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Information on EC 3.1.1.58 - N-acetylgalactosaminoglycan deacetylase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.58 N-acetylgalactosaminoglycan deacetylase
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UNIPROT: P69434 not found.
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
de-n-acetylase, polysaccharide deacetylase, bc0361, ba0150, pnag de-n-acetylase, n-acetyl galactosaminoglycan deacetylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PgaA
encoded within pgaABCD operon, BLAST analyses: not related to a protein of known function
deacetylase, polysaccharide
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N-acetyl galactosaminoglycan deacetylase
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polysaccharide deacetylase
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Vi-polysaccharide deacetylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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SYSTEMATIC NAME
IUBMB Comments
N-acetyl-D-galactosaminoglycan acetylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
52410-59-0
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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
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
predicted beta-barrel porin of PgaA that forms outer membrane secretin for poly-beta-1,6-N-acetyl-D-glucosamine (PGA) and promotes its export from periplasm in response to N-deacetylation by PgaB, defective PGA secretion in PgaA-deficient mutant strain
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGAA_ECOLI
Escherichia coli (strain K12)
807
0
92207
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alignment with PDB database: hits to tetratricopeptide repeat domains of human nucleoporin O-linked N-acetylglucosamine transferase, yeast mitochondrial outer membrane translocon protein Tom70p, and human peroxisomal targeting signal-1 receptor PEX5, putative domains: porin domain for export of poly-beta-1,6-N-acetyl-D-glucosamine, and periplasmic domain for protein-protein interactions
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
increased temperature might improve poly-beta-1,6-N-acetyl-D-glucosamine export in absence of deacetylation by PgaB
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, Y.; Rice, J.D.; Goller, C.; Pannuri, A.; Taylor, J.; Meisner, J.; Beveridge, T.J.; Preston, J.F.; Romeo, T.
Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine
J. Bacteriol.
190
3670-3680
2008
Escherichia coli (P69434), Escherichia coli (P75906), Escherichia coli K-12 MG1655 (P69434), Escherichia coli K-12 MG1655 (P75906)
Manually annotated by BRENDA team