid amide
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine amidohydrolase
Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(beta-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
CAS REGISTRY NUMBER
COMMENTARY hide
83534-39-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the Drosophila ortholog of PNGase (PngI) does not possess deglycosylation activity but retains carbohydrate-binding activity. The transglutaminase domain of Pngl participates in some type of catalytic activity even though the protein does not have the conventional deglycosylation activity
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are global developmental delay, movement disorder, and hypotonia
malfunction
-
homozygous deletion mutants show developmental defect
physiological function
-
the enzyme plays a critical role during larval development and metamorphosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NGLY1_DROME
631
0
73316
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
-
x * 74000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 74000, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PNG1, sequence comparisons and phylogenetic analysis
expressed in Sf21 insect cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Funakoshi, Y.; Negishi, Y.; Gergen, J.P.; Seino, J.; Ishii, K.; Lennarz, W.J.; Matsuo, I.; Ito, Y.; Taniguchi, N.; Suzuki, T.
Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster
PLoS ONE
5
e10545
2010
Saccharomyces cerevisiae, Drosophila melanogaster
Manually annotated by BRENDA team
Suzuki, T.
The cytoplasmic peptide N-glycanase (Ngly1) - basic science encounters a human genetic disorder
J. Biochem.
157
23-34
2015
Oryzias latipes, Neurospora crassa (D1MY48), Schizosaccharomyces pombe (O74739), Saccharomyces cerevisiae (Q02890), Saccharomyces cerevisiae, Dictyostelium discoideum (Q55FC8), Drosophila melanogaster (Q7KRR5), Homo sapiens (Q96IV0), Homo sapiens, Arabidopsis thaliana (Q9FGY9), Mus musculus (Q9JI78), Caenorhabditis elegans (Q9TW67), Schizosaccharomyces pombe ATCC 24843 (O74739), Schizosaccharomyces pombe 972 (O74739), Saccharomyces cerevisiae ATCC 204508 (Q02890)
Manually annotated by BRENDA team