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Conserved domains on  [gi|253735681|ref|NP_001136034|]
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hexosaminidase D [Rattus norvegicus]

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, ...
 9-323 1.34e-129

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: 378.09  E-value: 1.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681   9 MRLVHLDLKG-APPKVSYLSEVFPLFHALGANGLLIEYEDMFPYEGHLRLLRAKHAYSPSEVTEILRLARLSGLEVVPLV 87
Cdd:cd06565    1 FRGVHLDLKRnAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  88 QTFGHMEFVLKHAAFAHLREVAPFPNTLNPHEAESLALVQAMIDQILELHRdVRWLHIGCDEVYYLGEGETSKQWlqqEQ 167
Cdd:cd06565   81 QTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 168 NSHAKLCLNHMQAVASHVLTQHPgiTPLVWDDMLRDIPQEQLKASGVPQLVEPVLWDYGADLDVHSKNFLIGKYQECGFQ 247
Cdd:cd06565  157 LGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFA 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253735681 248 RLWAASAFKGATgasqalPPVEHHIRNHELWLQVAGSgpvDTLQGIILTGWQRYDHFSVLCELLPVGIPSLAACLQ 323
Cdd:cd06565  235 VAWGASAWKGAT------PPNDKHLENIKSWLKAAKK---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, ...
 9-323 1.34e-129

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: 378.09  E-value: 1.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681   9 MRLVHLDLKG-APPKVSYLSEVFPLFHALGANGLLIEYEDMFPYEGHLRLLRAKHAYSPSEVTEILRLARLSGLEVVPLV 87
Cdd:cd06565    1 FRGVHLDLKRnAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  88 QTFGHMEFVLKHAAFAHLREVAPFPNTLNPHEAESLALVQAMIDQILELHRdVRWLHIGCDEVYYLGEGETSKQWlqqEQ 167
Cdd:cd06565   81 QTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 168 NSHAKLCLNHMQAVASHVLTQHPgiTPLVWDDMLRDIPQEQLKASGVPQLVEPVLWDYGADLDVHSKNFLIGKYQECGFQ 247
Cdd:cd06565  157 LGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFA 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253735681 248 RLWAASAFKGATgasqalPPVEHHIRNHELWLQVAGSgpvDTLQGIILTGWQRYDHFSVLCELLPVGIPSLAACLQ 323
Cdd:cd06565  235 VAWGASAWKGAT------PPNDKHLENIKSWLKAAKK---NGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 64-203 3.61e-10

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


Pssm-ID: 425840  Cd Length: 344  Bit Score: 61.16  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681   64 YSPSEVTEILRLARLSGLEVVPLVQTFGHM--------EFVLKHAAFAHLREVA--PFPNTLNPHEAESLALVQAMIDQI 133
Cdd:pfam00728  75 YTQEDIREIVAYAAARGIRVIPEIDMPGHAraalaaypELGCGCGADSPWVSVQwgPPEGQLNPGNEKTYTFLDNVFDEV 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253735681  134 LELHRDvRWLHIGCDEVyylgegeTSKQWLQQE--QNSHAKLCLNHMQAVAS------HVLTQHPGITPLVWDDMLRD 203
Cdd:pfam00728 155 ADLFPS-DYIHIGGDEV-------PKGCWEKSPecQARMKEEGLKSLHELQQyfikraSKIVSSKGRRLIGWDEILDG 224
Chb COG3525
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism];
64-201 1.19e-03

N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 442747 [Multi-domain]  Cd Length: 578  Bit Score: 41.38  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  64 YSPSEVTEILRLARLSGLEVVPLVQTFGHMEFVLkhAAFAHLR------EVAP----FPNTLNPHEAESLALVQAMIDQI 133
Cdd:COG3525  239 YTQEDIREIVAYAAARGITVIPEIDMPGHARAAI--AAYPELGctgkpySVRSvwgvFDNVLNPGKESTYTFLEDVLDEV 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 134 LELHRDvRWLHIGCDEVYYlgegetsKQWlqqEQNSH-----AKLCLNHMQAVASH-------VLTQHpGITPLVWDDML 201
Cdd:COG3525  317 AALFPS-PYIHIGGDEVPK-------GQW---EKSPAcqalmKELGLKDEHELQSYfirrvekILASK-GRKMIGWDEIL 384
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 9-323 1.34e-129

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: 378.09  E-value: 1.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681   9 MRLVHLDLKG-APPKVSYLSEVFPLFHALGANGLLIEYEDMFPYEGHLRLLRAKHAYSPSEVTEILRLARLSGLEVVPLV 87
Cdd:cd06565    1 FRGVHLDLKRnAVPKVSYLKKLLRLLALLGANGLLLYYEDTFPYEGEPEVGRMRGAYTKEEIREIDDYAAELGIEVIPLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  88 QTFGHMEFVLKHAAFAHLREVAPFPNTLNPHEAESLALVQAMIDQILELHRdVRWLHIGCDEVYYLGEGETSKQWlqqEQ 167
Cdd:cd06565   81 QTLGHLEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 168 NSHAKLCLNHMQAVASHVLTQHPgiTPLVWDDMLRDIPQEQLKASGVPQLVEPVLWDYGADLDVHSKNFLIGKYQECGFQ 247
Cdd:cd06565  157 LGRGELYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFA 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253735681 248 RLWAASAFKGATgasqalPPVEHHIRNHELWLQVAGSgpvDTLQGIILTGWQRYDHFSVLCELLPVGIPSLAACLQ 323
Cdd:cd06565  235 VAWGASAWKGAT------PPNDKHLENIKSWLKAAKK---NGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
GH20_hexosaminidase cd02742
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ...
 60-298 2.40e-12

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: 67.46  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  60 AKHAYSPSEVTEILRLARLSGLEVVPLVQTFGHM--------EFVLKHAAFAHLREVAPfpnTLNPHEAESLALVQAMID 131
Cdd:cd02742   65 PGGFYTYAQLKDIIEYAAARGIEVIPEIDMPGHStafvksfpKLLTECYAGLKLRDVFD---PLDPTLPKGYDFLDDLFG 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 132 QILELHrDVRWLHIGCDEVYYlgegetskqwlqqEQNSHAKLClNHMQAVASHVLTQhpGITPLVWDDMLrdIPQEQLKA 211
Cdd:cd02742  142 EIAELF-PDRYLHIGGDEAHF-------------KQDRKHLMS-QFIQRVLDIVKKK--GKKVIVWQDGF--DKKMKLKE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 212 SgvpqlVEPVLWDYGADLDVHSKNFLIGKyqecGFQRLWAASAFKGATGASQalPPVEHHIRNHElwLQVAGSGPVDTLQ 291
Cdd:cd02742  203 D-----VIVQYWDYDGDKYNVELPEAAAK----GFPVILSNGYYLDIFIDGA--LDARKVYKNDP--LAVPTPQQKDLVL 269


                 ....*..
gi 253735681 292 GIILTGW 298
Cdd:cd02742  270 GVIACLW 276
Glyco_hydro_20 pfam00728
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
 64-203 3.61e-10

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


Pssm-ID: 425840  Cd Length: 344  Bit Score: 61.16  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681   64 YSPSEVTEILRLARLSGLEVVPLVQTFGHM--------EFVLKHAAFAHLREVA--PFPNTLNPHEAESLALVQAMIDQI 133
Cdd:pfam00728  75 YTQEDIREIVAYAAARGIRVIPEIDMPGHAraalaaypELGCGCGADSPWVSVQwgPPEGQLNPGNEKTYTFLDNVFDEV 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253735681  134 LELHRDvRWLHIGCDEVyylgegeTSKQWLQQE--QNSHAKLCLNHMQAVAS------HVLTQHPGITPLVWDDMLRD 203
Cdd:pfam00728 155 ADLFPS-DYIHIGGDEV-------PKGCWEKSPecQARMKEEGLKSLHELQQyfikraSKIVSSKGRRLIGWDEILDG 224
GH20_DspB_LnbB-like cd06564
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ...
 7-201 3.27e-08

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: 55.37  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681   7 FKMRLVHLDLKGAPPKVSYlsevfplFHALGANGLLIEYEDMFPYEGHLRLLRAKHAYSPSEVTEILRLARLSGLEVVPL 86
Cdd:cd06564   29 YKMNDLQLHLNDNLIFNLD-------DMSTTVNNATYASDDVKSGNNYYNLTANDGYYTKEEFKELIAYAKDRGVNIIPE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  87 VQTFGHMEFVLKhaAFAHLREVAPF----PNTLNPHEAESLALVQAMIDQILELHRDV-RWLHIGCDEvyYLGEGETSKQ 161
Cdd:cd06564  102 IDSPGHSLAFTK--AMPELGLKNPFskydKDTLDISNPEAVKFVKALFDEYLDGFNPKsDTVHIGADE--YAGDAGYAEA 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 253735681 162 WLQqeqnsHAklclNHM-QAVASHvltqhpGITPLVWDDML 201
Cdd:cd06564  178 FRA-----YV----NDLaKYVKDK------GKTPRVWGDGI 203
GH20_HexA_HexB-like cd06562
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine ...
 25-201 7.00e-06

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.


Pssm-ID: 119332 [Multi-domain]  Cd Length: 348  Bit Score: 47.98  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  25 YLSEVFPLFHALGANGllieyedmfpyeghlrllrAKHAYSPSEVTEILRLARLSGLEVVPLVQTFGHM--------EFV 96
Cdd:cd06562   47 LESPSYPELSKKGAYS-------------------PSEVYTPEDVKEIVEYARLRGIRVIPEIDTPGHTgswgqgypELL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  97 LKHAAFAHLREVAPFPNTLNPHEAESLALVQAMIDQILELHRDvRWLHIGCDEVY---YLGEGETsKQWLQQEQNSHAKL 173
Cdd:cd06562  108 TGCYAVWRKYCPEPPCGQLNPTNPKTYDFLKTLFKEVSELFPD-KYFHLGGDEVNfncWNSNPEI-QKFMKKNNGTDYSD 185

                        170       180
                 ....*....|....*....|....*...
gi 253735681 174 CLNHMQAVAsHVLTQHPGITPLVWDDML 201
Cdd:cd06562  186 LESYFIQRA-LDIVRSLGKTPIVWEEVF 212
GH20_chitobiase-like_1 cd06570
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic ...
 27-162 4.83e-05

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: 45.09  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  27 SEVFPLFHALGANGLLieyedmfpyeghlrllrakhaYSPSEVTEILRLARLSGLEVVPLVQTFGHM--------EFVLK 98
Cdd:cd06570   49 SKKYPKLQQKASDGLY---------------------YTQEQIREVVAYARDRGIRVVPEIDVPGHAsaiavaypELASG 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 253735681  99 HAAFAHLREVAPFPNTLNPHEAESLALVQAMIDQILELHRDvRWLHIGCDEVyylgegeTSKQW 162
Cdd:cd06570  108 PGPYVIERGWGVFEPLLDPTNEETYTFLDNLFGEMAELFPD-EYFHIGGDEV-------DPKQW 163
GH20_chitobiase-like cd06563
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl ...
 50-201 2.61e-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: 42.95  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  50 PYEGHlrllrakhaYSPSEVTEILRLARLSGLEVVPLVQTFGHM--------EFVLKHAAFAHLREVAPFPNTLNPHEAE 121
Cdd:cd06563   78 PYGGF---------YTQEEIREIVAYAAERGITVIPEIDMPGHAlaalaaypELGCTGGPGSVVSVQGVVSNVLCPGKPE 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 122 SLALVQAMIDQILELHRDvRWLHIGCDEVYYlgegetsKQWLQQE--QNSHAKLCLNHMQAVASH-------VLTQHpGI 192
Cdd:cd06563  149 TYTFLEDVLDEVAELFPS-PYIHIGGDEVPK-------GQWEKSPacQARMKEEGLKDEHELQSYfikrvekILASK-GK 219


                 ....*....
gi 253735681 193 TPLVWDDML 201
Cdd:cd06563  220 KMIGWDEIL 228
Chb COG3525
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism];
64-201 1.19e-03

N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 442747 [Multi-domain]  Cd Length: 578  Bit Score: 41.38  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681  64 YSPSEVTEILRLARLSGLEVVPLVQTFGHMEFVLkhAAFAHLR------EVAP----FPNTLNPHEAESLALVQAMIDQI 133
Cdd:COG3525  239 YTQEDIREIVAYAAARGITVIPEIDMPGHARAAI--AAYPELGctgkpySVRSvwgvFDNVLNPGKESTYTFLEDVLDEV 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253735681 134 LELHRDvRWLHIGCDEVYYlgegetsKQWlqqEQNSH-----AKLCLNHMQAVASH-------VLTQHpGITPLVWDDML 201
Cdd:COG3525  317 AALFPS-PYIHIGGDEVPK-------GQW---EKSPAcqalmKELGLKDEHELQSYfirrvekILASK-GRKMIGWDEIL 384
 
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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