Species | Aspergillus niger | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger | |||||||||||
CAZyme ID | ASPNIDRAFT2_1098404-t41_1-p1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | Glycoside hydrolase/deacetylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE4 | 10 | 151 | 6.5e-21 | 0.9153846153846154 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
200567 | CE4_u11 | 2.09e-110 | 13 | 208 | 1 | 196 | Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily. |
200563 | CE4_HpPgdA_like | 4.42e-31 | 13 | 171 | 1 | 170 | Catalytic domain of Helicobacter pylori peptidoglycan deacetylase (HpPgdA) and similar proteins. This family is represented by a peptidoglycan deacetylase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori. HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. It functions as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, HpPgdA does not exhibit a solvent-accessible polysaccharide binding groove, suggesting that the enzyme binds a small molecule at the active site. |
213021 | CE4_PuuE_HpPgdA_like | 4.93e-25 | 13 | 191 | 1 | 203 | Catalytic domain of bacterial PuuE allantoinases, Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and similar proteins. This family is a member of the very large and functionally diverse carbohydrate esterase 4 (CE4) superfamily. It contains bacterial PuuE (purine utilization E) allantoinases, a peptidoglycan deacetylase from Helicobacter pylori (HpPgdA), Escherichia coli ArnD, and many uncharacterized homologs from all three kingdoms of life. PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. However, in contrast with the typical DCAs, PuuE allantoinase and HpPgdA might not exhibit a solvent-accessible polysaccharide binding groove and only recognize a small substrate molecule. ArnD catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. |
396211 | Polysacc_deac_1 | 1.33e-24 | 46 | 150 | 19 | 124 | Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan. |
223798 | CDA1 | 8.54e-22 | 46 | 148 | 78 | 181 | Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.20e-63 | 2 | 193 | 6 | 194 | |
5.06e-57 | 2 | 203 | 4 | 202 | |
8.33e-53 | 3 | 206 | 2 | 202 | |
1.69e-17 | 3 | 175 | 5 | 187 | |
7.57e-15 | 8 | 135 | 51 | 158 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.21e-14 | 49 | 187 | 77 | 212 | Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_B Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_C Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_D Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],4LY4_A Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_B Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_C Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_D Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27] |
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2.65e-09 | 45 | 134 | 33 | 123 | Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579] |
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3.30e-08 | 45 | 134 | 33 | 123 | Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_C Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_D Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579] |
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3.76e-08 | 46 | 133 | 98 | 186 | Crystal structure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis] |
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4.98e-08 | 45 | 134 | 85 | 175 | Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus [Bacillus cereus ATCC 14579],4L1G_B Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus [Bacillus cereus ATCC 14579],4L1G_C Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus [Bacillus cereus ATCC 14579],4L1G_D Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus [Bacillus cereus ATCC 14579] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.78e-14 | 49 | 187 | 44 | 179 | Peptidoglycan deacetylase OS=Helicobacter pylori (strain G27) OX=563041 GN=pgdA PE=1 SV=1 |
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2.96e-12 | 49 | 187 | 44 | 179 | Peptidoglycan deacetylase OS=Helicobacter pylori (strain ATCC 700392 / 26695) OX=85962 GN=pgdA PE=1 SV=1 |
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1.82e-09 | 51 | 156 | 82 | 191 | Peptidoglycan deacetylase-like protein FGM2 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FGM2 PE=2 SV=1 |
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2.33e-09 | 51 | 141 | 148 | 239 | Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2 |
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2.22e-08 | 45 | 134 | 93 | 183 | Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_1960 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000058 | 0.000000 |
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