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CAZyme Information: P170DRAFT_379008-t37_1-p1

You are here: Home > Sequence: P170DRAFT_379008-t37_1-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 steynii
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
CAZyme ID P170DRAFT_379008-t37_1-p1
CAZy Family CE5
CAZyme Description putative beta-N-acetylglucosaminidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
859 MSFO01000002|CGC15 94408.96 5.7761
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AsteyniiIBT23096 13430 1392250 235 13195
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.52:8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH3 68 291 3.2e-61 0.9629629629629629

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
224389 BglX 2.30e-87 6 428 3 396
Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism].
395747 Glyco_hydro_3 1.19e-82 6 330 2 316
Glycosyl hydrolase family 3 N terminal domain.
235417 PRK05337 6.13e-47 26 294 17 281
beta-hexosaminidase; Provisional
185053 PRK15098 3.23e-13 6 331 47 353
beta-glucosidase BglX.
173926 NAT_SF 5.54e-08 585 641 1 56
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 859 1 865
0.0 1 859 1 865
0.0 1 855 1 852
0.0 5 857 5 852
0.0 1 859 1 859

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.84e-152 6 855 9 856
A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase [Rhizomucor miehei CAU432],4ZM6_B A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase [Rhizomucor miehei CAU432]
3.44e-95 6 538 13 534
Structure of a glycoside hydrolase family 3 beta-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7 [Paenibacillaceae]
7.07e-58 11 329 19 329
The crystal structure of glycosyl hydrolase from Deinococcus radiodurans R1 [Deinococcus radiodurans R1],3TEV_B The crystal structure of glycosyl hydrolase from Deinococcus radiodurans R1 [Deinococcus radiodurans R1]
5.18e-57 26 399 76 466
Beta-N-hexosaminidase (YbbD) from Bacillus subtilis [Bacillus subtilis],3BMX_B Beta-N-hexosaminidase (YbbD) from Bacillus subtilis [Bacillus subtilis],3NVD_A Structure of YBBD in complex with pugnac [Bacillus subtilis],3NVD_B Structure of YBBD in complex with pugnac [Bacillus subtilis]
1.58e-56 26 399 50 440
Chain A, Lipoprotein ybbD [Bacillus subtilis],3LK6_B Chain B, Lipoprotein ybbD [Bacillus subtilis],3LK6_C Chain C, Lipoprotein ybbD [Bacillus subtilis],3LK6_D Chain D, Lipoprotein ybbD [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.66e-56 26 399 76 466
Beta-hexosaminidase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagZ PE=1 SV=1
2.05e-55 22 331 50 380
Beta-hexosaminidase A OS=Pseudoalteromonas piscicida OX=43662 GN=cht60 PE=1 SV=1
1.96e-40 13 341 1 315
Beta-hexosaminidase OS=Xylella fastidiosa (strain Temecula1 / ATCC 700964) OX=183190 GN=nagZ PE=3 SV=1
1.96e-40 13 341 1 315
Beta-hexosaminidase OS=Xylella fastidiosa (strain M23) OX=405441 GN=nagZ PE=3 SV=1
1.24e-39 13 341 1 315
Beta-hexosaminidase OS=Xylella fastidiosa (strain 9a5c) OX=160492 GN=nagZ PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000048 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in P170DRAFT_379008-t37_1-p1.