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CAZyme Information: CPSG_02109-t26_1-p1

You are here: Home > Sequence: CPSG_02109-t26_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 Coccidioides posadasii
Lineage Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii
CAZyme ID CPSG_02109-t26_1-p1
CAZy Family AA7
CAZyme Description beta-hexosaminidase subunit beta
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
603 68499.01 6.7121
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CposadasiiSilveira 10379 443226 154 10225
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.52:9

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 208 557 6.1e-79 0.973293768545994

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119332 GH20_HexA_HexB-like 3.69e-151 213 580 1 346
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
395590 Glyco_hydro_20 2.38e-100 214 557 2 345
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333 GH20_chitobiase-like 1.32e-49 214 562 2 349
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
119338 GH20_chitobiase-like_1 4.11e-45 216 562 4 303
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
119336 GH20_SpHex_like 8.12e-45 214 562 2 321
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 603 1 603
5.47e-274 10 603 8 602
5.47e-274 10 603 8 602
8.97e-273 10 603 8 602
9.16e-228 10 539 8 539

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.40e-69 89 601 74 570
Crystal structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with naphthalimide derivative Q1 [Ostrinia furnacalis],3WMC_A Crystal structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with naphthalimide derivative Q2 [Ostrinia furnacalis]
2.74e-69 89 601 74 570
Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]
4.67e-69 89 601 74 570
Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 from Ostrinia furnacalis [Ostrinia furnacalis],3NSN_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with TMG-chitotriomycin [Ostrinia furnacalis],3OZO_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with NGT [Ostrinia furnacalis],3OZP_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with PUGNAc [Ostrinia furnacalis]
2.62e-68 89 601 77 573
Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
3.89e-68 89 601 74 570
Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with berberine [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.38e-275 17 603 16 605
Beta-hexosaminidase ARB_07893 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07893 PE=1 SV=1
1.26e-81 156 602 115 571
Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
3.85e-68 89 601 96 592
Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Ostrinia furnacalis OX=93504 PE=1 SV=1
1.48e-67 156 603 121 587
Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
2.93e-67 156 601 150 594
Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Bombyx mori OX=7091 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000304 0.999664 CS pos: 19-20. Pr: 0.9716

TMHMM  Annotations      help

There is no transmembrane helices in CPSG_02109-t26_1-p1.