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Conserved domains on  [gi|764952756|ref|WP_044523014|]
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MULTISPECIES: glycoside hydrolase family 10 protein [Klebsiella]

Protein Classification

glycoside hydrolase family 10 protein( domain architecture ID 11447250)

glycoside hydrolase family 10 protein similar to Bacillus subtilis sporulation protein YngK, which may be involved in antibiotic synthesis

CAZY:  GH10
EC:  3.2.1.-
Gene Ontology:  GO:0016787|GO:0005975
PubMed:  8535779|7624375|21639842|31731209|20552664

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YddW COG1649
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];
25-424 1.45e-141

Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];


:

Pssm-ID: 441255 [Multi-domain]  Cd Length: 451  Bit Score: 411.79  E-value: 1.45e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  25 LVTPPKSAAVKAGQTHREPVRGVWLTTVSrldwppvgsiiastpeSRITQQKLALIAKLDNLQRLGINTVFFQVKPDGTA 104
Cdd:COG1649   14 SLLGCSAPAPAAAPSPKREIRGVWLTTVD----------------LSVLKQKAELIEILDRLKELGFNAVFFQVRPAGDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 105 LWRSDILPWSDMLTGKIGEYPGYDPLQFMLDEAHKRGMKVHAWFNPYRVSVNTKPSTIAelnntltqvPASVFVLHRNWI 184
Cdd:COG1649   78 LYPSAIEPWSEYLTGTQGKDPGYDPLAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLA---------PSHIAKKHPEWL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 185 RTASD--RFVLDPGIPEARDWITSIVAEVVQNYPIDGVQFDDYFYTETAaspLNDNETFRRYGQGY-------ASKGDWR 255
Cdd:COG1649  149 TKYRDggKLWLNPGHPEVRDFILDLVLEVVTRYDVDGIHFDDYFYPSEF---GYDDATYALYGQETgfdnpkdLSWADWR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 256 RHNTQQLIAQVSATIKKLNPNVEFGVSPAGVWRNrshdpagSDTrGAAAYDESYADTRSWVQQGLLDYIAPQIYWPFARD 335
Cdd:COG1649  226 RDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRN-------SPT-GLFAYDDLYQDWRTWVKEGWVDYIVPQLYWPDGNS 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 336 AARYDVLANWWAEVVKPTHTRLYIGVALYKVgepsknepdwtvdgGVPELKKQLDLNESLPQIQGTILFRENNLNQPqtR 415
Cdd:COG1649  298 AADFEKLLDWWAQQAKGRKVPLYIGIGLYKV--------------PPEEILRQIQLNRDLPGVAGVVFFSYESLWNN--P 361


                 ....*....
gi 764952756 416 QAVNYLRSR 424
Cdd:COG1649  362 GLADALRQG 370
 
Name Accession Description Interval E-value
YddW COG1649
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];
25-424 1.45e-141

Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];


Pssm-ID: 441255 [Multi-domain]  Cd Length: 451  Bit Score: 411.79  E-value: 1.45e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  25 LVTPPKSAAVKAGQTHREPVRGVWLTTVSrldwppvgsiiastpeSRITQQKLALIAKLDNLQRLGINTVFFQVKPDGTA 104
Cdd:COG1649   14 SLLGCSAPAPAAAPSPKREIRGVWLTTVD----------------LSVLKQKAELIEILDRLKELGFNAVFFQVRPAGDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 105 LWRSDILPWSDMLTGKIGEYPGYDPLQFMLDEAHKRGMKVHAWFNPYRVSVNTKPSTIAelnntltqvPASVFVLHRNWI 184
Cdd:COG1649   78 LYPSAIEPWSEYLTGTQGKDPGYDPLAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLA---------PSHIAKKHPEWL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 185 RTASD--RFVLDPGIPEARDWITSIVAEVVQNYPIDGVQFDDYFYTETAaspLNDNETFRRYGQGY-------ASKGDWR 255
Cdd:COG1649  149 TKYRDggKLWLNPGHPEVRDFILDLVLEVVTRYDVDGIHFDDYFYPSEF---GYDDATYALYGQETgfdnpkdLSWADWR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 256 RHNTQQLIAQVSATIKKLNPNVEFGVSPAGVWRNrshdpagSDTrGAAAYDESYADTRSWVQQGLLDYIAPQIYWPFARD 335
Cdd:COG1649  226 RDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRN-------SPT-GLFAYDDLYQDWRTWVKEGWVDYIVPQLYWPDGNS 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 336 AARYDVLANWWAEVVKPTHTRLYIGVALYKVgepsknepdwtvdgGVPELKKQLDLNESLPQIQGTILFRENNLNQPqtR 415
Cdd:COG1649  298 AADFEKLLDWWAQQAKGRKVPLYIGIGLYKV--------------PPEEILRQIQLNRDLPGVAGVVFFSYESLWNN--P 361


                 ....*....
gi 764952756 416 QAVNYLRSR 424
Cdd:COG1649  362 GLADALRQG 370
GHL10 pfam02638
Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins ...
 43-376 4.67e-123

Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.


Pssm-ID: 251441 [Multi-domain]  Cd Length: 311  Bit Score: 359.60  E-value: 4.67e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756   43 PVRGVWLTTVSRLDWPpvgsiiastpesrITQQKLALIAKLDNLQrlgINTVFFQVKPDGTALWRSDILPWSDMLTGKIG 122
Cdd:pfam02638   1 EIRGVWLTNVDSNDWP-------------DPVQLQEAIALLDDLN---FNTVYPQVWNDGHALYPSAVAPWSGLKTGEKG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  123 EYPGYDPLQFMLDEAHKRGMKVHAWFnpyRVSVNTKPstiaeLNNTLTQVPASVFVLHRNWIRT----ASDRFVLDPGIP 198
Cdd:pfam02638  65 GDPGYDPLAFMIDEAHKRNLRVHPWF---EFGFNAPA-----LSDLVKAHPAWLTTQHRDWTITseggTGPRVWLNPGHP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  199 EARDWITSIVAEVVQNYPIDGVQFDDYFY-TETAASPLNDNETFRRYGQGYA-------SKGDWRRHNTQQLIAQVSATI 270
Cdd:pfam02638 137 EVQDFITALVVDVVRRYDVDGVQFDDHFYyPYSFGYDPITVALYRQETKQEPfsnpeddLNTDWRRDKISQLVQQLNPTI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  271 KKLNPNVEFGVSPAGVWRnrshdpagsdtrgaAAYDESYADTRSWVQQGLLDYIAPQIYWP-FARDAARYDVLANWWAEV 349
Cdd:pfam02638 217 KAAKPNVTFSISPAGVWN--------------FAYNCFLADWRTWIEAGVIDEIAPQVYREkQAAFTAEYQVLAVWWSKQ 282

                         330       340
                  ....*....|....*....|....*..
gi 764952756  350 VKPTHTRLYIGVALYKVGEPSKNEPDW 376
Cdd:pfam02638 283 VIPTVVGILIGLANYKIPSPIKQDPQW 309
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
 130-248 4.69e-08

glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269892 [Multi-domain]  Cd Length: 299  Bit Score: 54.15  E-value: 4.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 130 LQFMLDEAHKRGMKVHAWFNPYRVSVNtkpstiAELNNT----LTQVPASVFVLHRNWirtasdrFVLDPGIPEARDWIT 205
Cdd:cd14791   67 LKALADRIHALGMKFGLWLEPEMVGPD------SELYREhpdwLLKDPGGPPVTGRNQ-------YVLDLSNPEVRDYLR 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 764952756 206 SIVAEVVQNYPIDGVQFD--DYFYTETAASPLNDNETFRRYGQGY 248
Cdd:cd14791  134 EVIDRLLREWGIDYLKWDfnRAGAEGGSRALDSQGEGLHRYVEAL 178
malS PRK09505
alpha-amylase; Reviewed
 79-144 2.21e-03

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 40.42  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGINtvffqvkpdgtALWRSDILP----WsdMLTGKIGEYP-----GYDPLQF---------------ML 134
Cdd:PRK09505 232 LTEKLDYLQQLGVN-----------ALWISSPLEqihgW--VGGGTKGDFPhyayhGYYTLDWtkldanmgteadlrtLV 298

                         90
                 ....*....|
gi 764952756 135 DEAHKRGMKV 144
Cdd:PRK09505 299 DEAHQRGIRI 308
 
Name Accession Description Interval E-value
YddW COG1649
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];
25-424 1.45e-141

Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];


Pssm-ID: 441255 [Multi-domain]  Cd Length: 451  Bit Score: 411.79  E-value: 1.45e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  25 LVTPPKSAAVKAGQTHREPVRGVWLTTVSrldwppvgsiiastpeSRITQQKLALIAKLDNLQRLGINTVFFQVKPDGTA 104
Cdd:COG1649   14 SLLGCSAPAPAAAPSPKREIRGVWLTTVD----------------LSVLKQKAELIEILDRLKELGFNAVFFQVRPAGDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 105 LWRSDILPWSDMLTGKIGEYPGYDPLQFMLDEAHKRGMKVHAWFNPYRVSVNTKPSTIAelnntltqvPASVFVLHRNWI 184
Cdd:COG1649   78 LYPSAIEPWSEYLTGTQGKDPGYDPLAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLA---------PSHIAKKHPEWL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 185 RTASD--RFVLDPGIPEARDWITSIVAEVVQNYPIDGVQFDDYFYTETAaspLNDNETFRRYGQGY-------ASKGDWR 255
Cdd:COG1649  149 TKYRDggKLWLNPGHPEVRDFILDLVLEVVTRYDVDGIHFDDYFYPSEF---GYDDATYALYGQETgfdnpkdLSWADWR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 256 RHNTQQLIAQVSATIKKLNPNVEFGVSPAGVWRNrshdpagSDTrGAAAYDESYADTRSWVQQGLLDYIAPQIYWPFARD 335
Cdd:COG1649  226 RDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRN-------SPT-GLFAYDDLYQDWRTWVKEGWVDYIVPQLYWPDGNS 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 336 AARYDVLANWWAEVVKPTHTRLYIGVALYKVgepsknepdwtvdgGVPELKKQLDLNESLPQIQGTILFRENNLNQPqtR 415
Cdd:COG1649  298 AADFEKLLDWWAQQAKGRKVPLYIGIGLYKV--------------PPEEILRQIQLNRDLPGVAGVVFFSYESLWNN--P 361


                 ....*....
gi 764952756 416 QAVNYLRSR 424
Cdd:COG1649  362 GLADALRQG 370
GHL10 pfam02638
Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins ...
 43-376 4.67e-123

Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.


Pssm-ID: 251441 [Multi-domain]  Cd Length: 311  Bit Score: 359.60  E-value: 4.67e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756   43 PVRGVWLTTVSRLDWPpvgsiiastpesrITQQKLALIAKLDNLQrlgINTVFFQVKPDGTALWRSDILPWSDMLTGKIG 122
Cdd:pfam02638   1 EIRGVWLTNVDSNDWP-------------DPVQLQEAIALLDDLN---FNTVYPQVWNDGHALYPSAVAPWSGLKTGEKG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  123 EYPGYDPLQFMLDEAHKRGMKVHAWFnpyRVSVNTKPstiaeLNNTLTQVPASVFVLHRNWIRT----ASDRFVLDPGIP 198
Cdd:pfam02638  65 GDPGYDPLAFMIDEAHKRNLRVHPWF---EFGFNAPA-----LSDLVKAHPAWLTTQHRDWTITseggTGPRVWLNPGHP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  199 EARDWITSIVAEVVQNYPIDGVQFDDYFY-TETAASPLNDNETFRRYGQGYA-------SKGDWRRHNTQQLIAQVSATI 270
Cdd:pfam02638 137 EVQDFITALVVDVVRRYDVDGVQFDDHFYyPYSFGYDPITVALYRQETKQEPfsnpeddLNTDWRRDKISQLVQQLNPTI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  271 KKLNPNVEFGVSPAGVWRnrshdpagsdtrgaAAYDESYADTRSWVQQGLLDYIAPQIYWP-FARDAARYDVLANWWAEV 349
Cdd:pfam02638 217 KAAKPNVTFSISPAGVWN--------------FAYNCFLADWRTWIEAGVIDEIAPQVYREkQAAFTAEYQVLAVWWSKQ 282

                         330       340
                  ....*....|....*....|....*..
gi 764952756  350 VKPTHTRLYIGVALYKVGEPSKNEPDW 376
Cdd:pfam02638 283 VIPTVVGILIGLANYKIPSPIKQDPQW 309
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
135-248 1.38e-08

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 54.98  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 135 DEAHKRGMKVHAWFNPYRVSVNtkpSTIA-ELNNTLTQVPASVFVLHRNWirtasdrFVLDPGIPEARDWITSIVAEVVQ 213
Cdd:COG3345  104 DRIHALGMKFGLWVEPEMVNPD---SDLYrEHPDWVLKDPDGEPVEGRNQ-------YVLDLSNPEVRDYLFEVLDRLLA 173

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 764952756 214 NYPIDGVQFD--DYFYTETAASPLNDNETFRRYGQGY 248
Cdd:COG3345  174 EWGIDYIKWDfnRDLTEAGSLPGERQGEGLHRYVLGL 210
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
 130-248 4.69e-08

glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269892 [Multi-domain]  Cd Length: 299  Bit Score: 54.15  E-value: 4.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 130 LQFMLDEAHKRGMKVHAWFNPYRVSVNtkpstiAELNNT----LTQVPASVFVLHRNWirtasdrFVLDPGIPEARDWIT 205
Cdd:cd14791   67 LKALADRIHALGMKFGLWLEPEMVGPD------SELYREhpdwLLKDPGGPPVTGRNQ-------YVLDLSNPEVRDYLR 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 764952756 206 SIVAEVVQNYPIDGVQFD--DYFYTETAASPLNDNETFRRYGQGY 248
Cdd:cd14791  134 EVIDRLLREWGIDYLKWDfnRAGAEGGSRALDSQGEGLHRYVEAL 178
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 78-324 7.44e-06

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200488 [Multi-domain]  Cd Length: 390  Bit Score: 47.65  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  78 ALIAKLDNLQRLGINTVFfqvkpdgtalwrsdILPwsdmltgkIGEYP-----GYDPLQFM---------------LDEA 137
Cdd:cd11350   34 GVIDKLDYLQDLGVNAIE--------------LMP--------VQEFPgndswGYNPRHYFaldkaygtpedlkrlVDEC 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 138 HKRGMKV-------HAwF--NP----YRVSVNTKPSTIAELNNTLTQVPASVFvlhrnwirtaSDrfvLDPGIPEARDWI 204
Cdd:cd11350   92 HQRGIAVildvvynHA-EgqSPlarlYWDYWYNPPPADPPWFNVWGPHFYYVG----------YD---FNHESPPTRDFV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 205 TSIVAEVVQNYPIDGVQFDdyfytetaASPlndNETFRRYGQGYASKGDWRRhntQQLIAQVSATIKKLNPNV-----EF 279
Cdd:cd11350  158 DDVNRYWLEEYHIDGFRFD--------LTK---GFTQKPTGGGAWGGYDAAR---IDFLKRYADEAKAVDKDFyviaeHL 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 764952756 280 GVSPA---------GVWRNRSHD---PAGSDTRGAAAYDESYADTRS--WVQQGLLDYI 324
Cdd:cd11350  224 PDNPEetelatygmSLWGNSNYSfsqAAMGYQGGSLLLDYSGDPYQNggWSPKNAVNYM 282
Melibiase pfam02065
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
 126-223 1.08e-05

Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.


Pssm-ID: 307952  Cd Length: 347  Bit Score: 47.39  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  126 GYDPLqfmLDEAHKRGMKVHAWFNPYRVSVNTKpstiaelnntltqvpasVFVLHRNWIRTASDR--------FVLDPGI 197
Cdd:pfam02065 105 GLDPL---AKQVHALGMQFGLWFEPEMVNPNSD-----------------LYRQHPDWVLHVPGRprtegrnqLVLDLSR 164

                          90       100
                  ....*....|....*....|....*.
gi 764952756  198 PEARDWITSIVAEVVQNYPIDGVQFD 223
Cdd:pfam02065 165 PDVVDYIIETLDNLLQEAPIDYVKWD 190
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
79-152 2.42e-05

Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 46.39  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGIntvffqvkpdgTALWrsdILPW--SDMltgkigEYPGYDP---------------LQFMLDEAHKRG 141
Cdd:COG0366   33 IIEKLDYLKDLGV-----------DAIW---LSPFfpSPM------SDHGYDIsdyrdvdprfgtladFDELVAEAHARG 92

                         90       100       110
                 ....*....|....*....|....*....|.
gi 764952756 142 MKV------------HAWF--------NPYR 152
Cdd:COG0366   93 IKVildlvlnhtsdeHPWFqearagpdSPYR 123
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
 80-152 6.01e-04

Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200472 [Multi-domain]  Cd Length: 428  Bit Score: 42.06  E-value: 6.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  80 IAKLDNLQRLGINtvffqvkpdgtALWRSDILPwS---DMltgkigeypGYD--------PlQF--------MLDEAHKR 140
Cdd:cd11333   28 ISKLDYLKDLGVD-----------AIWLSPIYP-SpqvDN---------GYDisdyraidP-EFgtmedfdeLIKEAHKR 85

                         90       100       110
                 ....*....|....*....|....*....|..
gi 764952756 141 GMKV------------HAWF--------NPYR 152
Cdd:cd11333   86 GIKIimdlvvnhtsdeHPWFqesrssrdNPYR 117
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
 133-253 6.35e-04

glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269878 [Multi-domain]  Cd Length: 364  Bit Score: 41.82  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756 133 MLDEAHKRGMKVHAWFNPYrvsVNTKPSTIAELnntltqVPASVFVLHRNWIRTASDRF------VLDPGIPEARDWITS 206
Cdd:cd06592   63 MIDKLHEMGFRVTLWVHPF---INPDSPNFREL------RDKGYLVKEDSGGPPLIVKWwngygaVLDFTNPEARDWFKE 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 764952756 207 IVAEVVQNYPIDGVQFD----DYF--YTETAASPLNDNETFRRYGQGYASKGD 253
Cdd:cd06592  134 RLRELQEDYGIDGFKFDageaSYLpaDPATFPSGLNPNEYTTLYAELAAEFGL 186
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 79-152 8.63e-04

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 41.41  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGINtvffqvkpdgtALWRSDILPWSDmltgkigeYPGYDPLQFM---------------LDEAHKRGMK 143
Cdd:cd11316   25 LTEKLDYLNDLGVN-----------GIWLMPIFPSPS--------YHGYDVTDYYaiepdygtmedferlIAEAHKRGIK 85

                         90       100
                 ....*....|....*....|....*....
gi 764952756 144 V------------HAWF--------NPYR 152
Cdd:cd11316   86 ViidlvinhtsseHPWFqeaasspdSPYR 114
malS PRK09505
alpha-amylase; Reviewed
 79-144 2.21e-03

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 40.42  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGINtvffqvkpdgtALWRSDILP----WsdMLTGKIGEYP-----GYDPLQF---------------ML 134
Cdd:PRK09505 232 LTEKLDYLQQLGVN-----------ALWISSPLEqihgW--VGGGTKGDFPhyayhGYYTLDWtkldanmgteadlrtLV 298

                         90
                 ....*....|
gi 764952756 135 DEAHKRGMKV 144
Cdd:PRK09505 299 DEAHQRGIRI 308
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 79-160 3.52e-03

Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 39.26  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756   79 LIAKLDNLQRLGIntvffqvkpdgTALWRSDIL--PWSDM------LTGKIGEYPGYDPLQFMLDEAHKRGMKV------ 144
Cdd:pfam00128   6 IIEKLDYLKELGV-----------TAIWLSPIFdsPQADHgydiadYYKIDPHYGTMEDFKELISKAHERGIKVildlvv 74

                          90       100
                  ....*....|....*....|..
gi 764952756  145 ------HAWFNPYRvSVNTKPS 160
Cdd:pfam00128  75 nhtsdeHAWFQESR-SSKDNPY 95
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 79-152 3.73e-03

Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200473 [Multi-domain]  Cd Length: 447  Bit Score: 39.47  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGIntvffqvkpdgTALWrsdILPWsdmltgkigeYP------GYD--------P-------LQFMLDEA 137
Cdd:cd11334   29 LTEKLDYLQWLGV-----------TAIW---LLPF----------YPsplrddGYDiadyygvdPrlgtlgdFVEFLREA 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 764952756 138 HKRGMKV------------HAWF--------NPYR 152
Cdd:cd11334   85 HERGIRViidlvvnhtsdqHPWFqaarrdpdSPYR 119
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 79-144 5.91e-03

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200489 [Multi-domain]  Cd Length: 443  Bit Score: 38.84  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGIntvffqvkpdgTALWRSDILpwsdMLTGKIGEYPGY--------DP-------LQFMLDEAHKRGMK 143
Cdd:cd11352   52 VRSKLGYLKRLGV-----------TALWLSPVF----KQRPELETYHGYgiqnfldvDPrfgtredLRDLVDAAHARGIY 116


                 .
gi 764952756 144 V 144
Cdd:cd11352  117 V 117
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 79-144 5.94e-03

Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 38.77  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952756  79 LIAKLDNLQRLGIntvffqvkpdgTALWRSDILPWSDMLTGKIGeYPGY--------DP-------LQFMLDEAHKRGMK 143
Cdd:cd11339   47 LIDKLDYIKDLGF-----------TAIWITPVVKNRSVQAGSAG-YHGYwgydfyriDPhlgtdadLQDLIDAAHARGIK 114


                 .
gi 764952756 144 V 144
Cdd:cd11339  115 V 115
 
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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