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Conserved domains on  [gi|2032866617|gb|QUT31674|]
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Beta-1,4-mannooligosaccharide phosphorylase [Bacteroides xylanisolvens]

Protein Classification

GH130 domain-containing protein( domain architecture ID 13035689)

GH130 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 20-328 4.06e-129

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


:

Pssm-ID: 350126 [Multi-domain]  Cd Length: 276  Bit Score: 370.21  E-value: 4.06e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  20 WESLVTCNPGVFYDNGMFYMLYRAAGNDreHVIRLGLATSRDGFYFERHSDRPAFSPSVDGPDSGCVEDPRIVKFDGEYY 99
Cdd:cd18614     1 WESKAVFNPAAIYEDGKVHLLYRAVGED--NISRLGYASSKDGIHFDERLDEPVYVPKKSGGENGGCEDPRITKIDDTYY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 100 ITYAYRPVPPgqywkfghdevllpecgkyaPAAIAknlgnTGLAVTTDFCHFRRLGRLT----SPVLDDRDVILFPEKVN 175
Cdd:cd18614    79 MTYTAYDGWP--------------------PPRVA-----LTSISTKDFLNFKWNWVIPplisPPGVDDKDAVLFPEKIN 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 176 GQFVMLHRpkqyigekfgvEYPSIWIKFSDDLLDWEG-KESHLLLTGRENTWEE-KIGGSTPPLKTDKGWLMLYHGVEHG 253
Cdd:cd18614   134 GKYALLHR-----------IGPDIWIDYSDDLDFGKNwIDSKIILEPRPGMWDSrKIGAGAPPIKTKKGWLLIYHGVDDD 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032866617 254 GKgYYRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIVDDTLFVYYGSADKYVCVATCSV 328
Cdd:cd18614   203 DR-VYRLGAALLDLEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKDDTLFVYYGGADKVIGVATAPL 276
 
Name Accession Description Interval E-value
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 20-328 4.06e-129

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350126 [Multi-domain]  Cd Length: 276  Bit Score: 370.21  E-value: 4.06e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  20 WESLVTCNPGVFYDNGMFYMLYRAAGNDreHVIRLGLATSRDGFYFERHSDRPAFSPSVDGPDSGCVEDPRIVKFDGEYY 99
Cdd:cd18614     1 WESKAVFNPAAIYEDGKVHLLYRAVGED--NISRLGYASSKDGIHFDERLDEPVYVPKKSGGENGGCEDPRITKIDDTYY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 100 ITYAYRPVPPgqywkfghdevllpecgkyaPAAIAknlgnTGLAVTTDFCHFRRLGRLT----SPVLDDRDVILFPEKVN 175
Cdd:cd18614    79 MTYTAYDGWP--------------------PPRVA-----LTSISTKDFLNFKWNWVIPplisPPGVDDKDAVLFPEKIN 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 176 GQFVMLHRpkqyigekfgvEYPSIWIKFSDDLLDWEG-KESHLLLTGRENTWEE-KIGGSTPPLKTDKGWLMLYHGVEHG 253
Cdd:cd18614   134 GKYALLHR-----------IGPDIWIDYSDDLDFGKNwIDSKIILEPRPGMWDSrKIGAGAPPIKTKKGWLLIYHGVDDD 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032866617 254 GKgYYRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIVDDTLFVYYGSADKYVCVATCSV 328
Cdd:cd18614   203 DR-VYRLGAALLDLEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKDDTLFVYYGGADKVIGVATAPL 276
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
1-336 3.70e-127

Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 366.00  E-value: 3.70e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617   1 MKLKKFEGNPILSPSEKNDWESLVTCNPGVFYDNGMFYMLYRAAGNDRehVIRLGLATSRDGFYFERhSDRPAFSPSVDG 80
Cdd:COG2152     2 GILKRYPGNPILTPNDMPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDG--KSHLGLARSDDGINFRR-DDEPILFPETDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  81 PDSGCvEDPRIVKFDGEYYITYAYrpvppgqywkfghdevllpecgkYAPAAIAknlgnTGLAVTTDFCHFRRLGRLTSP 160
Cdd:COG2152    79 EDTGV-EDPRITKIDGRYYITYTA-----------------------YSGAGAR-----IGLARTKDFKTWERLGLIFPP 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 161 vlDDRDVILFPEKVNGQFVMLHRPKQyigeKFGVEYPSIWIKFSDDLLDWEgkESHLLLTGRENTWEE-KIGGSTPPLKT 239
Cdd:COG2152   130 --DNKDAVLFPEKINGKYALLHRPSD----GFHTGGPDIWISYSPDLEHWG--DHRIVMGPRPGTWDSlKIGAGPPPIKT 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 240 DKGWLMLYHGVEHGGKGY-YRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIV-DDTLFVYYGSA 317
Cdd:COG2152   202 EEGWLLIYHGVRNTAAGLvYRLGAALLDLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVDeDGTVYIYYGAA 281

                         330
                  ....*....|....*....
gi 2032866617 318 DKYVCVATCSVNELLSYLL 336
Cdd:COG2152   282 DTRIALATATLDELLDYLK 300
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 2-335 1.16e-49

beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the CAZy GH130 family. Several have been characterized as mannosylglucose phosphorylase. This enzyme is part of the mannan catalytic pathway and feeds into the glycolysis cycle. Specifically it catalyzes the reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine. This family was noted to belong to the Beta fructosidase superfamily in.


Pssm-ID: 397932 [Multi-domain]  Cd Length: 315  Bit Score: 168.43  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617   2 KLKKFEGNPIL---SPSEKNDWE-------SLVTCNPGV-FYDNGM-----FYMLYRAAGNDREHvIRLGLATSRDGFYF 65
Cdd:pfam04041   1 SLRKIPTIDILerpSYITGKDSRitnpvrnPVAVFNPAVvLYEKELhvyprVVMGYYKYVSDIAS-FRIGLEDSYDGIKK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  66 ERHSDrPAFSPSVDGPDSGCvEDPRIVKFDGEYYITYAYRPvppGQYWKfghdevllpecgkyapaaiaknlgnTGLAVT 145
Cdd:pfam04041  80 TLEPE-PIFWPRDKQEFWGV-EDPRVVKINSTYYMTYTGRD---YKYWR-------------------------IEVGTT 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 146 TDFCHFRRLGRLTSPV------LDDRDVILFPEKVNGQFVMLHRPkqyigekfgveyPSIWIKFSDDLLDWEGKESHLLL 219
Cdd:pfam04041 130 KDFLTWARLPVKIALFekrydsIKTSDGNAFPVKIKGKYLMYHRV------------GDIWLAVSPDLVHWENRLEPLGS 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 220 TGR---ENTWEEKIGGSTPPLKTDKGWLMLYHGVehGGKGY-YRVGALLLDLDNplKILAKTHESILEPEEDFEINGYYN 295
Cdd:pfam04041 198 PRPimfPNPFETKIGWGTPPVETKEGWLVLIHGV--DTEDLvYRVGAALLDLEG--KVLARTPEYILEPEEEYEEYGDRP 273

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2032866617 296 GCVFPTGNVIVDDTLFVYYGSADKYVCVATCSVNELLSYL 335
Cdd:pfam04041 274 NVVFPCGALVDGERVIIYYGAADTAIGLAEIPEEEIMNLL 313
 
Name Accession Description Interval E-value
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 20-328 4.06e-129

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350126 [Multi-domain]  Cd Length: 276  Bit Score: 370.21  E-value: 4.06e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  20 WESLVTCNPGVFYDNGMFYMLYRAAGNDreHVIRLGLATSRDGFYFERHSDRPAFSPSVDGPDSGCVEDPRIVKFDGEYY 99
Cdd:cd18614     1 WESKAVFNPAAIYEDGKVHLLYRAVGED--NISRLGYASSKDGIHFDERLDEPVYVPKKSGGENGGCEDPRITKIDDTYY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 100 ITYAYRPVPPgqywkfghdevllpecgkyaPAAIAknlgnTGLAVTTDFCHFRRLGRLT----SPVLDDRDVILFPEKVN 175
Cdd:cd18614    79 MTYTAYDGWP--------------------PPRVA-----LTSISTKDFLNFKWNWVIPplisPPGVDDKDAVLFPEKIN 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 176 GQFVMLHRpkqyigekfgvEYPSIWIKFSDDLLDWEG-KESHLLLTGRENTWEE-KIGGSTPPLKTDKGWLMLYHGVEHG 253
Cdd:cd18614   134 GKYALLHR-----------IGPDIWIDYSDDLDFGKNwIDSKIILEPRPGMWDSrKIGAGAPPIKTKKGWLLIYHGVDDD 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032866617 254 GKgYYRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIVDDTLFVYYGSADKYVCVATCSV 328
Cdd:cd18614   203 DR-VYRLGAALLDLEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKDDTLFVYYGGADKVIGVATAPL 276
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
1-336 3.70e-127

Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 366.00  E-value: 3.70e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617   1 MKLKKFEGNPILSPSEKNDWESLVTCNPGVFYDNGMFYMLYRAAGNDRehVIRLGLATSRDGFYFERhSDRPAFSPSVDG 80
Cdd:COG2152     2 GILKRYPGNPILTPNDMPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDG--KSHLGLARSDDGINFRR-DDEPILFPETDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  81 PDSGCvEDPRIVKFDGEYYITYAYrpvppgqywkfghdevllpecgkYAPAAIAknlgnTGLAVTTDFCHFRRLGRLTSP 160
Cdd:COG2152    79 EDTGV-EDPRITKIDGRYYITYTA-----------------------YSGAGAR-----IGLARTKDFKTWERLGLIFPP 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 161 vlDDRDVILFPEKVNGQFVMLHRPKQyigeKFGVEYPSIWIKFSDDLLDWEgkESHLLLTGRENTWEE-KIGGSTPPLKT 239
Cdd:COG2152   130 --DNKDAVLFPEKINGKYALLHRPSD----GFHTGGPDIWISYSPDLEHWG--DHRIVMGPRPGTWDSlKIGAGPPPIKT 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 240 DKGWLMLYHGVEHGGKGY-YRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIV-DDTLFVYYGSA 317
Cdd:COG2152   202 EEGWLLIYHGVRNTAAGLvYRLGAALLDLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVDeDGTVYIYYGAA 281

                         330
                  ....*....|....*....
gi 2032866617 318 DKYVCVATCSVNELLSYLL 336
Cdd:COG2152   282 DTRIALATATLDELLDYLK 300
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 27-332 1.73e-87

Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions.


Pssm-ID: 350107 [Multi-domain]  Cd Length: 279  Bit Score: 264.33  E-value: 1.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  27 NPGVFYDNGMFYMLYRAAGNDREHviRLGLATSRDGFYFERHSDRPAFSPSVDGPD-SGCVEDPRIVKFDGEYYITYAYr 105
Cdd:cd08993     8 NAGAVKFNGKYLLLFRVEDLNGRS--FLGLAESDDGIHFTVEPEPILTPDEPFEPYeETGVYDPRITKIDDTYYITFAA- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 106 pvppgqywkFGHDEVLLpecgkyapaaiaknlgntGLAVTTDFCHFRRLGRLTSPvlDDRDVILFPEKVNGQFVMLHRPK 185
Cdd:cd08993    85 ---------DSDHGPRI------------------GLARTKDFKTFERLELISEP--DNRNGVLFPEKINGKYARLDRPS 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 186 QYIGEKFGveypSIWIKFSDDLLDWEgkESHLLLTGRENTW-EEKIGGSTPPLKTDKGWLMLYHGVE-HGGKGYYRVGAL 263
Cdd:cd08993   136 DGGHTSGG----DIWISYSPDLIHWG--NSRLVMGPRPGPWdNDKIGPGAPPIKTEEGWLLIYHGVRtTCSGFVYRLGAA 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032866617 264 LLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGnVIVDD--TLFVYYGSADKYVCVATCSVNELL 332
Cdd:cd08993   210 LLDLEDPSKVIARSREPILAPEEPYERVGDVPNVVFPCG-AIVEEdgEVKIYYGAADTVICLATATIDDLV 279
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 20-327 9.99e-87

Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; This subfamily contains the glycosyl hydrolase family 130 (GH130), as classified by the carbohydrate-active enzymes database (CAZY), enzymes that are phosphorylases and hydrolases for beta-mannosides, and includes Listeria innocua beta-1,2-mannobiose phosphorylase (Lin0857). hey possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Structure of Lin0857 shows beta-1,2-mannotriose bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, with a significant open-close loop displacement observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size.


Pssm-ID: 350124 [Multi-domain]  Cd Length: 261  Bit Score: 261.68  E-value: 9.99e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  20 WESLVTCNPGVFYDNGMFYMLYRAAgndrEHvirLGLATSRDGFYFERhSDRPAFSPSVDGPDSGcVEDPRIVKFDGEYY 99
Cdd:cd18612     1 LEVIGVFNPGAARYGDEIILLLRVA----EH---LRLARSRDGIHFTV-DEKPALFPEGPYEAFG-IEDPRITRIDDTYY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 100 ITYAyrpvppgqywkfghdevllpecgkyapaAIAKNLGNTGLAVTTDFCHFRRLGRLTSPvlDDRDVILFPEKVNGQFV 179
Cdd:cd18612    72 ITYT----------------------------AVSEYGIATALASTKDFKTFERHGVIFPP--ENKDVVIFPEKINGKYY 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 180 MLHRPkqyIGEKFGVeyPSIWIKFSDDLLDWeGKESHLLLTgRENTWEE-KIGGSTPPLKTDKGWLMLYHGVEHGGKgyY 258
Cdd:cd18612   122 ALHRP---VPSGFGK--PEIWIAESPDLLHW-GNHRHLAGP-RPGMWDSgRIGAGAVPIKTEKGWLEIYHGADENNR--Y 192

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032866617 259 RVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIVDDTLFVYYGSADKYVCVATCS 327
Cdd:cd18612   193 CLGALLLDLEDPSKVIARSEEPILEPEAPYEKEGFFGNVVFTCGAVVEGDTLLIYYGAADTSIAVAEFS 261
GH130 cd18607
Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by ...
 20-326 1.27e-86

Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350119 [Multi-domain]  Cd Length: 269  Bit Score: 261.87  E-value: 1.27e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  20 WESLVTCNPGVFYDNGMFYMLYRAAGNDREHViRLGLATSRDGFYFERHSDRPAFSPSVDGPDSGCVEDPRIVKFDGEYY 99
Cdd:cd18607     1 WESAAVFNPGAILHDGKYHLLYRAVGKGTRRS-SIGYARSKDGIHFERLDEPPLYPPPENPYEKGGCEDPRITKIDDTYY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 100 ITY-AYRPVPPGqywkfghdevllpecgkyapaaiaknlgnTGLAVTTDFCHFRRLGRLTSPVLDDRDVILFPEKVNGQF 178
Cdd:cd18607    80 MTYtAYDGFGPR-----------------------------LALATTKDLKNWERHGLAFPPAPENKNGVIFPEKINGKY 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 179 VMLHRPkqyigekfgvEYPSIWIKFSDDLLDWeGKESHLLLTGRENTWEEKIGGSTPPLKTDKGWLMLYHGVEHGGKGY- 257
Cdd:cd18607   131 AMLHRP----------DGPDIWLATSDDLIHW-GDHKPLLKPRKGTWDSAKVGAGPPPIKTKKGWLLLYHGVNETAAGNr 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 258 YRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIVD-DTLFVYYGSADKYVCVATC 326
Cdd:cd18607   200 YRLGAALLDLNDPTRVLYRSDKPILEPEEDYEKSGYVPNVVFPCGAVAIDgDELKLYYGAADTKVAVATV 269
GH130 cd18615
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 27-325 1.15e-68

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350127 [Multi-domain]  Cd Length: 277  Bit Score: 216.32  E-value: 1.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  27 NPGVFYDNGMFYMLYRAagNDREHVIRLGLATSRDGFYFERHSDRPAFSPSVDGPDSGC--VEDPRIVKFD--GEYYITY 102
Cdd:cd18615    10 NPGAAKLGGETLLLVRV--EDRRGFSHLTVARSADGVTNWKIDPKPTLEPDPEDYPEEMwgIEDPRITWLEelGRYAITY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 103 -AYRPVPPGqywkfghdevllpecgkyapaaiaknlgnTGLAVTTDFCHFRRLGRLTSPvlDDRDVILFPEKVNGQFVML 181
Cdd:cd18615    88 tAYSPAGPG-----------------------------VSLATTKDFKTFERLGLVMPP--EDKDAALFPRRINGRWALL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 182 HRPKQYIGEkfgveypSIWIKFSDDLLDWEgkESHLLLTGRENTW--EEKIGGSTPPLKTDKGWLMLYHGV-EHGGKGYY 258
Cdd:cd18615   137 HRPVSAGRA-------HIWISFSPDLKHWG--DHRPVLPARRGPWwdAVKVGLGPPPIETPEGWLIIYHGVkETASGSIY 207

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032866617 259 RVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIV--DDTLFVYYGSADKYVCVAT 325
Cdd:cd18615   208 RVGLALLDLEDPTKVIRRSDEWVLGPEEPYERIGDVPNVVFPCGAILDedGDELRLYYGAADTCIALAT 276
GH130 cd18611
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 20-326 2.56e-63

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350123 [Multi-domain]  Cd Length: 289  Bit Score: 202.75  E-value: 2.56e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  20 WESLVTCNPGVFYDNGMFYMLYRAAGNDREHV---IRL---GLATSRDGFYFERHsdRPAFSPSVDGPDSGCvEDPRIVK 93
Cdd:cd18611     1 WEAEAVFNGSVIKDGGKYHLLYRALSSPQEIDgpkLGLstiGYAESKDGVHFENR--RQLIKPEEEWEKYGC-EDPRVTK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  94 FDGEYYITY-AYRPVPPGqywkfghdevllpecgkyaPAAIaknlgNTGLAVTTDFCHFrrlgrltspvlDDRDVI---- 168
Cdd:cd18611    78 IDGKYYIFYtALSGYPFG-------------------PEGI-----KVAVAITKDFKTI-----------EEKHLVtpfn 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 169 -----LFPEKVNGQFVML---H--RPKQYIG--------EKFGVEYpsiWIKFSDDLldwegkESHLLLTGRENTWEEKI 230
Cdd:cd18611   123 akamaLFPEKINGKYAALltvNtdNPPAKIAlayfdkieDLWSPEY---WDKWYANL------DDHALPLRRSEHDHVEV 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 231 GGstPPLKTDKGWLMLYHGVEH--GGKGYYRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCVFPTGNVIVDD 308
Cdd:cd18611   194 GA--PPIKTKDGWLLIYSYIQNyfSGERVFGIEAALLDLNDPRKIIGRTKGPLLVPEEEYELYGLVPNIVFPSGALIEGD 271

                         330
                  ....*....|....*...
gi 2032866617 309 TLFVYYGSADKYVCVATC 326
Cdd:cd18611   272 KLHIYYGAADTVCCLASV 289
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
 10-326 1.01e-58

Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This subfamily contains glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), and includes Bacteroides enzymes, BT3780 and BACOVA_03624. Members of this family possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. GH130 enzymes have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages where these phosphorylases mediate bond cleavage by a single displacement reaction in which phosphate functions as the catalytic nucleophile. However, some lack the conserved basic residues that bind the phosphate nucleophile, as observed for the Bacteroides enzymes, BT3780 and BACOVA_03624, which are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism.


Pssm-ID: 350122 [Multi-domain]  Cd Length: 301  Bit Score: 191.26  E-value: 1.01e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  10 PILSPSEKNdWESLVTCNPGVFYDNGMFYMLYRAAGND--REHVIRLGLATSRDGFYFERHSDrPAFSPSVDGPDSGCVE 87
Cdd:cd18610     1 CPLRPKEVA-WESKDVFNPAAIVRDGKVYLLYRAEDASgnGNGTSRIGLAVSDDGLHFTRLPE-PVLYPEEDYEWPGGCE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  88 DPRIVKF-DGEYYITY-AYrpvppgqywkfGHDEVLLpeCgkyapaaiaknlgntgLAVTTDFCHFRRLGrltsPVLDDR 165
Cdd:cd18610    79 DPRIVEIeDGTYYMTYtAY-----------DGKTARL--C----------------LATSTDLVHWTKHG----PAFPDA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 166 DVILFPE----------------KVNGQFVMlhrpkqYIGEKFgveypsIWIKFSDDLLDWEGKESHL----LLTGRENT 225
Cdd:cd18610   126 DGGKYRDlwsksgaivpelkgaaKINGKYWM------YWGESN------IYLATSDDLIHWTPVEDDGslrpVLSPRPGK 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 226 WEEK-IGGSTPPLKTDKGWLMLYHGVEHGG------KGYYRVGALLLDLDNPLKILAKTHESILEPEEDFEINGYYNGCV 298
Cdd:cd18610   194 FDSDlVEPGPPPILTDGGILLIYNGANDGGggpgypKGTYSAGQALFDANDPTKLLARLDKPFLEPETPYEKEGQVNNVV 273

                         330       340
                  ....*....|....*....|....*...
gi 2032866617 299 FPTGNVIVDDTLFVYYGSADKYVCVATC 326
Cdd:cd18610   274 FVEGLVYFKGKWLLYYGTADSKIGVATA 301
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 2-335 1.16e-49

beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the CAZy GH130 family. Several have been characterized as mannosylglucose phosphorylase. This enzyme is part of the mannan catalytic pathway and feeds into the glycolysis cycle. Specifically it catalyzes the reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine. This family was noted to belong to the Beta fructosidase superfamily in.


Pssm-ID: 397932 [Multi-domain]  Cd Length: 315  Bit Score: 168.43  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617   2 KLKKFEGNPIL---SPSEKNDWE-------SLVTCNPGV-FYDNGM-----FYMLYRAAGNDREHvIRLGLATSRDGFYF 65
Cdd:pfam04041   1 SLRKIPTIDILerpSYITGKDSRitnpvrnPVAVFNPAVvLYEKELhvyprVVMGYYKYVSDIAS-FRIGLEDSYDGIKK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  66 ERHSDrPAFSPSVDGPDSGCvEDPRIVKFDGEYYITYAYRPvppGQYWKfghdevllpecgkyapaaiaknlgnTGLAVT 145
Cdd:pfam04041  80 TLEPE-PIFWPRDKQEFWGV-EDPRVVKINSTYYMTYTGRD---YKYWR-------------------------IEVGTT 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 146 TDFCHFRRLGRLTSPV------LDDRDVILFPEKVNGQFVMLHRPkqyigekfgveyPSIWIKFSDDLLDWEGKESHLLL 219
Cdd:pfam04041 130 KDFLTWARLPVKIALFekrydsIKTSDGNAFPVKIKGKYLMYHRV------------GDIWLAVSPDLVHWENRLEPLGS 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 220 TGR---ENTWEEKIGGSTPPLKTDKGWLMLYHGVehGGKGY-YRVGALLLDLDNplKILAKTHESILEPEEDFEINGYYN 295
Cdd:pfam04041 198 PRPimfPNPFETKIGWGTPPVETKEGWLVLIHGV--DTEDLvYRVGAALLDLEG--KVLARTPEYILEPEEEYEEYGDRP 273

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2032866617 296 GCVFPTGNVIVDDTLFVYYGSADKYVCVATCSVNELLSYL 335
Cdd:pfam04041 274 NVVFPCGALVDGERVIIYYGAADTAIGLAEIPEEEIMNLL 313
GH130 cd18613
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 47-332 1.66e-41

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350125  Cd Length: 302  Bit Score: 146.49  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  47 DREHVIRLGLATSRDGFYFERHSDRPA-----FsPSVDGpDSGCVEDPRIVKF---DG--EYYITY-AYRpvppgqywkf 115
Cdd:cd18613    53 DPGGEIRLIRWLADSNYELRFPADVDLservlF-PVTPA-ESNGIEDARFVRFtddDGsvTYYATYtAYD---------- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 116 GHDevLLPEcgkyapaaiaknlgntgLAVTTDFCHFRrLGRLTSPVLDDRDVILFPEKVNGQFVMLHRPKqyiGEkfgve 195
Cdd:cd18613   121 GRA--IRPQ-----------------LLETRDFRTFK-VRPLTGPAARNKGMALFPRKIGGRYAMLSRQD---GE----- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 196 ypSIWIKFSDDLLDWEgkESHLLLTGREnTWE-EKIGGSTPPLKTDKGWLMLYHGVehGGKGYYRVGALLLDLDNPLKIL 274
Cdd:cd18613   173 --NIYLMFSDDLYFWD--EAELILKPRY-PWEfVQIGNCGSPIETDEGWLVLTHGV--GPMRRYSIGAILLDLDDPTKVI 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032866617 275 AKTHESILEPEEDfEINGYYNGCVFPTGNVIVDDTLFVYYGSADKYVCVATCSVNELL 332
Cdd:cd18613   246 GRLREPLLSPDEE-EREGYVPNVVYSCGALVHGDRLILPYGMSDSATGFATVDLDELL 302
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 27-274 8.35e-12

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350091 [Multi-domain]  Cd Length: 257  Bit Score: 64.54  E-value: 8.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  27 NPGVFYDNGMFYMLYRaaGNDREHVIRLGLATSRDGFYFERhsDRPAFSPSVDGP-DSGCVEDPRIVKFDGEYYITYAyr 105
Cdd:cd08772     2 DPSVVPYNGEYHLFFT--IGPKNTRPFLGHARSKDLIHWEE--EPPAIVARGGGSyDTSYAFDPEVVYIEGTYYLTYC-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 106 pvppgqywkfghdevllpecgKYAPAAIAKNLGNTGLAVTTDFCHFRRLGRLTSPVLDD------RDVILFPEKVNGqFV 179
Cdd:cd08772    76 ---------------------SDDLGDILRHGQHIGVAYSKDPKGPWTRKDAPLIEPPNayspknRDPVLFPRKIGK-YY 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617 180 MLHRPKQYIGEKFGVeypsIWIKFSDDLLDWegkeshllLTGRENTWEEKIGGSTP---PLKTDKGWLMLYHGVEHGGKG 256
Cdd:cd08772   134 LLNVPSDNGHTRFGK----IAIAESPD*LHW--------INHSFVYNYNEQGKVGEgpsLWKTKGGWYLIYHANTLTGYG 201

                         250
                  ....*....|....*...
gi 2032866617 257 yYRVGALLLDLDNPLKIL 274
Cdd:cd08772   202 -YGFGYALGDLDDPSKVL 218
GH43_62_32_68_117_130-like cd08994
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 5-99 1.68e-08

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350108 [Multi-domain]  Cd Length: 294  Bit Score: 54.96  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617   5 KFEGNPILSPSEkNDWESLVTCNPGVFY-DNGMFYMLYRAAGNDREHVIRLGLATSRDGF-YFERHSDRPAFSPSVDGPd 82
Cdd:cd08994   131 KRFDKPILDPRP-RSWDDLITSNPAVLKrPDGSYLLYYKGGKKNPGGNRKHGVAVSDSPEgPYTKLSDPPVYEPGVNGQ- 208

                          90
                  ....*....|....*..
gi 2032866617  83 sgcVEDPRIVKFDGEYY 99
Cdd:cd08994   209 ---TEDPFIWYDKGQYH 222
GH117 cd08992
Glycosyl hydrolase family 117 (GH117); This glycoside hydrolase 117 (GH117) family includes ...
 19-113 1.37e-06

Glycosyl hydrolase family 117 (GH117); This glycoside hydrolase 117 (GH117) family includes alpha-1,3-L-neoagarooligosaccharide hydrolase (EC 3.2.1.-); alpha-1,3-L-neoagarobiase/neoagarobiose hydrolase (NABH, EC 3.2.1.-). In the agarolytic pathway, in order to metabolize agar, NABH is an essential enzyme because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose). Thus, these enzymes have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate. This family includes Zobellia galactanivorans enzymes, Zg4663 and Zg3615 (also known as ZgAhgA and ZgAhgB, respectively) that have been shown to have similar activity on unsubstituted agarose oligosaccharides while Zg3597 has been shown to be inactive, possibly due to differences in dimerization conformation, active-site structure and function. GH117 shares distant sequence similarity with families GH43 and GH32. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350106  Cd Length: 314  Bit Score: 49.17  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  19 DWESLvtCNPGVFYDNGMFYMLYRAA----GNDREH-VIRLGLATSRDGFYfeRHSDRPAFSPSVDGP--------DSGC 85
Cdd:cd08992    94 DDRSV--FTPEILVHKGKYYLYYQAVkspyGGIRDKnPIGMAVADSPDGPW--TKLDEPILEPGDEGEwekakgdfDSHK 169

                          90       100
                  ....*....|....*....|....*...
gi 2032866617  86 VEDPRIVKFDGEYYITYAYRPVPPGQYW 113
Cdd:cd08992   170 VHDPCLIVYNGKFYLYYKGEPMGEGITG 197
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
 28-113 1.20e-04

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 43.08  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  28 PGVFYDNGMFYMLYRAAGNDREHVIRLGLATSRDGFYFERHSDRPAFSPSVDGPDSGC-----VEDPrivkfDGEYYITY 102
Cdd:pfam04616 178 PHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSRSPENPIYGPghaslVETP-----DGEWWIVY 252

                          90
                  ....*....|..
gi 2032866617 103 -AYRPVPPGQYW 113
Cdd:pfam04616 253 hAGRPGDGGYGL 264
GH43_62_32_68_117_130-like cd08994
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 4-104 5.20e-04

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350108 [Multi-domain]  Cd Length: 294  Bit Score: 41.09  E-value: 5.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617   4 KKFEGNPILSPSEKNDWEslvtcNPGVFYDNGMFYMLYRAAGNDREHVIR-LGLATSRDGFYFERHsDRPAFSPSV---D 79
Cdd:cd08994   193 TKLSDPPVYEPGVNGQTE-----DPFIWYDKGQYHLIVKDMGGIFTGEGGgGALLRSKDGINWKLA-PGLAYSTEVkwtD 266

                          90       100
                  ....*....|....*....|....*...
gi 2032866617  80 G--PDSGCVEDPRIVKF-DGEyyITYAY 104
Cdd:cd08994   267 GttEKWGRLERPQLLQDeDGK--PTYLF 292
GH32-like cd18609
Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase ...
 28-123 1.01e-03

Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350121  Cd Length: 303  Bit Score: 40.31  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  28 PGVFYDN--GMFYMLY--RAAGNDREH--VIrlGLATSRDGFYFERHsdRPAFSPSVdgpdSGCVEDPRIVKFDGEYYIT 101
Cdd:cd18609   149 PWVFRDPdgGGWHMLItaRANEGPPDGrgVI--GHATSPDLEHWEVL--PPLSAPGV----FGHLEVPQVFEIDGRWYLL 220

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2032866617 102 Y----------AYRPVPPGQYWKFGHDEVLLP 123
Cdd:cd18609   221 FscgadhlsreRRAAGGGGGTWYVPADSPLGP 252
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
 28-103 5.74e-03

Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350105 [Multi-domain]  Cd Length: 283  Bit Score: 37.92  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032866617  28 PGVFYDNGMFYMLYRAagNDREHVIRLGLATsrdgfyferhSDRPA--FSPSVDGPDSGCVE--DPRIVK-FDGEYYITY 102
Cdd:cd08991    57 PEVFYYNGKFYMYYSA--NGGDHGEHIAVAV----------SDSPLgpFRDKGKLLIPAGGFsiDAHVFIdDDGKWYLYY 124


                  .
gi 2032866617 103 A 103
Cdd:cd08991   125 V 125
 
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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