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Conserved domains on  [gi|500165186|ref|WP_011839802|]
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glycosidase [Staphylothermus marinus]

Protein Classification

glycoside hydrolase family protein( domain architecture ID 52385)

glycoside hydrolase (GH) family protein may catalyze the hydrolysis of glycosidic bonds in complex sugars; may belong to glycosyl hydrolase families GH32, GH43, GH62, GH68, GH117, or GH130

Gene Ontology:  GO:0016798
PubMed:  8535779

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH43_62_32_68_117_130 super family cl14647
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 21-361 1.67e-72

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.


The actual alignment was detected with superfamily member pfam04041:

Pssm-ID: 449341 [Multi-domain]  Cd Length: 315  Bit Score: 228.14  E-value: 1.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186   21 RRNETTDIVHRLGVIAPNRVYLNNYPiSNPIAVFNSALAVDEEDAILYARIIVGYFMYVSAIIAIRVPLDDIFSGsgdIN 100
Cdd:pfam04041   3 RKIPTIDILERPSYITGKDSRITNPV-RNPVAVFNPAVVLYEKELHVYPRVVMGYYKYVSDIASFRIGLEDSYDG---IK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  101 INYYAgQPVVYPSTKYDLWGTEDPRVYVIDGKLYMTYTGRTVNYFNPRIGRERTLPVTAVEEEKYykwkkihvYVFPPGL 180
Cdd:pfam04041  79 KTLEP-EPIFWPRDKQEFWGVEDPRVVKINSTYYMTYTGRDYKYWRIEVGTTKDFLTWARLPVKI--------ALFEKRY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  181 REHVVSNKDAFLVKLSNDLLLFHRPhmddDGFYLLTSRIGL------EELYSVaeqvrevvlrDTIWvtDKASFESKIGW 254
Cdd:pfam04041 150 DSIKTSDGNAFPVKIKGKYLMYHRV----GDIWLAVSPDLVhwenrlEPLGSP----------RPIM--FPNPFETKIGW 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  255 ATPPIKLRDnEIIALLHGVDYELEAYRLFAMQLEysrNEGiIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSrDK 334
Cdd:pfam04041 214 GTPPVETKE-GWLVLIHGVDTEDLVYRVGAALLD---LEG-KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDG-ER 287

                         330       340
                  ....*....|....*....|....*..
gi 500165186  335 ILISYGAGDYMIGLGEIDLNELLSILD 361
Cdd:pfam04041 288 VIIYYGAADTAIGLAEIPEEEIMNLLK 314
 
Name Accession Description Interval E-value
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 21-361 1.67e-72

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: 228.14  E-value: 1.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186   21 RRNETTDIVHRLGVIAPNRVYLNNYPiSNPIAVFNSALAVDEEDAILYARIIVGYFMYVSAIIAIRVPLDDIFSGsgdIN 100
Cdd:pfam04041   3 RKIPTIDILERPSYITGKDSRITNPV-RNPVAVFNPAVVLYEKELHVYPRVVMGYYKYVSDIASFRIGLEDSYDG---IK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  101 INYYAgQPVVYPSTKYDLWGTEDPRVYVIDGKLYMTYTGRTVNYFNPRIGRERTLPVTAVEEEKYykwkkihvYVFPPGL 180
Cdd:pfam04041  79 KTLEP-EPIFWPRDKQEFWGVEDPRVVKINSTYYMTYTGRDYKYWRIEVGTTKDFLTWARLPVKI--------ALFEKRY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  181 REHVVSNKDAFLVKLSNDLLLFHRPhmddDGFYLLTSRIGL------EELYSVaeqvrevvlrDTIWvtDKASFESKIGW 254
Cdd:pfam04041 150 DSIKTSDGNAFPVKIKGKYLMYHRV----GDIWLAVSPDLVhwenrlEPLGSP----------RPIM--FPNPFETKIGW 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  255 ATPPIKLRDnEIIALLHGVDYELEAYRLFAMQLEysrNEGiIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSrDK 334
Cdd:pfam04041 214 GTPPVETKE-GWLVLIHGVDTEDLVYRVGAALLD---LEG-KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDG-ER 287

                         330       340
                  ....*....|....*....|....*..
gi 500165186  335 ILISYGAGDYMIGLGEIDLNELLSILD 361
Cdd:pfam04041 288 VIIYYGAADTAIGLAEIPEEEIMNLLK 314
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
107-365 3.91e-28

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


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 111.77  E-value: 3.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 107 QPVVYPSTKYDLWGTEDPRVYVIDGKLYMTYTgrTVNYFNPRIGRERTlpvtaveeEKYYKWKKIHVyVFPPglrehvvS 186
Cdd:COG2152   69 EPILFPETDYEDTGVEDPRITKIDGRYYITYT--AYSGAGARIGLART--------KDFKTWERLGL-IFPP-------D 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 187 NKDAFL--VKLSNDLLLFHRPHmddDGFYLLTSRIGLEELYSVAEQVREVVL---RDTIWvtdkasFESKIGWATPPIKL 261
Cdd:COG2152  131 NKDAVLfpEKINGKYALLHRPS---DGFHTGGPDIWISYSPDLEHWGDHRIVmgpRPGTW------DSLKIGAGPPPIKT 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 262 RDNEIIaLLHGVDYELE--AYRLFAMQLeySRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSRDKILISY 339
Cdd:COG2152  202 EEGWLL-IYHGVRNTAAglVYRLGAALL--DLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVDEDGTVYIYY 278

                        250       260
                 ....*....|....*....|....*.
gi 500165186 340 GAGDYMIGLGEIDLNELLSILDKGRI 365
Cdd:COG2152  279 GAADTRIALATATLDELLDYLKNTPE 304
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 52-353 1.06e-24

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: 101.72  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  52 AVFNSAlAVDEEDAI--LY-AriiVGYFmYVSAI-IAIrvpLDDifsgsgDININYYAGQPVVYPST-KYDLWGTEDPRV 126
Cdd:cd18614    5 AVFNPA-AIYEDGKVhlLYrA---VGED-NISRLgYAS---SKD------GIHFDERLDEPVYVPKKsGGENGGCEDPRI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 127 YVIDGKLYMTYTGRTvNYFNPRIGrertlpVTAVEEEKYYKWKK---IHVYVFPPGLRehvvsNKDAFLV--KLSNDLLL 201
Cdd:cd18614   71 TKIDDTYYMTYTAYD-GWPPPRVA------LTSISTKDFLNFKWnwvIPPLISPPGVD-----DKDAVLFpeKINGKYAL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 202 FHRPHMD------DDgfylltsrigLEELYSVAEQVREVVLRDTIWvtdkasfES-KIGWATPPIKLRDNEIIaLLHGVD 274
Cdd:cd18614  139 LHRIGPDiwidysDD----------LDFGKNWIDSKIILEPRPGMW-------DSrKIGAGAPPIKTKKGWLL-IYHGVD 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500165186 275 YELEAYRLFAMQLEysRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSrDKILISYGAGDYMIGLGEIDL 353
Cdd:cd18614  201 DDDRVYRLGAALLD--LEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKD-DTLFVYYGGADKVIGVATAPL 276
 
Name Accession Description Interval E-value
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 21-361 1.67e-72

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: 228.14  E-value: 1.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186   21 RRNETTDIVHRLGVIAPNRVYLNNYPiSNPIAVFNSALAVDEEDAILYARIIVGYFMYVSAIIAIRVPLDDIFSGsgdIN 100
Cdd:pfam04041   3 RKIPTIDILERPSYITGKDSRITNPV-RNPVAVFNPAVVLYEKELHVYPRVVMGYYKYVSDIASFRIGLEDSYDG---IK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  101 INYYAgQPVVYPSTKYDLWGTEDPRVYVIDGKLYMTYTGRTVNYFNPRIGRERTLPVTAVEEEKYykwkkihvYVFPPGL 180
Cdd:pfam04041  79 KTLEP-EPIFWPRDKQEFWGVEDPRVVKINSTYYMTYTGRDYKYWRIEVGTTKDFLTWARLPVKI--------ALFEKRY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  181 REHVVSNKDAFLVKLSNDLLLFHRPhmddDGFYLLTSRIGL------EELYSVaeqvrevvlrDTIWvtDKASFESKIGW 254
Cdd:pfam04041 150 DSIKTSDGNAFPVKIKGKYLMYHRV----GDIWLAVSPDLVhwenrlEPLGSP----------RPIM--FPNPFETKIGW 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  255 ATPPIKLRDnEIIALLHGVDYELEAYRLFAMQLEysrNEGiIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSrDK 334
Cdd:pfam04041 214 GTPPVETKE-GWLVLIHGVDTEDLVYRVGAALLD---LEG-KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDG-ER 287

                         330       340
                  ....*....|....*....|....*..
gi 500165186  335 ILISYGAGDYMIGLGEIDLNELLSILD 361
Cdd:pfam04041 288 VIIYYGAADTAIGLAEIPEEEIMNLLK 314
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
107-365 3.91e-28

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


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 111.77  E-value: 3.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 107 QPVVYPSTKYDLWGTEDPRVYVIDGKLYMTYTgrTVNYFNPRIGRERTlpvtaveeEKYYKWKKIHVyVFPPglrehvvS 186
Cdd:COG2152   69 EPILFPETDYEDTGVEDPRITKIDGRYYITYT--AYSGAGARIGLART--------KDFKTWERLGL-IFPP-------D 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 187 NKDAFL--VKLSNDLLLFHRPHmddDGFYLLTSRIGLEELYSVAEQVREVVL---RDTIWvtdkasFESKIGWATPPIKL 261
Cdd:COG2152  131 NKDAVLfpEKINGKYALLHRPS---DGFHTGGPDIWISYSPDLEHWGDHRIVmgpRPGTW------DSLKIGAGPPPIKT 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 262 RDNEIIaLLHGVDYELE--AYRLFAMQLeySRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSRDKILISY 339
Cdd:COG2152  202 EEGWLL-IYHGVRNTAAglVYRLGAALL--DLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVDEDGTVYIYY 278

                        250       260
                 ....*....|....*....|....*.
gi 500165186 340 GAGDYMIGLGEIDLNELLSILDKGRI 365
Cdd:COG2152  279 GAADTRIALATATLDELLDYLKNTPE 304
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 52-353 1.06e-24

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: 101.72  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  52 AVFNSAlAVDEEDAI--LY-AriiVGYFmYVSAI-IAIrvpLDDifsgsgDININYYAGQPVVYPST-KYDLWGTEDPRV 126
Cdd:cd18614    5 AVFNPA-AIYEDGKVhlLYrA---VGED-NISRLgYAS---SKD------GIHFDERLDEPVYVPKKsGGENGGCEDPRI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 127 YVIDGKLYMTYTGRTvNYFNPRIGrertlpVTAVEEEKYYKWKK---IHVYVFPPGLRehvvsNKDAFLV--KLSNDLLL 201
Cdd:cd18614   71 TKIDDTYYMTYTAYD-GWPPPRVA------LTSISTKDFLNFKWnwvIPPLISPPGVD-----DKDAVLFpeKINGKYAL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 202 FHRPHMD------DDgfylltsrigLEELYSVAEQVREVVLRDTIWvtdkasfES-KIGWATPPIKLRDNEIIaLLHGVD 274
Cdd:cd18614  139 LHRIGPDiwidysDD----------LDFGKNWIDSKIILEPRPGMW-------DSrKIGAGAPPIKTKKGWLL-IYHGVD 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500165186 275 YELEAYRLFAMQLEysRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSrDKILISYGAGDYMIGLGEIDL 353
Cdd:cd18614  201 DDDRVYRLGAALLD--LEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKD-DTLFVYYGGADKVIGVATAPL 276
GH130 cd18607
Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by ...
 107-343 5.11e-17

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: 80.05  E-value: 5.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 107 QPVVYPSTK--YDLWGTEDPRVYVIDGKLYMTYTGrtVNYFNPRIGRERTlpvtaveeEKYYKWKKiHVYVFPPGLRehv 184
Cdd:cd18607   50 EPPLYPPPEnpYEKGGCEDPRITKIDDTYYMTYTA--YDGFGPRLALATT--------KDLKNWER-HGLAFPPAPE--- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 185 vsNKDA--FLVKLSNDLLLFHRPhmDDDGFYLLTSriglEELYSVAEQVRevVLRDTIwvtdKASFESKIGWATPPIKLR 262
Cdd:cd18607  116 --NKNGviFPEKINGKYAMLHRP--DGPDIWLATS----DDLIHWGDHKP--LLKPRK----GTWDSAKVGAGPPPIKTK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 263 DNeIIALLHGVD--YELEAYRLFAMQLEYSRNEGIIvkAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSRDKILISYG 340
Cdd:cd18607  182 KG-WLLLYHGVNetAAGNRYRLGAALLDLNDPTRVL--YRSDKPILEPEEDYEKSGYVPNVVFPCGAVAIDGDELKLYYG 258


                 ...
gi 500165186 341 AGD 343
Cdd:cd18607  259 AAD 261
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 107-350 2.25e-14

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: 72.16  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 107 QPVVYPSTKYDLWGTEDPRVYVIDGKLYMTYTGrtVNYFNPRIGRERTlpvtaveeEKYYKWKKIHVyVFPPglrehvvS 186
Cdd:cd18612   44 KPALFPEGPYEAFGIEDPRITRIDDTYYITYTA--VSEYGIATALAST--------KDFKTFERHGV-IFPP-------E 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 187 NKDA--FLVKLSNDLLLFHRP---HMDDDGFYLLTSriglEELYSVAEQVREVVLRDTIWVTDKasfeskIGWATPPIKL 261
Cdd:cd18612  106 NKDVviFPEKINGKYYALHRPvpsGFGKPEIWIAES----PDLLHWGNHRHLAGPRPGMWDSGR------IGAGAVPIKT 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 262 RDNEIIaLLHGVDyELEAYRLFAMQLEYSRNEGIIVKAVTPtyIMEPKLLYEIFGDRPYTIFPCGLWRLSrDKILISYGA 341
Cdd:cd18612  176 EKGWLE-IYHGAD-ENNRYCLGALLLDLEDPSKVIARSEEP--ILEPEAPYEKEGFFGNVVFTCGAVVEG-DTLLIYYGA 250


                 ....*....
gi 500165186 342 GDYMIGLGE 350
Cdd:cd18612  251 ADTSIAVAE 259
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 107-357 1.63e-13

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: 69.80  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 107 QPVVYPST---KYDLWGTEDPRVYVIDGKLYMTYTgrtVNYFN-PRIGRERTlpvtavEEEKyyKWKKIHvYVFPPGLRE 182
Cdd:cd08993   49 EPILTPDEpfePYEETGVYDPRITKIDDTYYITFA---ADSDHgPRIGLART------KDFK--TFERLE-LISEPDNRN 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 183 HVVsnkdaFLVKLSNDLLLFHRPHmddDGFYLLTSRIGLEelYS----VAEQVREVVL-RDTIWvtdkasFESKIGWATP 257
Cdd:cd08993  117 GVL-----FPEKINGKYARLDRPS---DGGHTSGGDIWIS--YSpdliHWGNSRLVMGpRPGPW------DNDKIGPGAP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 258 PIKLRDN--EIIallHGVDYEL--EAYRLFAMQLEysRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLSRD 333
Cdd:cd08993  181 PIKTEEGwlLIY---HGVRTTCsgFVYRLGAALLD--LEDPSKVIARSREPILAPEEPYERVGDVPNVVFPCGAIVEEDG 255

                        250       260
                 ....*....|....*....|....
gi 500165186 334 KILISYGAGDYMIGLGEIDLNELL 357
Cdd:cd08993  256 EVKIYYGAADTVICLATATIDDLV 279
GH130 cd18615
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 45-348 4.34e-09

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: 56.85  E-value: 4.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  45 YPISnpiAVFNSALAVDEEDAILYARiiVGYFMYVSAIIAIRVPlddifSGSGDININyyaGQPVVYPSTK---YDLWGT 121
Cdd:cd18615    3 YPAN---AVFNPGAAKLGGETLLLVR--VEDRRGFSHLTVARSA-----DGVTNWKID---PKPTLEPDPEdypEEMWGI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 122 EDPR-VYVID-GKLYMTYTGRTvnyfnprigreRTLPVTAVEEEKYYKWKKIHVYVFPPglrehvvSNKDA--FLVKLSN 197
Cdd:cd18615   70 EDPRiTWLEElGRYAITYTAYS-----------PAGPGVSLATTKDFKTFERLGLVMPP-------EDKDAalFPRRING 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 198 DLLLFHRPhMDDDGFYLLTSRIglEELYSVAEqvREVVL--RDTIWvTDKAsfesKIGWATPPIKLRDNEIIaLLHGVDY 275
Cdd:cd18615  132 RWALLHRP-VSAGRAHIWISFS--PDLKHWGD--HRPVLpaRRGPW-WDAV----KVGLGPPPIETPEGWLI-IYHGVKE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500165186 276 EL--EAYRLFAMQLEysRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCG-LWRLSRDKILISYGAGDYMIGL 348
Cdd:cd18615  201 TAsgSIYRVGLALLD--LEDPTKVIRRSDEWVLGPEEPYERIGDVPNVVFPCGaILDEDGDELRLYYGAADTCIAL 274
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
 107-348 1.04e-06

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: 49.89  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 107 QPVVYPSTKYDlW--GTEDPRVYVI-DGKLYMTYTGrtvnyFNPRIGRertLPVtAVEEEkYYKWKKiHVYVFP--PGLR 181
Cdd:cd18610   62 EPVLYPEEDYE-WpgGCEDPRIVEIeDGTYYMTYTA-----YDGKTAR---LCL-ATSTD-LVHWTK-HGPAFPdaDGGK 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 182 EHVVSNKD-AFLVKLSNDLLLFHRPHM--DDDGFYLLTSriglEELYSVAEQVREVVLRdTIWVTDKASFESKIGWATPP 258
Cdd:cd18610  130 YRDLWSKSgAIVPELKGAAKINGKYWMywGESNIYLATS----DDLIHWTPVEDDGSLR-PVLSPRPGKFDSDLVEPGPP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186 259 IKLRDNEIIALLHGVD-------YELEAYRlfAMQLEYSRNEGIIVKAVTPTYIMEPKLLYEIFGDRPYTIFPCGLWRLs 331
Cdd:cd18610  205 PILTDGGILLIYNGANdggggpgYPKGTYS--AGQALFDANDPTKLLARLDKPFLEPETPYEKEGQVNNVVFVEGLVYF- 281

                        250
                 ....*....|....*..
gi 500165186 332 RDKILISYGAGDYMIGL 348
Cdd:cd18610  282 KGKWLLYYGTADSKIGV 298
GH130 cd18611
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 52-139 2.09e-03

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: 39.43  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165186  52 AVFNSALAVDEED------AILYARIIVGYFMYVSAI-IAirvplddiFSGSGdinINYYAGQPVVYPSTKYDLWGTEDP 124
Cdd:cd18611    5 AVFNGSVIKDGGKyhllyrALSSPQEIDGPKLGLSTIgYA--------ESKDG---VHFENRRQLIKPEEEWEKYGCEDP 73

                         90
                 ....*....|....*
gi 500165186 125 RVYVIDGKLYMTYTG 139
Cdd:cd18611   74 RVTKIDGKYYIFYTA 88
 
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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