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CAZyme Information: AO090701000899-T-p1

You are here: Home > Sequence: AO090701000899-T-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus oryzae
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
CAZyme ID AO090701000899-T-p1
CAZy Family GT69
CAZyme Description Has domain(s) with predicted hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds activity and role in carbohydrate metabolic process
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
696 Chr5_A_oryzae_RIB40|CGC8 79491.35 5.9984
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AoryzaeRIB40 12364 510516 274 12090
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in AO090701000899-T-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE4 45 149 1.6e-20 0.7846153846153846

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200563 CE4_HpPgdA_like 3.08e-94 8 230 2 203
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 6.41e-41 8 230 2 194
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.
369159 HET 2.60e-37 234 396 1 146
Heterokaryon incompatibility protein (HET). This family represents a conserved region approximately 150 residues long within various heterokaryon incompatibility proteins that seem to be restricted to ascomycete fungi. Genetic differences in specific het genes prevent a viable heterokaryotic fungal cell from being formed by the fusion of filaments from two different wild-type strains. Many family members also contain the pfam00400 repeat and the pfam05729 domain.
223798 CDA1 1.93e-22 43 154 79 192
Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
200566 CE4_PuuE_HpPgdA_like_2 2.74e-21 24 151 17 141
Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). 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 homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of 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, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.55e-41 232 523 868 1167
3.24e-22 28 246 38 233
5.98e-14 27 138 54 164
6.64e-14 44 139 25 120
8.10e-13 32 146 30 151

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.80e-104 4 239 36 272
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]
6.33e-22 4 241 23 237
Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_B Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_C Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_D Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155]
1.94e-11 44 130 36 122
Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]
2.17e-10 44 124 36 116
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]
4.76e-10 44 124 88 168
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.07e-104 4 239 3 239
Peptidoglycan deacetylase OS=Helicobacter pylori (strain G27) OX=563041 GN=pgdA PE=1 SV=1
5.25e-102 4 239 3 239
Peptidoglycan deacetylase OS=Helicobacter pylori (strain ATCC 700392 / 26695) OX=85962 GN=pgdA PE=1 SV=1
1.86e-58 3 254 37 293
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
2.37e-10 44 130 96 182
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
1.07e-06 44 124 82 169
Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000031 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in AO090701000899-T-p1.