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Conserved domains on  [gi|193210765|ref|NP_499390|]
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beta-N-acetylhexosaminidase [Caenorhabditis elegans]

Protein Classification

beta-N-acetylhexosaminidase( domain architecture ID 10159022)

beta-N-acetylhexosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 112-425 5.95e-90

Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.


:

Pssm-ID: 119335  Cd Length: 301  Bit Score: 279.86  E-value: 5.95e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 112 RIVHLDLKG-APYKPEFFTELFAFFNRIQATGILLEWEDMFPFKGRLRGAINKNAYSMETVEHILQEAQKHHLQIIPLVQ 190
Cdd:cd06565    2 RGVHLDLKRnAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLIQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 191 TMGHLEWILKLEEFAHLREDTRFPQVICFSDENAWELIKEMIEEVANVHKKygmSYFHIGADEAFQIGICNASitQIKKE 270
Cdd:cd06565   82 TLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHPS---KYIHIGMDEAYDLGRGRSL--RKHGN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 271 FTRERLMLWHIARTARFVKEKYPetQVLAWHDMLASAMESDIEDYKLTELLQPVLWNYAEDLD-IYLPRSTWM-ILRNFR 348
Cdd:cd06565  157 LGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDeHDRPIGLWKkYGSVFA 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210765 349 NVWGSSAWKGADGPARystnanHYLKNHESWIKQftmvyKDFEVVEGLIMAGWSRYDHFAVLAETIPVALPTLAMSM 425
Cdd:cd06565  235 VAWGASAWKGATPPND------KHLENIKSWLKA-----AKKNGVQGILLTGWGDYGHEAVLCELLPGLIPSLALAL 300
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 112-425 5.95e-90

Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.


Pssm-ID: 119335  Cd Length: 301  Bit Score: 279.86  E-value: 5.95e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 112 RIVHLDLKG-APYKPEFFTELFAFFNRIQATGILLEWEDMFPFKGRLRGAINKNAYSMETVEHILQEAQKHHLQIIPLVQ 190
Cdd:cd06565    2 RGVHLDLKRnAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLIQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 191 TMGHLEWILKLEEFAHLREDTRFPQVICFSDENAWELIKEMIEEVANVHKKygmSYFHIGADEAFQIGICNASitQIKKE 270
Cdd:cd06565   82 TLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHPS---KYIHIGMDEAYDLGRGRSL--RKHGN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 271 FTRERLMLWHIARTARFVKEKYPetQVLAWHDMLASAMESDIEDYKLTELLQPVLWNYAEDLD-IYLPRSTWM-ILRNFR 348
Cdd:cd06565  157 LGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDeHDRPIGLWKkYGSVFA 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210765 349 NVWGSSAWKGADGPARystnanHYLKNHESWIKQftmvyKDFEVVEGLIMAGWSRYDHFAVLAETIPVALPTLAMSM 425
Cdd:cd06565  235 VAWGASAWKGATPPND------KHLENIKSWLKA-----AKKNGVQGILLTGWGDYGHEAVLCELLPGLIPSLALAL 300
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 166-304 2.16e-06

Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.


Pssm-ID: 425840  Cd Length: 344  Bit Score: 49.99  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765  166 YSMETVEHILQEAQKHHLQIIPLVQTMGH-LEWILKLEEFA----------HLREDTrFPQVICFSDENAWELIKEMIEE 234
Cdd:pfam00728  75 YTQEDIREIVAYAAARGIRVIPEIDMPGHaRAALAAYPELGcgcgadspwvSVQWGP-PEGQLNPGNEKTYTFLDNVFDE 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193210765  235 VANVHKKygmSYFHIGADEAF--QIGICNASITQIKKE--FTRERLMLWHIARTARFVKEKypETQVLAWHDML 304
Cdd:pfam00728 154 VADLFPS---DYIHIGGDEVPkgCWEKSPECQARMKEEglKSLHELQQYFIKRASKIVSSK--GRRLIGWDEIL 222
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 112-425 5.95e-90

Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.


Pssm-ID: 119335  Cd Length: 301  Bit Score: 279.86  E-value: 5.95e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 112 RIVHLDLKG-APYKPEFFTELFAFFNRIQATGILLEWEDMFPFKGRLRGAINKNAYSMETVEHILQEAQKHHLQIIPLVQ 190
Cdd:cd06565    2 RGVHLDLKRnAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLIQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 191 TMGHLEWILKLEEFAHLREDTRFPQVICFSDENAWELIKEMIEEVANVHKKygmSYFHIGADEAFQIGICNASitQIKKE 270
Cdd:cd06565   82 TLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHPS---KYIHIGMDEAYDLGRGRSL--RKHGN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 271 FTRERLMLWHIARTARFVKEKYPetQVLAWHDMLASAMESDIEDYKLTELLQPVLWNYAEDLD-IYLPRSTWM-ILRNFR 348
Cdd:cd06565  157 LGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDeHDRPIGLWKkYGSVFA 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210765 349 NVWGSSAWKGADGPARystnanHYLKNHESWIKQftmvyKDFEVVEGLIMAGWSRYDHFAVLAETIPVALPTLAMSM 425
Cdd:cd06565  235 VAWGASAWKGATPPND------KHLENIKSWLKA-----AKKNGVQGILLTGWGDYGHEAVLCELLPGLIPSLALAL 300
GH20_hexosaminidase cd02742
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ...
 166-328 9.04e-10

Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) 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. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.


Pssm-ID: 119331 [Multi-domain]  Cd Length: 303  Bit Score: 60.14  E-value: 9.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 166 YSMETVEHILQEAQKHHLQIIPLVQTMGHLEWILKL--EEFAHLREDTRFPQV---ICFSDENAWELIKEMIEEVANVHK 240
Cdd:cd02742   69 YTYAQLKDIIEYAAARGIEVIPEIDMPGHSTAFVKSfpKLLTECYAGLKLRDVfdpLDPTLPKGYDFLDDLFGEIAELFP 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 241 KygmSYFHIGADEAfqigicnasitqiKKEFTRERLMLWHIARTARFVKEKYPETQVlaWHDMLasamesdIEDYKLTEL 320
Cdd:cd02742  149 D---RYLHIGGDEA-------------HFKQDRKHLMSQFIQRVLDIVKKKGKKVIV--WQDGF-------DKKMKLKED 203


                 ....*...
gi 193210765 321 LQPVLWNY 328
Cdd:cd02742  204 VIVQYWDY 211
GH20_DspB_LnbB-like cd06564
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ...
 111-304 3.13e-07

Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.


Pssm-ID: 119334  Cd Length: 326  Bit Score: 52.67  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 111 RRIVHLDLKGAPYKPEF---FTELFAFF-----------NRIQATGILLEWEDM-----FPFKGRLRGAI---NKNAYSM 168
Cdd:cd06564    2 VRGFMLDVGRKYYSMDFlkdIIKTMSWYkmndlqlhlndNLIFNLDDMSTTVNNatyasDDVKSGNNYYNltaNDGYYTK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 169 ETVEHILQEAQKHHLQIIPLVQTMGHLEWILKleefahLREDTRFPQVICFSDEN--------AWELIKEMIEEVANVHK 240
Cdd:cd06564   82 EEFKELIAYAKDRGVNIIPEIDSPGHSLAFTK------AMPELGLKNPFSKYDKDtldisnpeAVKFVKALFDEYLDGFN 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193210765 241 KYGMsYFHIGADEAfqigicnASITQIKKEFTRerlmlwHIARTARFVKEKYPetQVLAWHDML 304
Cdd:cd06564  156 PKSD-TVHIGADEY-------AGDAGYAEAFRA------YVNDLAKYVKDKGK--TPRVWGDGI 203
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 166-304 2.16e-06

Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.


Pssm-ID: 425840  Cd Length: 344  Bit Score: 49.99  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765  166 YSMETVEHILQEAQKHHLQIIPLVQTMGH-LEWILKLEEFA----------HLREDTrFPQVICFSDENAWELIKEMIEE 234
Cdd:pfam00728  75 YTQEDIREIVAYAAARGIRVIPEIDMPGHaRAALAAYPELGcgcgadspwvSVQWGP-PEGQLNPGNEKTYTFLDNVFDE 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193210765  235 VANVHKKygmSYFHIGADEAF--QIGICNASITQIKKE--FTRERLMLWHIARTARFVKEKypETQVLAWHDML 304
Cdd:pfam00728 154 VADLFPS---DYIHIGGDEVPkgCWEKSPECQARMKEEglKSLHELQQYFIKRASKIVSSK--GRRLIGWDEIL 222
GH20_chitobiase-like cd06563
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl ...
 166-304 6.11e-04

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.


Pssm-ID: 119333  Cd Length: 357  Bit Score: 42.18  E-value: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 166 YSMETVEHILQEAQKHHLQIIPLVQTMGHLEWILK-LEEF------AHLREDTRFPQ-VICFSDENAWELIKEMIEEVAN 237
Cdd:cd06563   83 YTQEEIREIVAYAAERGITVIPEIDMPGHALAALAaYPELgctggpGSVVSVQGVVSnVLCPGKPETYTFLEDVLDEVAE 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193210765 238 VHKKygmSYFHIGADEA--FQIGICNASITQIKKE-FTRER-LMLWHIARTARFVKEKypETQVLAWHDML 304
Cdd:cd06563  163 LFPS---PYIHIGGDEVpkGQWEKSPACQARMKEEgLKDEHeLQSYFIKRVEKILASK--GKKMIGWDEIL 228
GH20_SpHex_like cd06568
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins ...
 159-310 3.48e-03

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.


Pssm-ID: 119336  Cd Length: 329  Bit Score: 40.01  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 159 GAINKNAYSMETVEHILQEAQKHHLQIIPLVQTMGHLEWILklEEFAHLREDTRFPQV----------ICFSDENAWELI 228
Cdd:cd06568   65 GGGPGGYYTQEDYKDIVAYAAERHITVVPEIDMPGHTNAAL--AAYPELNCDGKAKPLytgievgfssLDVDKPTTYEFV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210765 229 KEMIEEVAnvhkkyGMS---YFHIGADEAfqigicnasITQIKKEFTRerlmlwHIARTARFVkEKYPETqVLAWHDMLA 305
Cdd:cd06568  143 DDVFRELA------ALTpgpYIHIGGDEA---------HSTPHDDYAY------FVNRVRAIV-AKYGKT-PVGWQEIAR 199


                 ....*
gi 193210765 306 SAMES 310
Cdd:cd06568  200 ADLPA 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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