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Conserved domains on  [gi|767997374|ref|XP_011521862|]
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hexosaminidase D isoform X2 [Homo sapiens]

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, ...
 24-287 1.60e-104

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: 316.07  E-value: 1.60e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  24 PKFWS-----SPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVGAMIDQVL 98
Cdd:cd06565   48 PEVGRmrgayTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  99 ELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGKLCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPEDQLAASGV 178
Cdd:cd06565  128 ELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374 179 PQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAASAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPTDSLQGII 258
Cdd:cd06565  202 PKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGAT------PPNDKHLENIKSWLKAA---KKNGVQGIL 272

                        250       260
                 ....*....|....*....|....*....
gi 767997374 259 LTGWQRYDHYSVLCELLPAGVPSLAACLQ 287
Cdd:cd06565  273 LTGWGDYGHEAVLCELLPGLIPSLALALG 301
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 24-287 1.60e-104

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: 316.07  E-value: 1.60e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  24 PKFWS-----SPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVGAMIDQVL 98
Cdd:cd06565   48 PEVGRmrgayTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  99 ELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGKLCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPEDQLAASGV 178
Cdd:cd06565  128 ELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374 179 PQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAASAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPTDSLQGII 258
Cdd:cd06565  202 PKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGAT------PPNDKHLENIKSWLKAA---KKNGVQGIL 272

                        250       260
                 ....*....|....*....|....*....
gi 767997374 259 LTGWQRYDHYSVLCELLPAGVPSLAACLQ 287
Cdd:cd06565  273 LTGWGDYGHEAVLCELLPGLIPSLALALG 301
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 9-167 2.19e-05

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


Pssm-ID: 425840  Cd Length: 344  Bit Score: 46.91  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374    9 LKSEPLL--------EDVLEHHLPKFWSsPSEIKEILHLAGLNELEVIPLVQTFGHM--------EFVLKHTAFAHLR-- 70
Cdd:pfam00728  49 IKKYPKLtekgayrpSDLDGTPYGGFYT-QEDIREIVAYAAARGIRVIPEIDMPGHAraalaaypELGCGCGADSPWVsv 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374   71 EVGSFPCTLNPHEAESLALVGAMIDQVLELHPGaQRLHIGCDEVyylgegeASRRWLQ----QEQNSTGKLCLSH----- 141
Cdd:pfam00728 128 QWGPPEGQLNPGNEKTYTFLDNVFDEVADLFPS-DYIHIGGDEV-------PKGCWEKspecQARMKEEGLKSLHelqqy 199

                         170       180
                  ....*....|....*....|....*..
gi 767997374  142 -MRAVASGVKARRPsvTPLVWDDMLRD 167
Cdd:pfam00728 200 fIKRASKIVSSKGR--RLIGWDEILDG 224
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 24-287 1.60e-104

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: 316.07  E-value: 1.60e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  24 PKFWS-----SPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVGAMIDQVL 98
Cdd:cd06565   48 PEVGRmrgayTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  99 ELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGKLCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPEDQLAASGV 178
Cdd:cd06565  128 ELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374 179 PQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAASAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPTDSLQGII 258
Cdd:cd06565  202 PKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGAT------PPNDKHLENIKSWLKAA---KKNGVQGIL 272

                        250       260
                 ....*....|....*....|....*....
gi 767997374 259 LTGWQRYDHYSVLCELLPAGVPSLAACLQ 287
Cdd:cd06565  273 LTGWGDYGHEAVLCELLPGLIPSLALALG 301
GH20_hexosaminidase cd02742
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ...
 29-262 2.75e-08

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: 55.52  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  29 SPSEIKEILHLAGLNELEVIPLVQTFGHMefvlkhTAFAHLREVGSFPCT-----------LNPHEAESLALVGAMIDQV 97
Cdd:cd02742   70 TYAQLKDIIEYAAARGIEVIPEIDMPGHS------TAFVKSFPKLLTECYaglklrdvfdpLDPTLPKGYDFLDDLFGEI 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  98 LELHPGaQRLHIGCDEVYYLGEGEASrrwlqqeqNSTgklclsHMRAVASGVKARrpSVTPLVWDDMLRDLPEdqlaasg 177
Cdd:cd02742  144 AELFPD-RYLHIGGDEAHFKQDRKHL--------MSQ------FIQRVLDIVKKK--GKKVIVWQDGFDKKMK------- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374 178 VPQLVEPVLWDYTADLDVHGKVLLMQKyrrcGFPQLWAASAFKGATGPSQavppveHHLRNHVQW--LQVAGSGPTDSLQ 255
Cdd:cd02742  200 LKEDVIVQYWDYDGDKYNVELPEAAAK----GFPVILSNGYYLDIFIDGA------LDARKVYKNdpLAVPTPQQKDLVL 269


                 ....*..
gi 767997374 256 GIILTGW 262
Cdd:cd02742  270 GVIACLW 276
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 9-167 2.19e-05

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


Pssm-ID: 425840  Cd Length: 344  Bit Score: 46.91  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374    9 LKSEPLL--------EDVLEHHLPKFWSsPSEIKEILHLAGLNELEVIPLVQTFGHM--------EFVLKHTAFAHLR-- 70
Cdd:pfam00728  49 IKKYPKLtekgayrpSDLDGTPYGGFYT-QEDIREIVAYAAARGIRVIPEIDMPGHAraalaaypELGCGCGADSPWVsv 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374   71 EVGSFPCTLNPHEAESLALVGAMIDQVLELHPGaQRLHIGCDEVyylgegeASRRWLQ----QEQNSTGKLCLSH----- 141
Cdd:pfam00728 128 QWGPPEGQLNPGNEKTYTFLDNVFDEVADLFPS-DYIHIGGDEV-------PKGCWEKspecQARMKEEGLKSLHelqqy 199

                         170       180
                  ....*....|....*....|....*..
gi 767997374  142 -MRAVASGVKARRPsvTPLVWDDMLRD 167
Cdd:pfam00728 200 fIKRASKIVSSKGR--RLIGWDEILDG 224
GH20_DspB_LnbB-like cd06564
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ...
 31-126 6.59e-04

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: 41.89  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997374  31 SEIKEILHLAGLNELEVIPLVQTFGHMEFVLKhtAFAHLREVGSF----PCTLNPHEAESLALVGAMIDQVLEL-HPGAQ 105
Cdd:cd06564   82 EEFKELIAYAKDRGVNIIPEIDSPGHSLAFTK--AMPELGLKNPFskydKDTLDISNPEAVKFVKALFDEYLDGfNPKSD 159

                         90       100
                 ....*....|....*....|..
gi 767997374 106 RLHIGCDEVYYL-GEGEASRRW 126
Cdd:cd06564  160 TVHIGADEYAGDaGYAEAFRAY 181
 
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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