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Conserved domains on  [gi|578832008|ref|XP_006722343|]
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hexosaminidase D isoform X3 [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, ...
 1-276 1.55e-114

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: 341.49  E-value: 1.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   1 MFPYEGPLRLLRAKYAYSPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVG 80
Cdd:cd06565   41 TFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  81 AMIDQVLELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGKLCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPED 160
Cdd:cd06565  121 EMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008 161 QLAASGVPQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAASAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPT 240
Cdd:cd06565  195 PEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGAT------PPNDKHLENIKSWLKAA---KK 265

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 578832008 241 DSLQGIILTGWQRYDHYSVLCELLPAGVPSLAACLQ 276
Cdd:cd06565  266 NGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 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, ...
 1-276 1.55e-114

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: 341.49  E-value: 1.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   1 MFPYEGPLRLLRAKYAYSPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVG 80
Cdd:cd06565   41 TFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  81 AMIDQVLELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGKLCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPED 160
Cdd:cd06565  121 EMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008 161 QLAASGVPQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAASAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPT 240
Cdd:cd06565  195 PEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGAT------PPNDKHLENIKSWLKAA---KK 265

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 578832008 241 DSLQGIILTGWQRYDHYSVLCELLPAGVPSLAACLQ 276
Cdd:cd06565  266 NGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 17-156 1.56e-06

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


Pssm-ID: 425840  Cd Length: 344  Bit Score: 50.38  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   17 YSPSEIKEILHLAGLNELEVIPLVQTFGHM--------EFVLKHTAFAHLR--EVGSFPCTLNPHEAESLALVGAMIDQV 86
Cdd:pfam00728  75 YTQEDIREIVAYAAARGIRVIPEIDMPGHAraalaaypELGCGCGADSPWVsvQWGPPEGQLNPGNEKTYTFLDNVFDEV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   87 LELHPGaQRLHIGCDEVyylgegeASRRWLQ----QEQNSTGKLCLSH------MRAVASGVKARRPsvTPLVWDDMLRD 156
Cdd:pfam00728 155 ADLFPS-DYIHIGGDEV-------PKGCWEKspecQARMKEEGLKSLHelqqyfIKRASKIVSSKGR--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, ...
 1-276 1.55e-114

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: 341.49  E-value: 1.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   1 MFPYEGPLRLLRAKYAYSPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVG 80
Cdd:cd06565   41 TFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  81 AMIDQVLELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGKLCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPED 160
Cdd:cd06565  121 EMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008 161 QLAASGVPQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAASAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPT 240
Cdd:cd06565  195 PEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGASAWKGAT------PPNDKHLENIKSWLKAA---KK 265

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 578832008 241 DSLQGIILTGWQRYDHYSVLCELLPAGVPSLAACLQ 276
Cdd:cd06565  266 NGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
GH20_hexosaminidase cd02742
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ...
 17-251 2.21e-09

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: 58.98  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  17 YSPSEIKEILHLAGLNELEVIPLVQTFGHMefvlkhTAFAHLREVGSFPCT-----------LNPHEAESLALVGAMIDQ 85
Cdd:cd02742   69 YTYAQLKDIIEYAAARGIEVIPEIDMPGHS------TAFVKSFPKLLTECYaglklrdvfdpLDPTLPKGYDFLDDLFGE 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  86 VLELHPGaQRLHIGCDEVYYLGEGEASrrwlqqeqNSTgklclsHMRAVASGVKARrpSVTPLVWDDMLRDLPEdqlaas 165
Cdd:cd02742  143 IAELFPD-RYLHIGGDEAHFKQDRKHL--------MSQ------FIQRVLDIVKKK--GKKVIVWQDGFDKKMK------ 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008 166 gVPQLVEPVLWDYTADLDVHGKVLLMQKyrrcGFPQLWAASAFKGATGPSQavppveHHLRNHVQW--LQVAGSGPTDSL 243
Cdd:cd02742  200 -LKEDVIVQYWDYDGDKYNVELPEAAAK----GFPVILSNGYYLDIFIDGA------LDARKVYKNdpLAVPTPQQKDLV 268


                 ....*...
gi 578832008 244 QGIILTGW 251
Cdd:cd02742  269 LGVIACLW 276
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 17-156 1.56e-06

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


Pssm-ID: 425840  Cd Length: 344  Bit Score: 50.38  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   17 YSPSEIKEILHLAGLNELEVIPLVQTFGHM--------EFVLKHTAFAHLR--EVGSFPCTLNPHEAESLALVGAMIDQV 86
Cdd:pfam00728  75 YTQEDIREIVAYAAARGIRVIPEIDMPGHAraalaaypELGCGCGADSPWVsvQWGPPEGQLNPGNEKTYTFLDNVFDEV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008   87 LELHPGaQRLHIGCDEVyylgegeASRRWLQ----QEQNSTGKLCLSH------MRAVASGVKARRPsvTPLVWDDMLRD 156
Cdd:pfam00728 155 ADLFPS-DYIHIGGDEV-------PKGCWEKspecQARMKEEGLKSLHelqqyfIKRASKIVSSKGR--RLIGWDEILDG 224
GH20_DspB_LnbB-like cd06564
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ...
 12-115 5.56e-05

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: 45.36  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  12 RAKYAYSPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLKhtAFAHLREVGSF----PCTLNPHEAESLALVGAMIDQVL 87
Cdd:cd06564   74 ANDGYYTKEEFKELIAYAKDRGVNIIPEIDSPGHSLAFTK--AMPELGLKNPFskydKDTLDISNPEAVKFVKALFDEYL 151

                         90       100       110
                 ....*....|....*....|....*....|
gi 578832008  88 EL-HPGAQRLHIGCDEVYYL-GEGEASRRW 115
Cdd:cd06564  152 DGfNPKSDTVHIGADEYAGDaGYAEAFRAY 181
GH20_chitobiase-like cd06563
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl ...
 17-160 1.50e-03

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: 41.02  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  17 YSPSEIKEILHLAGLNELEVIPLVQTFGHM--------EFVLKHTAFaHLREVGSFPC-TLNPHEAESLALVGAMIDQVL 87
Cdd:cd06563   83 YTQEEIREIVAYAAERGITVIPEIDMPGHAlaalaaypELGCTGGPG-SVVSVQGVVSnVLCPGKPETYTFLEDVLDEVA 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578832008  88 ELHPGaQRLHIGCDEVYYlGEGEAS---RRWLQQEQNSTGKLCLSH-MRAVASGVKARRpsVTPLVWDDMLR-DLPED 160
Cdd:cd06563  162 ELFPS-PYIHIGGDEVPK-GQWEKSpacQARMKEEGLKDEHELQSYfIKRVEKILASKG--KKMIGWDEILEgGLPPN 235
GH20_chitobiase-like_1 cd06570
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic ...
 17-103 7.88e-03

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.


Pssm-ID: 119338  Cd Length: 311  Bit Score: 38.55  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832008  17 YSPSEIKEILHLAGLNELEVIPLVQTFGHMEFVLkhTAFAHL----------REVGSFPCTLNPHEAESLALVGAMIDQV 86
Cdd:cd06570   65 YTQEQIREVVAYARDRGIRVVPEIDVPGHASAIA--VAYPELasgpgpyvieRGWGVFEPLLDPTNEETYTFLDNLFGEM 142

                         90
                 ....*....|....*..
gi 578832008  87 LELHPGAQrLHIGCDEV 103
Cdd:cd06570  143 AELFPDEY-FHIGGDEV 158
 
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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