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Conserved domains on  [gi|3130021|emb|CAA76702|]
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sucrase, partial [Lactiplantibacillus plantarum]

Protein Classification

sucrose-6-phosphate hydrolase( domain architecture ID 1003399)

sucrose-6-phosphate hydrolase catalyzes the hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides

EC:  3.2.1.26
Gene Ontology:  GO:0005975|GO:0004564

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
scrB_fam super family cl36871
sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of ...
1-231 3.70e-139

sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of polysaccharides]


The actual alignment was detected with superfamily member TIGR01322:

Pssm-ID: 273554 [Multi-domain]  Cd Length: 445  Bit Score: 397.14  E-value: 3.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:TIGR01322  33 IYFKGEYHLFYQWFPFGPVHGLKSWGHYTSKDLVHWEDEGVALAPDDPYDSHGCYSGSAVDNNGQLTLMYTGNVRDSDWN 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     81 RESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGELN 160
Cdd:TIGR01322 113 RESYQCLATMDDDGHFEKFGIVVIELPPAGYTAHFRDPKVWKHNGHWYMVIGAQTETEKGSILLYRSKDLKNWTFVGEIL 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3130021    161 VPA----NARGYMIECPNLVWIDQQPVLLFCPQGLSQTTTPYQNIYPNMYLVAdQLDLAQAQFTEPHALTQLDDG 231
Cdd:TIGR01322 193 GDGqnglDDRGYMWECPDLFSLDGQDVLLFSPQGLDASGYDYQNIYQNGYIVG-QLDYEAPEFTHGTEFHELDYG 266
 
Name Accession Description Interval E-value
scrB_fam TIGR01322
sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of ...
1-231 3.70e-139

sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273554 [Multi-domain]  Cd Length: 445  Bit Score: 397.14  E-value: 3.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:TIGR01322  33 IYFKGEYHLFYQWFPFGPVHGLKSWGHYTSKDLVHWEDEGVALAPDDPYDSHGCYSGSAVDNNGQLTLMYTGNVRDSDWN 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     81 RESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGELN 160
Cdd:TIGR01322 113 RESYQCLATMDDDGHFEKFGIVVIELPPAGYTAHFRDPKVWKHNGHWYMVIGAQTETEKGSILLYRSKDLKNWTFVGEIL 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3130021    161 VPA----NARGYMIECPNLVWIDQQPVLLFCPQGLSQTTTPYQNIYPNMYLVAdQLDLAQAQFTEPHALTQLDDG 231
Cdd:TIGR01322 193 GDGqnglDDRGYMWECPDLFSLDGQDVLLFSPQGLDASGYDYQNIYQNGYIVG-QLDYEAPEFTHGTEFHELDYG 266
GH32_ScrB-like cd18623
glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase ...
1-231 1.25e-113

glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose. 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. 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: 350135  Cd Length: 289  Bit Score: 326.77  E-value: 1.25e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:cd18623  10 CYFNGKYHIFYQWNPFGPVHGLKYWGHVTSKDLVHWEDEGVALKPDTPYDKHGVYSGSALVEDDKLYLFYTGNVKDEGGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   81 RESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGELN 160
Cdd:cd18623  90 REPYQCLATSDDGGKFKKKEVLLIEDPPEGYTEHFRDPKVFKKDGKYYMLLGAQTKDDKGRILLYRSDDLLDWTYLGELL 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3130021  161 VPANARGYMIECPNLVWIDQQPVLLFCPQGLSQTTTPYQNIYPNMYLVADQLDLaqAQFTEPHALTQLDDG 231
Cdd:cd18623 170 TGLEDFGYMWECPDLFELDGKDVLIFCPQGLDKEGDRYQNIYQSGYLIGDLDFE--NLFFNHGDFQELDYG 238
Glyco_hydro_32N pfam00251
Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal ...
1-231 3.21e-86

Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.


Pssm-ID: 425557  Cd Length: 308  Bit Score: 257.95  E-value: 3.21e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRtADWQ 80
Cdd:pfam00251  16 VYYNGEYHLFYQYNPFGAVWGNKHWGHAVSKDLVHWEHLPVALAPDEWYDSNGCFSGSAVVDPDNLVLIYTGNVR-DEGR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     81 RESYQLGAWM-DTDNHIKKLS-RPLIAHAPAGYTSSFRDPDLI-RTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQG 157
Cdd:pfam00251  95 DTQVQNLAYSkDDGRTFTKYPnNPVIINLPAGYTKHFRDPKVAwYEDGKWYMVLGAQDNDKKGKILLYKSDDLKNWTFVG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    158 ELNVPANARGYMIECPNLVWIDQQP------VLLFCPQGLSqtttpYQNIYPNMYLVAdQLDLAQAQFTEPHALTQLDDG 231
Cdd:pfam00251 175 ELLHSNDGGGYMWECPDLFPLDGKDgekwkhVLKFSPQGLS-----YDNIYQDYYFIG-SFDLDGDKFTPDGEFLRLDYG 248
SacC COG1621
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];
1-231 1.17e-84

Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];


Pssm-ID: 441228 [Multi-domain]  Cd Length: 459  Bit Score: 258.70  E-value: 1.17e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:COG1621  25 VYFDGEYHLFYQYNPYGPVWGPMHWGHATSTDLVHWEHLPIALAPDEEYDSGGCFSGSAVVDDGNLVLFYTGNVRDGDGG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   81 RESYQLGAWMDTDNHIKKLS-RPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGEL 159
Cdd:COG1621 105 RRQYQCLAYSTDGRTFTKYEgNPVIPNPPGGYTKDFRDPKVWWDDGKWYMVLGAQTGDGKGTVLLYTSPDLKNWTYLGEF 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3130021  160 NVPANARGYMIECPNLVWIDQQPVLLFCPQGLsqtttPYQNIYPNMYLVADqLDLaqAQFTePHALTQLDDG 231
Cdd:COG1621 185 GEGDGAFGYMWECPDLFPLDGKWVLIFSPQGG-----GPEGGSQTGYFVGD-FDG--ETFT-PEEFQELDYG 247
Glyco_32 smart00640
Glycosyl hydrolases family 32;
2-210 2.16e-68

Glycosyl hydrolases family 32;


Pssm-ID: 214757 [Multi-domain]  Cd Length: 437  Bit Score: 216.42  E-value: 2.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021       2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVR---TAD 78
Cdd:smart00640  17 YYKGKYHLFYQYNPFGAVWGNIHWGHAVSKDLVHWTHLPVALAPDEWYDSNGVFSGSAVIDPGNLSLLYTGNVAidtNVQ 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      79 WQRESYQLGAWMDTDNHIKKLSR-PLIAHAPAGYTSSFRDPDLIRTDHG-YYALIGAQTTTEIGAILVYFSKDLTTWTCQ 156
Cdd:smart00640  97 VQRQAYQCAASDDLGGTWTKYDGnPVLTPPPGGGTEHFRDPKVFWYDGDkWYMVIGASDEDKRGIALLYRSTDLKNWTLL 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     157 GE-LNVPANARGYMIECPNLVWID-----QQPVLLFCPQGlsqtttPYQNIYPNMYLVAD 210
Cdd:smart00640 177 SEfLHSLLGDTGGMWECPDLFPLPgegdtSKHVLKVSPQG------GSGNYYFVGYFDGD 230
beta-fruc_BfrA NF041092
beta-fructosidase;
2-186 6.29e-23

beta-fructosidase;


Pssm-ID: 469018 [Multi-domain]  Cd Length: 433  Bit Score: 95.74  E-value: 6.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTpyDSHGAYTGTALPIDDQLFIMYT--GNVRTADW 79
Cdd:NF041092  23 FWKGKYHMFYQYNPKKPKWGNICWGHAVSDDLVHWRHLPVALYPKD--ETHGVFSGSAVEKDGKMVLVYTyyRDPGHNIG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    80 QRESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGEL 159
Cdd:NF041092 101 EKEVQCIAMSEDGINFVEYTRNPVISKPPEEGTHAFRDPKVNRNGDRWRMVLGSGKDEKIGKVLLYTSEDLIHWYYEGVL 180
                        170       180
                 ....*....|....*....|....*..
gi 3130021   160 NVPANARgyMIECPNLVWIDQQPVLLF 186
Cdd:NF041092 181 FEDESTK--EIECPDLVKIGGKDVLIY 205
 
Name Accession Description Interval E-value
scrB_fam TIGR01322
sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of ...
1-231 3.70e-139

sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273554 [Multi-domain]  Cd Length: 445  Bit Score: 397.14  E-value: 3.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:TIGR01322  33 IYFKGEYHLFYQWFPFGPVHGLKSWGHYTSKDLVHWEDEGVALAPDDPYDSHGCYSGSAVDNNGQLTLMYTGNVRDSDWN 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     81 RESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGELN 160
Cdd:TIGR01322 113 RESYQCLATMDDDGHFEKFGIVVIELPPAGYTAHFRDPKVWKHNGHWYMVIGAQTETEKGSILLYRSKDLKNWTFVGEIL 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3130021    161 VPA----NARGYMIECPNLVWIDQQPVLLFCPQGLSQTTTPYQNIYPNMYLVAdQLDLAQAQFTEPHALTQLDDG 231
Cdd:TIGR01322 193 GDGqnglDDRGYMWECPDLFSLDGQDVLLFSPQGLDASGYDYQNIYQNGYIVG-QLDYEAPEFTHGTEFHELDYG 266
GH32_ScrB-like cd18623
glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase ...
1-231 1.25e-113

glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose. 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. 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: 350135  Cd Length: 289  Bit Score: 326.77  E-value: 1.25e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:cd18623  10 CYFNGKYHIFYQWNPFGPVHGLKYWGHVTSKDLVHWEDEGVALKPDTPYDKHGVYSGSALVEDDKLYLFYTGNVKDEGGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   81 RESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGELN 160
Cdd:cd18623  90 REPYQCLATSDDGGKFKKKEVLLIEDPPEGYTEHFRDPKVFKKDGKYYMLLGAQTKDDKGRILLYRSDDLLDWTYLGELL 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3130021  161 VPANARGYMIECPNLVWIDQQPVLLFCPQGLSQTTTPYQNIYPNMYLVADQLDLaqAQFTEPHALTQLDDG 231
Cdd:cd18623 170 TGLEDFGYMWECPDLFELDGKDVLIFCPQGLDKEGDRYQNIYQSGYLIGDLDFE--NLFFNHGDFQELDYG 238
Glyco_hydro_32N pfam00251
Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal ...
1-231 3.21e-86

Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.


Pssm-ID: 425557  Cd Length: 308  Bit Score: 257.95  E-value: 3.21e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRtADWQ 80
Cdd:pfam00251  16 VYYNGEYHLFYQYNPFGAVWGNKHWGHAVSKDLVHWEHLPVALAPDEWYDSNGCFSGSAVVDPDNLVLIYTGNVR-DEGR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     81 RESYQLGAWM-DTDNHIKKLS-RPLIAHAPAGYTSSFRDPDLI-RTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQG 157
Cdd:pfam00251  95 DTQVQNLAYSkDDGRTFTKYPnNPVIINLPAGYTKHFRDPKVAwYEDGKWYMVLGAQDNDKKGKILLYKSDDLKNWTFVG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    158 ELNVPANARGYMIECPNLVWIDQQP------VLLFCPQGLSqtttpYQNIYPNMYLVAdQLDLAQAQFTEPHALTQLDDG 231
Cdd:pfam00251 175 ELLHSNDGGGYMWECPDLFPLDGKDgekwkhVLKFSPQGLS-----YDNIYQDYYFIG-SFDLDGDKFTPDGEFLRLDYG 248
SacC COG1621
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];
1-231 1.17e-84

Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];


Pssm-ID: 441228 [Multi-domain]  Cd Length: 459  Bit Score: 258.70  E-value: 1.17e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    1 SYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQ 80
Cdd:COG1621  25 VYFDGEYHLFYQYNPYGPVWGPMHWGHATSTDLVHWEHLPIALAPDEEYDSGGCFSGSAVVDDGNLVLFYTGNVRDGDGG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   81 RESYQLGAWMDTDNHIKKLS-RPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGEL 159
Cdd:COG1621 105 RRQYQCLAYSTDGRTFTKYEgNPVIPNPPGGYTKDFRDPKVWWDDGKWYMVLGAQTGDGKGTVLLYTSPDLKNWTYLGEF 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3130021  160 NVPANARGYMIECPNLVWIDQQPVLLFCPQGLsqtttPYQNIYPNMYLVADqLDLaqAQFTePHALTQLDDG 231
Cdd:COG1621 185 GEGDGAFGYMWECPDLFPLDGKWVLIFSPQGG-----GPEGGSQTGYFVGD-FDG--ETFT-PEEFQELDYG 247
Glyco_32 smart00640
Glycosyl hydrolases family 32;
2-210 2.16e-68

Glycosyl hydrolases family 32;


Pssm-ID: 214757 [Multi-domain]  Cd Length: 437  Bit Score: 216.42  E-value: 2.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021       2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVR---TAD 78
Cdd:smart00640  17 YYKGKYHLFYQYNPFGAVWGNIHWGHAVSKDLVHWTHLPVALAPDEWYDSNGVFSGSAVIDPGNLSLLYTGNVAidtNVQ 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021      79 WQRESYQLGAWMDTDNHIKKLSR-PLIAHAPAGYTSSFRDPDLIRTDHG-YYALIGAQTTTEIGAILVYFSKDLTTWTCQ 156
Cdd:smart00640  97 VQRQAYQCAASDDLGGTWTKYDGnPVLTPPPGGGTEHFRDPKVFWYDGDkWYMVIGASDEDKRGIALLYRSTDLKNWTLL 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     157 GE-LNVPANARGYMIECPNLVWID-----QQPVLLFCPQGlsqtttPYQNIYPNMYLVAD 210
Cdd:smart00640 177 SEfLHSLLGDTGGMWECPDLFPLPgegdtSKHVLKVSPQG------GSGNYYFVGYFDGD 230
GH32_FFase cd08996
Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves ...
2-231 1.99e-53

Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves 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: 350110  Cd Length: 281  Bit Score: 173.21  E-value: 1.99e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGnVRTADWQR 81
Cdd:cd08996  11 YYKGRYHLFYQYNPYGPVWGPMHWGHAVSDDLVHWEHLPIALAPPGGYDEDGCFSGSAVVDDGKPTLFYTG-VRDLGDGR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   82 ESyQLGAWMDTD-NHIKKLSR-PLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGEL 159
Cdd:cd08996  90 QT-QCLATSDDDlITWEKYPGnPVIPPPPGGGVTDFRDPFVWKEGGTWYMVVGGGLEDGGGAVLLYRSDDLRDWEYLGVL 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3130021  160 --NVPANARGYMIECPNLVWIDQQPVLLFCPQGLsqtttpyQNIYPNMYLVADqLDLAQAQFtEPHALTQLDDG 231
Cdd:cd08996 169 ldAASDGDTGEMWECPDFFPLGGKWVLLFSPQGG-------GNLLGVVYLIGD-FDGETFRF-EPESFGLLDYG 233
GH32_BfrA-like cd18625
glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414); ...
2-187 2.74e-32

glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414); This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that cleaves 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. 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. 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: 350137  Cd Length: 286  Bit Score: 118.54  E-value: 2.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDT-----PYDSHGAYTGTALPIDDQLFIMYT---GN 73
Cdd:cd18625  11 YFKGYYHLFYQYNPHGQEWGNMHWGHAVSKDLVHWTHLPVALYPQPellldRELTGGAFSGSAVVKDDKMRLFYTrhfDP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   74 VRTADWQREsYQLGAWMDTDNHIKKlSRPLIAHAPAGYTSSFRDPDLIRTDHG-YYALIGAQTTtEIGAILVYFSKDLTT 152
Cdd:cd18625  91 RDLRSGEIE-WQKTAVSKDGIHFEK-EETIIEIRPEGVSHDFRDPKVFREEDGkWKMVLGSGLD-GIPAVLLYESDDLEH 167
                       170       180       190
                ....*....|....*....|....*....|....*
gi 3130021  153 WTCQGELNVPANARGYMIECPNLVWIDQQPVLLFC 187
Cdd:cd18625 168 WTYEGVLYTEEEEGGRCIECPDLFPLDGKWVLIYS 202
GH32_Inu-like cd18622
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This ...
2-176 1.19e-24

glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes 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). 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: 350134  Cd Length: 289  Bit Score: 98.46  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYdsHGAYTGTALpIDDQ------------LFIM 69
Cdd:cd18622  12 YYDGEYHLFYQYNPDGNVWGNMHWGHAVSKDLVHWEELPIALPPPDEL--GDIFSGSAV-VDKNntsglggfgkgaLVAI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   70 YTGNvrtadWQRESYQLGAWMDTDN--HIKKLSRPLIahAPAGYTSSFRDPDLIR-TDHGYYALIGAqtttEIGAILVYF 146
Cdd:cd18622  89 YTSA-----GPDGGQTQSLAYSTDGgrTFTKYEGNPV--LPNPGSTDFRDPKVFWhEPSGKWVMVLA----EGDKIGFYT 157
                       170       180       190
                ....*....|....*....|....*....|
gi 3130021  147 SKDLTTWTCQGELnVPANARGYMIECPNLV 176
Cdd:cd18622 158 SPDLKNWTYLSEF-GPEGADGGVWECPDLF 186
GH32_Fruct1-like cd18624
glycoside hydrolase family 32 protein such as Arabidopsis thaliana cell-wall invertase 1 ...
2-175 3.18e-24

glycoside hydrolase family 32 protein such as Arabidopsis thaliana cell-wall invertase 1 (AtBFruct1;Fruct1;AtcwINV1;At3g13790); This subfamily of glycosyl hydrolase family GH32 includes fructan beta-(2,1)-fructosidase and fructan 1-exohydrolase IIa (1-FEH IIa, EC 3.2.1.153), cell-wall invertase 1 (EC 3.2.1.26), sucrose:fructan 6-fructosyltransferase (6-Sst/6-Dft, EC 2.4.1.10), and levan fructosyltransferases (EC 2.4.1.-) among others. This enzyme cleaves 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. 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. 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: 350136 [Multi-domain]  Cd Length: 296  Bit Score: 97.46  E-value: 3.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQL-FIMYTGnVRTADWQ 80
Cdd:cd18624  11 YYKGLYHLFYQYNPHGAVWGNIVWGHAVSRDLVNWQHLPIALDPDEWYDINGVWSGSATILPDGTpVILYTG-VDANSVQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   81 RESYQLGA---------WmdtdnhIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHG--YYALIGAqTTTEIGAILVYFSKD 149
Cdd:cd18624  90 VQNLAFPAnpsdpllreW------VKPPGNPVIAPPPGINPDNFRDPTTAWLGPDglWRIVVGA-RIGGRGIALLYRSKD 162
                       170       180
                ....*....|....*....|....*.
gi 3130021  150 LTTWTcQGELNVPANARGYMIECPNL 175
Cdd:cd18624 163 FKTWE-LNPAPLHSVDGTGMWECPDF 187
beta-fruc_BfrA NF041092
beta-fructosidase;
2-186 6.29e-23

beta-fructosidase;


Pssm-ID: 469018 [Multi-domain]  Cd Length: 433  Bit Score: 95.74  E-value: 6.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021     2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTpyDSHGAYTGTALPIDDQLFIMYT--GNVRTADW 79
Cdd:NF041092  23 FWKGKYHMFYQYNPKKPKWGNICWGHAVSDDLVHWRHLPVALYPKD--ETHGVFSGSAVEKDGKMVLVYTyyRDPGHNIG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    80 QRESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRTDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGEL 159
Cdd:NF041092 101 EKEVQCIAMSEDGINFVEYTRNPVISKPPEEGTHAFRDPKVNRNGDRWRMVLGSGKDEKIGKVLLYTSEDLIHWYYEGVL 180
                        170       180
                 ....*....|....*....|....*..
gi 3130021   160 NVPANARgyMIECPNLVWIDQQPVLLF 186
Cdd:NF041092 181 FEDESTK--EIECPDLVKIGGKDVLIY 205
GH32_EcAec43-like cd08995
Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 ...
2-175 1.06e-19

Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2); This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes 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). GH32 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.


Pssm-ID: 350109 [Multi-domain]  Cd Length: 281  Bit Score: 84.93  E-value: 1.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFY-QVFPFGPVHGLK-SWQHVTSKNLVDWHDEGLAI-RPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTAD 78
Cdd:cd08995   7 YDDGKFHLFYlHDPRDPAPHRGGhPWALVTTKDLVHWTEHGEAIpYGGDDDQDLAIGTGSVIKDDGTYHAFYTGHNPDFG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   79 WQRESYQLgAWMDTDNHIKKLSRPLIAHAPAGY-TSSFRDPDLIR-TDHG-YYALIGAQTTTEI----GAILVYFSKDLT 151
Cdd:cd08995  87 KPKQVIMH-ATSTDLKTWTKDPEFTFIADPEGYeKNDFRDPFVFWnEEEGeYWMLVAARKNDGPgnrrGCIALYTSKDLK 165
                       170       180
                ....*....|....*....|....
gi 3130021  152 TWTCQGELNVPANarGYMIECPNL 175
Cdd:cd08995 166 NWTFEGPFYAPGS--YNMPECPDL 187
GH32_XdINV-like cd18621
glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous ...
5-165 3.78e-17

glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV); This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), among others. These enzymes 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). 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. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. 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: 350133  Cd Length: 337  Bit Score: 78.82  E-value: 3.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    5 GQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEG---LAIRPDTPYDSHGAYTGTALP-----IDDQLFIMYTGNVRT 76
Cdd:cd18621  16 GLYHLFYQWNPNGVEWGNISWGHATSKDLVTWTDSGedpPALGPDGPYDSLGVFTGCVIPnglngQDGTLTLFYTSVSHL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   77 ADWQRESYQLG------AWmDTDNHI--KKLSR-PLIAHAPAGY-TSSFRDP----------DLIRTDHGYYALIGAQTT 136
Cdd:cd18621  96 PIHWTLPYTRGsetqslAT-SSDGGRtwQKYEGnPILPGPPEGLnVTGWRDPfvfpwpaldkLLGDSGPTLYGLISGGIR 174
                       170       180       190
                ....*....|....*....|....*....|.
gi 3130021  137 TEIGAILVYFS--KDLTTWTCQGELNVPANA 165
Cdd:cd18621 175 GVGPRVFLYRIddSDLTDWTYLGPLEPPVNS 205
GH32-like cd18609
Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase ...
4-187 2.16e-11

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: 62.27  E-value: 2.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    4 DGQWHLFYQVFP--FGPV---HGLKSWQHVTSKNLVDWHDEGLAIRPDTP--YDSHGAYTGTALPIDDQLFIM-YTGNVR 75
Cdd:cd18609  18 GGTYHLFYLQAPrsLGDPelrHRNARIGHAVSTDLVHWERLGDALGPGDPgaWDDLATWTGSVIRDPDGLWRMfYTGTSR 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   76 TADWQRE------SYQLGAWmdtdnhiKKLSR-PLIAHAPAGYTS---------SFRDPDLIR--TDHGYYALIGAQTTT 137
Cdd:cd18609  98 AEDGLVQriglatSDDLITW-------TKHPGnPLLAADPRWYETlgdsgwhdeAWRDPWVFRdpDGGGWHMLITARANE 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3130021  138 ----EIGAILVYFSKDLTTWTCQGELNVPAnARGYMiECPNLVWIDQQPVLLFC 187
Cdd:cd18609 171 gppdGRGVIGHATSPDLEHWEVLPPLSAPG-VFGHL-EVPQVFEIDGRWYLLFS 222
GH_J cd08979
Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase ...
2-196 4.23e-10

Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other 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.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and 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. 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: 350093 [Multi-domain]  Cd Length: 292  Bit Score: 58.35  E-value: 4.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAI--RPDTPYDSHGAYTGTALPI-DDQLFIMYTG-NVRTA 77
Cdd:cd08979   8 NANGYYHLFYLYGPPKNFADNVSIGHAYSKDLENWIDLPKALgaNDTISDDQTQEWSGSATFTsDGKWRAFYTGfSGKHY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   78 DWQRESYqlgAWMDTDNH------IKKLSRPLIAHAPAGYTSSFRDPDLI--RTDHGYYALIGAQTTTEiGAILVYFSKD 149
Cdd:cd08979  88 GVQSQTI---AYSKDLASwsslniNGVPQFPDELPPSSGDNQTFRDPHVVwdKEKGHWYMVFTAREGAN-GVLGMYESTD 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3130021  150 LTTWTCQGELNvPANARGYMIECPNLVWIDQQPVLLFCPQGLSQTTT 196
Cdd:cd08979 164 LKHWKKVMKPI-ASNTVTGEWECPNLVKMNGRWYLFFGSRGSKGITS 209
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
2-176 9.65e-09

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: 54.14  E-value: 9.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021    2 YFDGQWHLFYQvfpFGPVHGLKSWQHVTSKNLVDWHDEGLAI--RPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADW 79
Cdd:cd08772   7 PYNGEYHLFFT---IGPKNTRPFLGHARSKDLIHWEEEPPAIvaRGGGSYDTSYAFDPEVVYIEGTYYLTYCSDDLGDIL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3130021   80 QRESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDL-IRTDHGYYALI--GAQTTTEIGAILVYFSKDLTTWTcQ 156
Cdd:cd08772  84 RHGQHIGVAYSKDPKGPWTRKDAPLIEPPNAYSPKNRDPVLfPRKIGKYYLLNvpSDNGHTRFGKIAIAESPD*LHWI-N 162
                       170       180
                ....*....|....*....|
gi 3130021  157 GELNVPANARGYMIECPNLV 176
Cdd:cd08772 163 HSFVYNYNEQGKVGEGPSLW 182
 
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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