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Conserved domains on  [gi|398365967|ref|NP_009858|]
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alpha-glucosidase MAL32 [Saccharomyces cerevisiae S288C]

Protein Classification

alpha-glucosidase( domain architecture ID 10877748)

alpha-glucosidase catalyzes the hydrolysis of terminal, non-reducing, alpha-glucosidic linkages of oligosaccharides to produce alpha-glucose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
15-501 0e+00

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: 612.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  15 KEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELID 94
Cdd:cd11333    1 KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFGTMEDFDELIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  95 KTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKgydaegKPIPPNNWKSFFGGSAWTFDETTNEFYL 174
Cdd:cd11333   81 EAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGK------DGKPPNNWRSFFGGSAWEYDPETGQYYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 175 RLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSKLQHPNwgSHNGPRIHEYH 254
Cdd:cd11333  155 HLFAKEQPDLNWENPEVRQEIYD-MMRFWLDKGVDGFRLDVINLISKDPDFPDAPPGDGDGLSGHKY--YANGPGVHEYL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 255 QELHRfmknRVKDGREIMTVGEVAHGSDN--ALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNFL 332
Cdd:cd11333  232 QELNR----EVFSKYDIMTVGEAPGVDPEeaLKYVGPDRGELSMVFNFEHLDLDYGPGGKWKPKPWDLEELKKILSKWQK 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 333 FINGtDSWATTYIENHDQARSITRFADDSpKYRKISGKLLTLLECSLTGTLYVYQGQEIGQINfkewpiekyedvdvknn 412
Cdd:cd11333  308 ALQG-DGWNALFLENHDQPRSVSRFGNDG-EYRVESAKMLATLLLTLRGTPFIYQGEEIGMTN----------------- 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 413 yeiikksfgknskemkdffkgiallSRDHSRTPMPWTkDKPNAGFTgpDVKPWFFLNESFEQgINVEQESRDDDSVLNFW 492
Cdd:cd11333  369 -------------------------SRDNARTPMQWD-DSPNAGFS--TGKPWLPVNPNYKE-INVEAQLADPDSVLNFY 419

                 ....*....
gi 398365967 493 KRALQARKK 501
Cdd:cd11333  420 KKLIALRKE 428
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
511-583 6.76e-07

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


:

Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 47.16  E-value: 6.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365967  511 DFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSLPR-EGASLsfilgnyddTDVSSRVLKPWEGRIYLV 583
Cdd:pfam16657   2 DFRFLEPDNRKVLAYLREYEDETILVVANRSAQPVELDLSAfEGRVP---------VELFGGEPFPPIGGLYFL 66
 
Name Accession Description Interval E-value
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
15-501 0e+00

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: 612.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  15 KEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELID 94
Cdd:cd11333    1 KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFGTMEDFDELIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  95 KTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKgydaegKPIPPNNWKSFFGGSAWTFDETTNEFYL 174
Cdd:cd11333   81 EAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGK------DGKPPNNWRSFFGGSAWEYDPETGQYYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 175 RLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSKLQHPNwgSHNGPRIHEYH 254
Cdd:cd11333  155 HLFAKEQPDLNWENPEVRQEIYD-MMRFWLDKGVDGFRLDVINLISKDPDFPDAPPGDGDGLSGHKY--YANGPGVHEYL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 255 QELHRfmknRVKDGREIMTVGEVAHGSDN--ALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNFL 332
Cdd:cd11333  232 QELNR----EVFSKYDIMTVGEAPGVDPEeaLKYVGPDRGELSMVFNFEHLDLDYGPGGKWKPKPWDLEELKKILSKWQK 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 333 FINGtDSWATTYIENHDQARSITRFADDSpKYRKISGKLLTLLECSLTGTLYVYQGQEIGQINfkewpiekyedvdvknn 412
Cdd:cd11333  308 ALQG-DGWNALFLENHDQPRSVSRFGNDG-EYRVESAKMLATLLLTLRGTPFIYQGEEIGMTN----------------- 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 413 yeiikksfgknskemkdffkgiallSRDHSRTPMPWTkDKPNAGFTgpDVKPWFFLNESFEQgINVEQESRDDDSVLNFW 492
Cdd:cd11333  369 -------------------------SRDNARTPMQWD-DSPNAGFS--TGKPWLPVNPNYKE-INVEAQLADPDSVLNFY 419

                 ....*....
gi 398365967 493 KRALQARKK 501
Cdd:cd11333  420 KKLIALRKE 428
trehalose_treC TIGR02403
alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many ...
13-582 6.73e-174

alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.


Pssm-ID: 274115 [Multi-domain]  Cd Length: 543  Bit Score: 503.80  E-value: 6.73e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   13 WWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFEL 92
Cdd:TIGR02403   1 WWQKKVIYQIYPKSFYDSTGDGTGDLRGIIEKLDYLKKLGVDYIWLNPFYVSPQKDNGYDVSDYYAINPLFGTMADFEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   93 IDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKtNPKRDWFFWRPPKGYdaegkpiPPNNWKSFFGGSAWTFDETTNEF 172
Cdd:TIGR02403  81 VSEAKKRNIKIMLDMVFNHTSTEHEWFKKALAGD-SPYRDFYIWRDPKGK-------PPTNWQSKFGGSAWEYFGDTGQY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  173 YLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSKLQhpnwgshNGPRIHE 252
Cdd:TIGR02403 153 YLHLFDKTQADLNWENPEVREELKD-VVNFWRDKGVDGFRLDVINLISKDQFFEDDEIGDGRRFYT-------DGPRVHE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  253 YHQELHrfmkNRVKDGREIMTVGEVAHGS-DNA-LYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASN 330
Cdd:TIGR02403 225 YLQEMN----QEVFGDNDSVTVGEMSSTTiENCiRYSNPENKELSMVFTFHHLKVDYPNGEKWTLAKFDFAKLKEIFSTW 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  331 FLFINGTDSWATTYIENHDQARSITRFADDsPKYRKISGKLLTLLECSLTGTLYVYQGQEIGQINFKEWPIEKYEDVDVK 410
Cdd:TIGR02403 301 QTGMQAGGGWNALFWNNHDQPRAVSRFGDD-GEYRVESAKMLAAAIHLLRGTPYIYQGEEIGMTNPKFTNIEDYRDVESL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  411 NNYEIIKKSfGKNSKEMkdfFKGIALLSRDHSRTPMPWTkDKPNAGFTgpDVKPWFFLNESFEQgINVEQESRDDDSVLN 490
Cdd:TIGR02403 380 NAYDILLKK-GKSEEEA---LAILKQKSRDNSRTPMQWN-NEKNAGFT--TGKPWLGVATNYKE-INVEKALADDNSIFY 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  491 FWKRALQARKKYkELMIYGyDFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSLPREGASLSFILGNYDDTDVSS 570
Cdd:TIGR02403 452 FYQKLIALRKSE-PVITDG-DYQFLLPDDPSVWAYTRTYKNQKLLVINNFYGEEKTIELPLDLLSGKILLSNYEEAEKDA 529
                         570
                  ....*....|...
gi 398365967  571 RV-LKPWEGRIYL 582
Cdd:TIGR02403 530 KLeLKPYEAIVLL 542
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
36-397 1.41e-159

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: 459.13  E-value: 1.41e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   36 GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTE 115
Cdd:pfam00128   1 GDLQGIIEKLDYLKELGVTAIWLSPIFDSPQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  116 HEWFKESRSSKTNPKRDWFFWRPPkgydaeGKPIPPNNWKSFFGGSAWTFDETTNEFYLRLFASRQVDLNWENEDCRRAI 195
Cdd:pfam00128  81 HAWFQESRSSKDNPYRDYYFWRPG------GGPIPPNNWRSYFGGSAWTYDEKGQEYYLHLFVAGQPDLNWENPEVRNEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  196 FEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPdspifdktsklqhpnwGSHNGPRIHEYHQElhrfMKNRVKDGREIMTVG 275
Cdd:pfam00128 155 YD-VVRFWLDKGIDGFRIDVVKHISKVPGLP----------------FENNGPFWHEFTQA----MNETVFGYKDVMTVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  276 EVAHGSDN--ALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNFLFINGTDSWATTYIENHDQARS 353
Cdd:pfam00128 214 EVFHGDGEwaRVYTTEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDALPDTNGWNFTFLGNHDQPRF 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 398365967  354 ITRFADDSPKyrkisGKLLTLLECSLTGTLYVYQGQEIGQINFK 397
Cdd:pfam00128 294 LSRFGDDRAS-----AKLLAVFLLTLRGTPYIYQGEEIGMTGGN 332
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
9-499 6.73e-157

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 455.48  E-value: 6.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   9 TEPKWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNED 88
Cdd:COG0366    1 ADPDWWKDAVIYQIYPDSFADSNGDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSPMSDHGYDISDYRDVDPRFGTLAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  89 CFELIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKGydaegkPIPPNNWKSFFGGSAWTFDET 168
Cdd:COG0366   81 FDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGPDSPYRDWYVWRDGKP------DLPPNNWFSIFGGSAWTWDPE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 169 TNEFYLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDspifdktsklqhpnwgshNGP 248
Cdd:COG0366  155 DGQYYLHLFFSSQPDLNWENPEVREELLD-VLRFWLDRGVDGFRLDAVNHLDKDEGLPE------------------NLP 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 249 RIHEYHQELHRFMKNRvkdGREIMTVGEVAHGSDNALytsaARY----EVSEVFSFTHVELgtspfFRYNIVPFTLKQWK 324
Cdd:COG0366  216 EVHEFLRELRAAVDEY---YPDFFLVGEAWVDPPEDV----ARYfggdELDMAFNFPLMPA-----LWDALAPEDAAELR 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 325 EAIAsNFLFINGTDSWATTYIENHDQARSITRFADDspkYRKISGKLLTLLECSLTGTLYVYQGQEIGQINFkewpieKY 404
Cdd:COG0366  284 DALA-QTPALYPEGGWWANFLRNHDQPRLASRLGGD---YDRRRAKLAAALLLTLPGTPYIYYGDEIGMTGD------KL 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 405 EDVDvknnyeiikksfgknskemkdffkgiallSRDHSRTPMPWTKDkPNAGFTgpdvKPWFFLNESFeQGINVEQESRD 484
Cdd:COG0366  354 QDPE-----------------------------GRDGCRTPMPWSDD-RNAGFS----TGWLPVPPNY-KAINVEAQEAD 398
                        490
                 ....*....|....*
gi 398365967 485 DDSVLNFWKRALQAR 499
Cdd:COG0366  399 PDSLLNFYRKLIALR 413
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
9-582 1.54e-129

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 390.65  E-value: 1.54e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   9 TEPKWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNED 88
Cdd:PRK10933   3 NLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYVSPQVDNGYDVANYTAIDPTYGTLDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  89 CFELIDKTHKLGMKFITDLVINHCSTEHEWFKESRsSKTNPKRDWFFWRppkgydaEGKP-IPPNNWKSFFGGSAWTFDE 167
Cdd:PRK10933  83 FDELVAQAKSRGIRIILDMVFNHTSTQHAWFREAL-NKESPYRQFYIWR-------DGEPeTPPNNWRSKFGGSAWRWHA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 168 TTNEFYLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDktsklqhpnwGSH-- 245
Cdd:PRK10933 155 ESEQYYLHLFAPEQADLNWENPAVRAELKK-VCEFWADRGVDGLRLDVVNLISKDQDFPDDLDGD----------GRRfy 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 246 -NGPRIHEYHQELHRfmknRVKDGREIMTVGEVahgSDNAL-----YTSAARYEVSEVFSFTHVELGTSPFFRYNIVP-- 317
Cdd:PRK10933 224 tDGPRAHEFLQEMNR----DVFTPRGLMTVGEM---SSTSLehcqrYAALTGSELSMTFNFHHLKVDYPNGEKWTLAKpd 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 318 -FTLKQ----WKEAI---ASNFLFingtdsWAttyieNHDQARSITRFADDSpKYRKISGKLLTLLECSLTGTLYVYQGQ 389
Cdd:PRK10933 297 fVALKTlfrhWQQGMhnvAWNALF------WC-----NHDQPRIVSRFGDEG-EYRVPAAKMLAMVLHGMQGTPYIYQGE 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 390 EIGQINFKEWPIEKYEDVDVKNNYEIIKKSfGKNSKEMkdfFKGIALLSRDHSRTPMPWtKDKPNAGFTgpDVKPWFFLN 469
Cdd:PRK10933 365 EIGMTNPHFTRITDYRDVESLNMFAELRND-GRDADEL---LAILASKSRDNSRTPMQW-DNGDNAGFT--QGEPWIGLC 437
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 470 ESFEQgINVEQESRDDDSVLNFWKRALQARKKYkELMIYGyDFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSL 549
Cdd:PRK10933 438 DNYQE-INVEAALADEDSVFYTYQKLIALRKQE-PVLTWG-DYQDLLPNHPSLWCYRREWQGQTLLVIANLSREPQPWQP 514
                        570       580       590
                 ....*....|....*....|....*....|....*
gi 398365967 550 PREGASLSFILGNYDDTDV--SSRVLKPWEGRIYL 582
Cdd:PRK10933 515 GQMRGNWQLLMHNYEEASPqpCAMTLRPFEAVWWL 549
Aamy smart00642
Alpha-amylase domain;
21-113 2.81e-40

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 144.01  E-value: 2.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967    21 QIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQ---DMGYDISNYEKVWPTYGTNEDCFELIDKTH 97
Cdd:smart00642   1 QIYPDRFADGNGDGGGDLQGIIEKLDYLKDLGVTAIWLSPIFESPQGypsYHGYDISDYKQIDPRFGTMEDFKELVDAAH 80
                           90
                   ....*....|....*.
gi 398365967    98 KLGMKFITDLVINHCS 113
Cdd:smart00642  81 ARGIKVILDVVINHTS 96
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
511-583 6.76e-07

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 47.16  E-value: 6.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365967  511 DFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSLPR-EGASLsfilgnyddTDVSSRVLKPWEGRIYLV 583
Cdd:pfam16657   2 DFRFLEPDNRKVLAYLREYEDETILVVANRSAQPVELDLSAfEGRVP---------VELFGGEPFPPIGGLYFL 66
 
Name Accession Description Interval E-value
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
15-501 0e+00

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: 612.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  15 KEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELID 94
Cdd:cd11333    1 KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFGTMEDFDELIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  95 KTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKgydaegKPIPPNNWKSFFGGSAWTFDETTNEFYL 174
Cdd:cd11333   81 EAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGK------DGKPPNNWRSFFGGSAWEYDPETGQYYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 175 RLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSKLQHPNwgSHNGPRIHEYH 254
Cdd:cd11333  155 HLFAKEQPDLNWENPEVRQEIYD-MMRFWLDKGVDGFRLDVINLISKDPDFPDAPPGDGDGLSGHKY--YANGPGVHEYL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 255 QELHRfmknRVKDGREIMTVGEVAHGSDN--ALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNFL 332
Cdd:cd11333  232 QELNR----EVFSKYDIMTVGEAPGVDPEeaLKYVGPDRGELSMVFNFEHLDLDYGPGGKWKPKPWDLEELKKILSKWQK 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 333 FINGtDSWATTYIENHDQARSITRFADDSpKYRKISGKLLTLLECSLTGTLYVYQGQEIGQINfkewpiekyedvdvknn 412
Cdd:cd11333  308 ALQG-DGWNALFLENHDQPRSVSRFGNDG-EYRVESAKMLATLLLTLRGTPFIYQGEEIGMTN----------------- 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 413 yeiikksfgknskemkdffkgiallSRDHSRTPMPWTkDKPNAGFTgpDVKPWFFLNESFEQgINVEQESRDDDSVLNFW 492
Cdd:cd11333  369 -------------------------SRDNARTPMQWD-DSPNAGFS--TGKPWLPVNPNYKE-INVEAQLADPDSVLNFY 419

                 ....*....
gi 398365967 493 KRALQARKK 501
Cdd:cd11333  420 KKLIALRKE 428
trehalose_treC TIGR02403
alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many ...
13-582 6.73e-174

alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.


Pssm-ID: 274115 [Multi-domain]  Cd Length: 543  Bit Score: 503.80  E-value: 6.73e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   13 WWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFEL 92
Cdd:TIGR02403   1 WWQKKVIYQIYPKSFYDSTGDGTGDLRGIIEKLDYLKKLGVDYIWLNPFYVSPQKDNGYDVSDYYAINPLFGTMADFEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   93 IDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKtNPKRDWFFWRPPKGYdaegkpiPPNNWKSFFGGSAWTFDETTNEF 172
Cdd:TIGR02403  81 VSEAKKRNIKIMLDMVFNHTSTEHEWFKKALAGD-SPYRDFYIWRDPKGK-------PPTNWQSKFGGSAWEYFGDTGQY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  173 YLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSKLQhpnwgshNGPRIHE 252
Cdd:TIGR02403 153 YLHLFDKTQADLNWENPEVREELKD-VVNFWRDKGVDGFRLDVINLISKDQFFEDDEIGDGRRFYT-------DGPRVHE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  253 YHQELHrfmkNRVKDGREIMTVGEVAHGS-DNA-LYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASN 330
Cdd:TIGR02403 225 YLQEMN----QEVFGDNDSVTVGEMSSTTiENCiRYSNPENKELSMVFTFHHLKVDYPNGEKWTLAKFDFAKLKEIFSTW 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  331 FLFINGTDSWATTYIENHDQARSITRFADDsPKYRKISGKLLTLLECSLTGTLYVYQGQEIGQINFKEWPIEKYEDVDVK 410
Cdd:TIGR02403 301 QTGMQAGGGWNALFWNNHDQPRAVSRFGDD-GEYRVESAKMLAAAIHLLRGTPYIYQGEEIGMTNPKFTNIEDYRDVESL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  411 NNYEIIKKSfGKNSKEMkdfFKGIALLSRDHSRTPMPWTkDKPNAGFTgpDVKPWFFLNESFEQgINVEQESRDDDSVLN 490
Cdd:TIGR02403 380 NAYDILLKK-GKSEEEA---LAILKQKSRDNSRTPMQWN-NEKNAGFT--TGKPWLGVATNYKE-INVEKALADDNSIFY 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  491 FWKRALQARKKYkELMIYGyDFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSLPREGASLSFILGNYDDTDVSS 570
Cdd:TIGR02403 452 FYQKLIALRKSE-PVITDG-DYQFLLPDDPSVWAYTRTYKNQKLLVINNFYGEEKTIELPLDLLSGKILLSNYEEAEKDA 529
                         570
                  ....*....|...
gi 398365967  571 RV-LKPWEGRIYL 582
Cdd:TIGR02403 530 KLeLKPYEAIVLL 542
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
36-397 1.41e-159

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: 459.13  E-value: 1.41e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   36 GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTE 115
Cdd:pfam00128   1 GDLQGIIEKLDYLKELGVTAIWLSPIFDSPQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  116 HEWFKESRSSKTNPKRDWFFWRPPkgydaeGKPIPPNNWKSFFGGSAWTFDETTNEFYLRLFASRQVDLNWENEDCRRAI 195
Cdd:pfam00128  81 HAWFQESRSSKDNPYRDYYFWRPG------GGPIPPNNWRSYFGGSAWTYDEKGQEYYLHLFVAGQPDLNWENPEVRNEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  196 FEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPdspifdktsklqhpnwGSHNGPRIHEYHQElhrfMKNRVKDGREIMTVG 275
Cdd:pfam00128 155 YD-VVRFWLDKGIDGFRIDVVKHISKVPGLP----------------FENNGPFWHEFTQA----MNETVFGYKDVMTVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  276 EVAHGSDN--ALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNFLFINGTDSWATTYIENHDQARS 353
Cdd:pfam00128 214 EVFHGDGEwaRVYTTEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDALPDTNGWNFTFLGNHDQPRF 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 398365967  354 ITRFADDSPKyrkisGKLLTLLECSLTGTLYVYQGQEIGQINFK 397
Cdd:pfam00128 294 LSRFGDDRAS-----AKLLAVFLLTLRGTPYIYQGEEIGMTGGN 332
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
9-499 6.73e-157

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 455.48  E-value: 6.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   9 TEPKWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNED 88
Cdd:COG0366    1 ADPDWWKDAVIYQIYPDSFADSNGDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSPMSDHGYDISDYRDVDPRFGTLAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  89 CFELIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKGydaegkPIPPNNWKSFFGGSAWTFDET 168
Cdd:COG0366   81 FDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGPDSPYRDWYVWRDGKP------DLPPNNWFSIFGGSAWTWDPE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 169 TNEFYLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDspifdktsklqhpnwgshNGP 248
Cdd:COG0366  155 DGQYYLHLFFSSQPDLNWENPEVREELLD-VLRFWLDRGVDGFRLDAVNHLDKDEGLPE------------------NLP 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 249 RIHEYHQELHRFMKNRvkdGREIMTVGEVAHGSDNALytsaARY----EVSEVFSFTHVELgtspfFRYNIVPFTLKQWK 324
Cdd:COG0366  216 EVHEFLRELRAAVDEY---YPDFFLVGEAWVDPPEDV----ARYfggdELDMAFNFPLMPA-----LWDALAPEDAAELR 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 325 EAIAsNFLFINGTDSWATTYIENHDQARSITRFADDspkYRKISGKLLTLLECSLTGTLYVYQGQEIGQINFkewpieKY 404
Cdd:COG0366  284 DALA-QTPALYPEGGWWANFLRNHDQPRLASRLGGD---YDRRRAKLAAALLLTLPGTPYIYYGDEIGMTGD------KL 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 405 EDVDvknnyeiikksfgknskemkdffkgiallSRDHSRTPMPWTKDkPNAGFTgpdvKPWFFLNESFeQGINVEQESRD 484
Cdd:COG0366  354 QDPE-----------------------------GRDGCRTPMPWSDD-RNAGFS----TGWLPVPPNY-KAINVEAQEAD 398
                        490
                 ....*....|....*
gi 398365967 485 DDSVLNFWKRALQAR 499
Cdd:COG0366  399 PDSLLNFYRKLIALR 413
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
12-520 2.56e-144

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, 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. 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: 200469 [Multi-domain]  Cd Length: 472  Bit Score: 425.52  E-value: 2.56e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  12 KWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFE 91
Cdd:cd11330    1 PWWRGAVIYQIYPRSFLDSNGDGIGDLPGITEKLDYIASLGVDAIWLSPFFKSPMKDFGYDVSDYCAVDPLFGTLDDFDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  92 LIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKgydAEGKpiPPNNWKSFFGGSAWTFDETTNE 171
Cdd:cd11330   81 LVARAHALGLKVMIDQVLSHTSDQHPWFEESRQSRDNPKADWYVWADPK---PDGS--PPNNWLSVFGGSAWQWDPRRGQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 172 FYLRLFASRQVDLNWENEDCRRAIFESaVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIfdktsklQHPNWGSHNGPRIH 251
Cdd:cd11330  156 YYLHNFLPSQPDLNFHNPEVQDALLDV-ARFWLDRGVDGFRLDAVNFYMHDPALRDNPP-------RPPDEREDGVAPTN 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 252 EYHQELHRFMKNR-------------VKDGREIMTVGEVahGSDNALYTSAAryevsevfsFTHVE--LGTSPFFRYNIV 316
Cdd:cd11330  228 PYGMQLHIHDKSQpenlaflerlralLDEYPGRFLVGEV--SDDDPLEVMAE---------YTSGGdrLHMAYSFDLLGR 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 317 PFTLKQWKEAIASnfLFINGTDSWATTYIENHDQARSITRFADdsPKYRKISGKLLTLLECSLTGTLYVYQGQEIGQinf 396
Cdd:cd11330  297 PFSAAVVRDALEA--FEAEAPDGWPCWAFSNHDVPRAVSRWAG--GADDPALARLLLALLLSLRGSVCLYQGEELGL--- 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 397 kewpiekyEDVDVknNYEIIKKSFGKNskeMKDFFKGiallsRDHSRTPMPWTKDKPNAGFTgpDVKPWFFLNESFEQGi 476
Cdd:cd11330  370 --------PEAEL--PFEELQDPYGIT---FWPEFKG-----RDGCRTPMPWQADAPHAGFS--TAKPWLPVPPEHLAL- 428
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 398365967 477 NVEQESRDDDSVLNFWKRALQARKKYKELMiYGyDFQFIDLDSD 520
Cdd:cd11330  429 AVDVQEKDPGSVLNFYRRFLAWRKAQPALR-TG-TITFLDAPEP 470
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
9-582 1.54e-129

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 390.65  E-value: 1.54e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   9 TEPKWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNED 88
Cdd:PRK10933   3 NLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYVSPQVDNGYDVANYTAIDPTYGTLDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  89 CFELIDKTHKLGMKFITDLVINHCSTEHEWFKESRsSKTNPKRDWFFWRppkgydaEGKP-IPPNNWKSFFGGSAWTFDE 167
Cdd:PRK10933  83 FDELVAQAKSRGIRIILDMVFNHTSTQHAWFREAL-NKESPYRQFYIWR-------DGEPeTPPNNWRSKFGGSAWRWHA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 168 TTNEFYLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDktsklqhpnwGSH-- 245
Cdd:PRK10933 155 ESEQYYLHLFAPEQADLNWENPAVRAELKK-VCEFWADRGVDGLRLDVVNLISKDQDFPDDLDGD----------GRRfy 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 246 -NGPRIHEYHQELHRfmknRVKDGREIMTVGEVahgSDNAL-----YTSAARYEVSEVFSFTHVELGTSPFFRYNIVP-- 317
Cdd:PRK10933 224 tDGPRAHEFLQEMNR----DVFTPRGLMTVGEM---SSTSLehcqrYAALTGSELSMTFNFHHLKVDYPNGEKWTLAKpd 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 318 -FTLKQ----WKEAI---ASNFLFingtdsWAttyieNHDQARSITRFADDSpKYRKISGKLLTLLECSLTGTLYVYQGQ 389
Cdd:PRK10933 297 fVALKTlfrhWQQGMhnvAWNALF------WC-----NHDQPRIVSRFGDEG-EYRVPAAKMLAMVLHGMQGTPYIYQGE 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 390 EIGQINFKEWPIEKYEDVDVKNNYEIIKKSfGKNSKEMkdfFKGIALLSRDHSRTPMPWtKDKPNAGFTgpDVKPWFFLN 469
Cdd:PRK10933 365 EIGMTNPHFTRITDYRDVESLNMFAELRND-GRDADEL---LAILASKSRDNSRTPMQW-DNGDNAGFT--QGEPWIGLC 437
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 470 ESFEQgINVEQESRDDDSVLNFWKRALQARKKYkELMIYGyDFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSL 549
Cdd:PRK10933 438 DNYQE-INVEAALADEDSVFYTYQKLIALRKQE-PVLTWG-DYQDLLPNHPSLWCYRREWQGQTLLVIANLSREPQPWQP 514
                        570       580       590
                 ....*....|....*....|....*....|....*
gi 398365967 550 PREGASLSFILGNYDDTDV--SSRVLKPWEGRIYL 582
Cdd:PRK10933 515 GQMRGNWQLLMHNYEEASPqpCAMTLRPFEAVWWL 549
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
12-505 3.85e-129

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, 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. 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: 200470 [Multi-domain]  Cd Length: 450  Bit Score: 385.91  E-value: 3.85e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  12 KWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFE 91
Cdd:cd11331    1 LWWQTGVIYQIYPRSFQDSNGDGVGDLRGIISRLDYLSDLGVDAVWLSPIYPSPMADFGYDVSDYCGIDPLFGTLEDFDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  92 LIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKgydAEGKpiPPNNWKSFFGGSAWTFDETTNE 171
Cdd:cd11331   81 LVAEAHARGLKVILDFVPNHTSDQHPWFLESRSSRDNPKRDWYIWRDPA---PDGG--PPNNWRSEFGGSAWTWDERTGQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 172 FYLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIfdktsklqHPNWGSHNGPR-- 249
Cdd:cd11331  156 YYLHAFLPEQPDLNWRNPEVRAAMHD-VLRFWLDRGVDGFRVDVLWLLIKDPQFRDNPP--------NPDWRGGMPPHer 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 250 ---IHEYHQ-ELHRFMKN--RVKDG-REIMTVGEVAHGSDNAL-YTSAARYEVSEVFSFTHVELG-TSPFFRYNIVPFtl 320
Cdd:cd11331  227 llhIYTADQpETHEIVREmrRVVDEfGDRVLIGEIYLPLDRLVaYYGAGRDGLHLPFNFHLISLPwDAAALARAIEEY-- 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 321 kqwkEAIASNFlfingtdSWATTYIENHDQARSITRFadDSPKYRKISGKLLTllecsLTGTLYVYQGQEIGQINfKEWP 400
Cdd:cd11331  305 ----EAALPAG-------AWPNWVLGNHDQPRIASRV--GPAQARVAAMLLLT-----LRGTPTLYYGDELGMED-VPIP 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 401 IEKYEDVDVKNNYEiikksfgknskemkdffkgiALLSRDHSRTPMPWTkDKPNAGFTGPDvkPWFFLNESFEQgINVEQ 480
Cdd:cd11331  366 PERVQDPAELNQPG--------------------GGLGRDPERTPMPWD-ASPNAGFSAAD--PWLPLSPDARQ-RNVAT 421
                        490       500
                 ....*....|....*....|....*
gi 398365967 481 ESRDDDSVLNFWKRALQARKKYKEL 505
Cdd:cd11331  422 QEADPGSMLSLYRRLLALRRAHPAL 446
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-500 2.79e-127

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins; 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. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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: 200471 [Multi-domain]  Cd Length: 481  Bit Score: 382.39  E-value: 2.79e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  13 WWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFEL 92
Cdd:cd11332    2 WWRDAVVYQVYPRSFADANGDGIGDLAGIRARLPYLAALGVDAIWLSPFYPSPMADGGYDVADYRDVDPLFGTLADFDAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  93 IDKTHKLGMKFITDLVINHCSTEHEWFKESRSS-KTNPKRDWFFWRPPKGYDAEgkpIPPNNWKSFFGGSAWT----FDE 167
Cdd:cd11332   82 VAAAHELGLRVIVDIVPNHTSDQHPWFQAALAAgPGSPERARYIFRDGRGPDGE---LPPNNWQSVFGGPAWTrvtePDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 168 TTNEFYLRLFASRQVDLNWENEDCRRAiFESAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSP---IFDKTSKLQHPNWgs 244
Cdd:cd11332  159 TDGQWYLHLFAPEQPDLNWDNPEVRAE-FEDVLRFWLDRGVDGFRIDVAHGLAKDPGLPDAPgggLPVGERPGSHPYW-- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 245 hNGPRIHEYHQELHRFMKNRvkdGREIMTVGE--VAHGSDNALYtsaARYEvsevfsfthvELGTSPFFRYNIVPFTLKQ 322
Cdd:cd11332  236 -DRDEVHDIYREWRAVLDEY---DPPRVLVAEawVPDPERLARY---LRPD----------ELHQAFNFDFLKAPWDAAA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 323 WKEAIASNFLFINGTDSWATTYIENHDQARSITRFADDSPKYRKISGKLL----------------TLLECSLTGTLYVY 386
Cdd:cd11332  299 LRRAIDRSLAAAAAVGAPPTWVLSNHDVVRHVSRYGLPTPGPDPSGIDGTdeppdlalglrraraaALLMLALPGSAYLY 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 387 QGQEIGQINFKEWPIEKYEDvdvknnyEIIKKSFGKnskemkdfFKGiallsRDHSRTPMPWTKDKPNAGFTGPDVKPWF 466
Cdd:cd11332  379 QGEELGLPEVEDLPDALRQD-------PIWERSGGT--------ERG-----RDGCRVPLPWSGDAPPFGFSPGGAEPWL 438
                        490       500       510
                 ....*....|....*....|....*....|....
gi 398365967 467 FLNESFEQgINVEQESRDDDSVLNFWKRALQARK 500
Cdd:cd11332  439 PQPAWWAR-YAVDAQEADPGSTLSLYRRALRLRR 471
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
10-500 2.00e-115

Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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: 200467 [Multi-domain]  Cd Length: 470  Bit Score: 351.53  E-value: 2.00e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  10 EPKWWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDC 89
Cdd:cd11328    1 DKDWWENAVFYQIYPRSFKDSDGDGIGDLKGITEKLDYFKDIGIDAIWLSPIFKSPMVDFGYDISDFTDIDPIFGTMEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  90 FELIDKTHKLGMKFITDLVINHCSTEHEWFKESrSSKTNPKRDWFFWRPPKGyDAEGKPIPPNNWKSFFGGSAWTFDETT 169
Cdd:cd11328   81 EELIAEAKKLGLKVILDFVPNHSSDEHEWFQKS-VKRDEPYKDYYVWHDGKN-NDNGTRVPPNNWLSVFGGSAWTWNEER 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 170 NEFYLRLFASRQVDLNWENEDCRRAIFESaVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSK-------LQHPNw 242
Cdd:cd11328  159 QQYYLHQFAVKQPDLNYRNPKVVEEMKNV-LRFWLDKGVDGFRIDAVPHLFEDEDFLDEPYSDEPGAdpddydyLDHIY- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 243 gSHNGPR----IHEYHQELHRFMKNRVKDGREIMTvgEVAHGSDN--ALYTSAARYEVSEVFSF---THVELGTSP-FFR 312
Cdd:cd11328  237 -TKDQPEtydlVYEWREVLDEYAKENNGDTRVMMT--EAYSSLDNtmKYYGNETTYGAHFPFNFeliTNLNKNSNAtDFK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 313 YNIvpftlKQWKEAIASNflfingtdSWATTYIENHDQARSITRFADDspkyrkiSGKLLTLLECSLTGTLYVYQGQEIG 392
Cdd:cd11328  314 DLI-----DKWLDNMPEG--------QTANWVLGNHDNPRVASRFGEE-------RVDGMNMLSMLLPGVAVTYYGEEIG 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 393 QinfkewpiekyedVDVKNNYEIIKKSFGKNSKEMKDffkgiALLSRDHSRTPMPWTkDKPNAGFTGPDvKPWFFLNESF 472
Cdd:cd11328  374 M-------------EDTTISWEDTVDPPACNAGPENY-----EAYSRDPARTPFQWD-DSKNAGFSTAN-KTWLPVNPNY 433
                        490       500
                 ....*....|....*....|....*...
gi 398365967 473 EQgINVEQESRDDDSVLNFWKRALQARK 500
Cdd:cd11328  434 KT-LNLEAQKKDPRSHYNIYKKLAQLRK 460
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
13-510 1.40e-102

Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. 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: 200494 [Multi-domain]  Cd Length: 456  Bit Score: 317.76  E-value: 1.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  13 WWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFEL 92
Cdd:cd11359    2 WWQTSVIYQIYPRSFKDSNGDGNGDLKGIREKLDYLKYLGVKTVWLSPIYKSPMKDFGYDVSDFTDIDPMFGTMEDFERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  93 IDKTHKLGMKFITDLVINHCSTEHEWFKESRSSkTNPKRDWFFWRPPKgydAEGKPIPPNNWKSFFGGSAWTFDETTNEF 172
Cdd:cd11359   82 LAAMHDRGMKLIMDFVPNHTSDKHEWFQLSRNS-TNPYTDYYIWADCT---ADGPGTPPNNWVSVFGNSAWEYDEKRNQC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 173 YLRLFASRQVDLNWENEDCRRAIfESAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKT---------SKLQHPNwg 243
Cdd:cd11359  158 YLHQFLKEQPDLNFRNPDVQQEM-DDVLRFWLDKGVDGFRVDAVKHLLEATHLRDEPQVNPTqppetqynySELYHDY-- 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 244 SHNGPRIHEYHQELHRFM-KNRVKDGREIMTVGEVAHGSDNALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQ 322
Cdd:cd11359  235 TTNQEGVHDIIRDWRQTMdKYSSEPGRYRFMITEVYDDIDTTMRYYGTSFKQEADFPFNFYLLDLGANLSGNSINELVES 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 323 WKEAIASNflfingtdSWATTYIENHDQARSITRFAddsPKYRKIsgklLTLLECSLTGTLYVYQGQEIGQinfkewpie 402
Cdd:cd11359  315 WMSNMPEG--------KWPNWVLGNHDNSRIASRLG---PQYVRA----MNMLLLTLPGTPTTYYGEEIGM--------- 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 403 kyEDVDVKNNyeiikksfgknskEMKDFFKGIallSRDHSRTPMPWTkDKPNAGFTGPDvKPWFFLNESFEQgINVEQES 482
Cdd:cd11359  371 --EDVDISVD-------------KEKDPYTFE---SRDPERTPMQWN-NSNNAGFSDAN-KTWLPVNSDYKT-VNVEVQK 429
                        490       500
                 ....*....|....*....|....*...
gi 398365967 483 RDDDSVLNFWKRALQARKkyKELMIYGY 510
Cdd:cd11359  430 TDPTSMLNLYRELLLLRS--SELALHRG 455
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
13-499 1.60e-89

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: 283.69  E-value: 1.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  13 WWKEATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFEL 92
Cdd:cd11334    1 WYKNAVIYQLDVRTFMDSNGDGIGDFRGLTEKLDYLQWLGVTAIWLLPFYPSPLRDDGYDIADYYGVDPRLGTLGDFVEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  93 IDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPIPPNnwksfFGGSAWTFDETTNEF 172
Cdd:cd11334   81 LREAHERGIRVIIDLVVNHTSDQHPWFQAARRDPDSPYRDYYVWSDTPPKYKDARIIFPD-----VEKSNWTWDEVAGAY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 173 YLRLFASRQVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSpifdktsklqhpnwgshNGPRIHE 252
Cdd:cd11334  156 YWHRFYSHQPDLNFDNPAVREEILR-IMDFWLDLGVDGFRLDAVPYLIEREGTNCE-----------------NLPETHD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 253 YHQELHRFMKNRvkdGREIMTVGEVahgsdNALYTSAARY-----EVSEVFSF---THVELG-----TSPFFRynivpfT 319
Cdd:cd11334  218 FLKRLRAFVDRR---YPDAILLAEA-----NQWPEEVREYfgdgdELHMAFNFplnPRLFLAlaredAFPIID------A 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 320 LKQWKEaiasnflfINGTDSWAtTYIENHDQ-----------ARSITRFADDsPK-------------------YRKIsg 369
Cdd:cd11334  284 LRQTPP--------IPEGCQWA-NFLRNHDEltlemltdeerDYVYAAFAPD-PRmriynrgirrrlapmlggdRRRI-- 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 370 KLLTLLECSLTGTLYVYQGQEIGqinfkewpiekyedvdvknnyeiikksfgknskeMKDffkGIALLSRDHSRTPMPWT 449
Cdd:cd11334  352 ELAYSLLFSLPGTPVIYYGDEIG----------------------------------MGD---NLYLPDRDGVRTPMQWS 394
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 398365967 450 KDkPNAGFTGPDvKPWFFL------NESFEQgINVEQESRDDDSVLNFWKRALQAR 499
Cdd:cd11334  395 AD-RNGGFSTAD-PQKLYLpviddgPYGYER-VNVEAQRRDPSSLLNWVRRLIALR 447
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
17-507 4.83e-86

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: 272.92  E-value: 4.83e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  17 ATIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQqDMGYDISNYEKVWPTYGTNEDCFELIDKT 96
Cdd:cd11316    1 GVFYEIFVRSFYDSDGDGIGDLNGLTEKLDYLNDLGVNGIWLMPIFPSPS-YHGYDVTDYYAIEPDYGTMEDFERLIAEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  97 HKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKgydaegkpippNNWKSFFGGSAWTFDEtTNEFYLRL 176
Cdd:cd11316   80 HKRGIKVIIDLVINHTSSEHPWFQEAASSPDSPYRDYYIWADDD-----------PGGWSSWGGNVWHKAG-DGGYYYGA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 177 FASRQVDLNWENEDCRRAIfESAVGFWLDHGVDGFRIDTAG-LYSKRPGLPDSPifdKTsklqhpnwgshngpriHEYHQ 255
Cdd:cd11316  148 FWSGMPDLNLDNPAVREEI-KKIAKFWLDKGVDGFRLDAAKhIYENGEGQADQE---EN----------------IEFWK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 256 ELHRFMKnRVKDGReiMTVGEV-AHGSDNALYtsaARYEVSEVFSF---THVELGTSPFFRYNIVPFTLKQWKEAIASnf 331
Cdd:cd11316  208 EFRDYVK-SVKPDA--YLVGEVwDDPSTIAPY---YASGLDSAFNFdlaEAIIDSVKNGGSGAGLAKALLRVYELYAK-- 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 332 lfINGTDSWAtTYIENHDQARSITRFADDSPKYRKISGKLLTllecsLTGTLYVYQGQEIGQInfkewpiekyedvdvkn 411
Cdd:cd11316  280 --YNPDYIDA-PFLSNHDQDRVASQLGGDEAKAKLAAALLLT-----LPGNPFIYYGEEIGML----------------- 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 412 nyeiikksfGKNSKEMKdffkgiallsrdhsRTPMPWTKDkPNAGFTgpDVKPWFFLNESfeQGINVEQESRDDDSVLNF 491
Cdd:cd11316  335 ---------GSKPDENI--------------RTPMSWDAD-SGAGFT--TWIPPRPNTNA--TTASVEAQEADPDSLLNH 386
                        490
                 ....*....|....*.
gi 398365967 492 WKRALQARKKYKELMI 507
Cdd:cd11316  387 YKRLIALRNEYPALAR 402
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
18-494 9.24e-56

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 catalytic triad (DED) is not present here. 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: 200486 [Multi-domain]  Cd Length: 429  Bit Score: 194.06  E-value: 9.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  18 TIYQIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELIDKTH 97
Cdd:cd11348    1 VFYEIYPQSFYDSNGDGIGDLQGIISKLDYIKSLGCNAIWLNPCFDSPFKDAGYDVRDYYKVAPRYGTNEDLVRLFDEAH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  98 KLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPippnnwksFFGGSAwtfdeTTNEFYLRLF 177
Cdd:cd11348   81 KRGIHVLLDLVPGHTSDEHPWFKESKKAENNEYSDRYIWTDSIWSGGPGLP--------FVGGEA-----ERNGNYIVNF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 178 ASRQVDLN----------WENE----DCR--RAIFESAVGFWLDHGVDGFRIDTAGLYSKrpglpDSPIFDKTSKLqhpn 241
Cdd:cd11348  148 FSCQPALNygfahpptepWQQPvdapGPQatREAMKDIMRFWLDKGADGFRVDMADSLVK-----NDPGNKETIKL---- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 242 WgshngpriheyhQELHRFMKNRVKDGREIMTVGE----VAHGSDNALYTSAARYEVSEVFSFTHVELGTSPFFRY---- 313
Cdd:cd11348  219 W------------QEIRAWLDEEYPEAVLVSEWGNpeqsLKAGFDMDFLLHFGGNGYNSLFRNLNTDGGHRRDNCYfdas 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 314 ---NIVPFTLKQWK--EAIASN--FLFINGtdswattyieNHDQARSITRFaddSPKYRKIS-GKLLTllecsLTGTLYV 385
Cdd:cd11348  287 gkgDIKPFVDEYLPqyEATKGKgyISLPTC----------NHDTPRLNARL---TEEELKLAfAFLLT-----MPGVPFI 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 386 YQGQEIGQinfkewpiekyedvdvkNNYEIIKKSFGKNskemkdffkgiallSRDHSRTPMPWTkDKPNAGFTGPDVKPW 465
Cdd:cd11348  349 YYGDEIGM-----------------RYIEGLPSKEGGY--------------NRTGSRTPMQWD-SGKNAGFSTAPAERL 396
                        490       500
                 ....*....|....*....|....*....
gi 398365967 466 FFLNESFEQGINVEQESRDDDSVLNFWKR 494
Cdd:cd11348  397 YLPVDPAPDRPTVAAQEDDPNSLLNFVRD 425
Aamy smart00642
Alpha-amylase domain;
21-113 2.81e-40

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 144.01  E-value: 2.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967    21 QIYPASFKDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQ---DMGYDISNYEKVWPTYGTNEDCFELIDKTH 97
Cdd:smart00642   1 QIYPDRFADGNGDGGGDLQGIIEKLDYLKDLGVTAIWLSPIFESPQGypsYHGYDISDYKQIDPRFGTMEDFKELVDAAH 80
                           90
                   ....*....|....*.
gi 398365967    98 KLGMKFITDLVINHCS 113
Cdd:smart00642  81 ARGIKVILDVVINHTS 96
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
18-394 4.78e-37

Alpha amylase catalytic domain 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; and 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 this 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: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 138.46  E-value: 4.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  18 TIYQIYPASFKDSN---NDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYDIS---NYEKVWPTYGTNEDCFE 91
Cdd:cd00551    1 VIYQLFPDRFTDGDssgGDGGGDLKGIIDKLDYLKDLGVTAIWLTPIFESPEYDGYDKDDgylDYYEIDPRLGTEEDFKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  92 LIDKTHKLGMKFITDLVINHcstehewfkesrssktnpkrdwffwrppkgydaegkpippnnwksffggsawtfdettne 171
Cdd:cd00551   81 LVKAAHKRGIKVILDLVFNH------------------------------------------------------------ 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 172 fylrlfasrqvdlnwenedcrraifeSAVGFWLDHGVDGFRIDTAGLYSKrpglpdspifdktsklqhpnwgshngPRIH 251
Cdd:cd00551  101 --------------------------DILRFWLDEGVDGFRLDAAKHVPK--------------------------PEPV 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 252 EYHQELHRFMKNRVKDgreIMTVGEVAHGSDNALYTSAARYEVSEVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNF 331
Cdd:cd00551  129 EFLREIRKDAKLAKPD---TLLLGEAWGGPDELLAKAGFDDGLDSVFDFPLLEALRDALKGGEGALAILAALLLLNPEGA 205
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365967 332 LFINgtdswattYIENHDQARSITRFADDSPKYRKISGKLLTLLECSLTGTLYVYQGQEIGQI 394
Cdd:cd00551  206 LLVN--------FLGNHDTFRLADLVSYKIVELRKARLKLALALLLTLPGTPMIYYIKKLIAL 260
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
13-218 3.69e-34

Alpha amylase catalytic domain found in archaeal and 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 firmicutes, bacteroidetes, and proteobacteria. 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: 200452 [Multi-domain]  Cd Length: 336  Bit Score: 132.29  E-value: 3.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  13 WWKEATIYQIYPASFKDSnndgwGDLKGITSKLQYIKDLGVDAIWVCPFY-----------DSPqqdmgYDISNYEKVWP 81
Cdd:cd11313    1 WLRDAVIYEVNVRQFTPE-----GTFKAVTKDLPRLKDLGVDILWLMPIHpigeknrkgslGSP-----YAVKDYRAVNP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  82 TYGTNEDCFELIDKTHKLGMKFITDLVINHCSTEHEWFKEsrssktNPkrDWFFWrppkgyDAEGKPIPPnnwksFFGgs 161
Cdd:cd11313   71 EYGTLEDFKALVDEAHDRGMKVILDWVANHTAWDHPLVEE------HP--EWYLR------DSDGNITNK-----VFD-- 129
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 398365967 162 aWTfdettnefylrlfasRQVDLNWENEDCRRAIFEsAVGFWLD-HGVDGFRIDTAGL 218
Cdd:cd11313  130 -WT---------------DVADLDYSNPELRDYMID-AMKYWVReFDVDGFRCDVAWG 170
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
11-404 1.22e-33

Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. 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: 200468 [Multi-domain]  Cd Length: 477  Bit Score: 134.05  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  11 PKWWKEATIYQIYPASFkdsnndgwgdlkGITSKLQYIKDLGVDAIwvcpFYDSPQQDmgydisnyEKVWPTYGTNEDCF 90
Cdd:cd11329   63 LKWWQKGPLVELDTESF------------FKEEHVEAISKLGAKGV----IYELPADE--------TYLNNSYGVESDLK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  91 ELIDKTHKLGMKFITDLVINHCSTEHEWFKESrSSKTNPKRDWFFWRPPKGydaegkPIPPNNWKSFFGGSAWTFDETTN 170
Cdd:cd11329  119 ELVKTAKQKDIKVILDLTPNHSSKQHPLFKDS-VLKEPPYRSAFVWADGKG------HTPPNNWLSVTGGSAWKWVEDRQ 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 171 eFYLRLFASRQVDLNWENEDCRRAiFESAVGFWLDHGVDGFRIDTAGLYSKRPGLPDSPIFDKTSKLQHPNWGS------ 244
Cdd:cd11329  192 -YYLHQFGPDQPDLNLNNPAVVDE-LKDVLKHWLDLGVRGFRLANAKYLLEDPNLKDEEISSNTKGVTPNDYGFythikt 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 245 HNGPRIHEYHQELHRFMKNrVKDGREIMTVGEVAHGSDNALYTSAARYevsevfsfthVELGTSPFFRYNIVPFTLKQWK 324
Cdd:cd11329  270 TNLPELGELLREWRSVVKN-YTDGGGLSVAEDIIRPDVYQVNGTLDLL----------IDLPLYGNFLAKLSKAITANAL 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 325 EAIASNFLFINGTDSWATTYIENHDQARSitrfADDSpkyrkisgklLTLLECSLTGTLYVYQGQEIGQINFKE--WPIE 402
Cdd:cd11329  339 HKILASISTVSATTSWPQWNLRYRDTKVV----ASDA----------LTLFTSLLPGTPVVPLDSELYANVSKPtiSTLE 404

                 ..
gi 398365967 403 KY 404
Cdd:cd11329  405 KF 406
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
16-392 6.26e-33

Alpha amylase catalytic domain found in 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). 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: 200477 [Multi-domain]  Cd Length: 389  Bit Score: 130.30  E-value: 6.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  16 EATIYQIYPASFKDSN---------------------NDGW-----------GDLKGITSKLQYIKDLGVDAIWVCPFYD 63
Cdd:cd11338    1 DAVFYQIFPDRFANGDpsndpkggeynyfgwpdlpdyPPPWggeptrrdfygGDLQGIIEKLDYLKDLGVNAIYLNPIFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  64 SPQqDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPK-RDWFFWRppkgY 142
Cdd:cd11338   81 APS-NHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGESSAyQDWFSIY----Y 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 143 DAEGKPIPPNNWKSFFGgsawtfdettnefylrlfasrqVD----LNWENEDCRRaIFESAVGFWLDHG-VDGFRIDTAg 217
Cdd:cd11338  156 FWPYFTDEPPNYESWWG----------------------VPslpkLNTENPEVRE-YLDSVARYWLKEGdIDGWRLDVA- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 218 lyskrPGLPdspifdktsklqhpnwgshngpriHEYHQELHRFMKNRVKDgreIMTVGEVAHGSDNAL----YTSAARYE 293
Cdd:cd11338  212 -----DEVP------------------------HEFWREFRKAVKAVNPD---AYIIGEVWEDARPWLqgdqFDSVMNYP 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 294 vsevfsFTHVELGtspFFRYNivPFTLKQWKEAIASnFLFINGTDSWATTY--IENHDQARSITRFADDSPKYrkisgKL 371
Cdd:cd11338  260 ------FRDAVLD---FLAGE--EIDAEEFANRLNS-LRANYPKQVLYAMMnlLDSHDTPRILTLLGGDKARL-----KL 322
                        410       420
                 ....*....|....*....|.
gi 398365967 372 LTLLECSLTGTLYVYQGQEIG 392
Cdd:cd11338  323 ALALQFTLPGAPCIYYGDEIG 343
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
18-215 1.76e-26

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: 200479 [Multi-domain]  Cd Length: 407  Bit Score: 111.92  E-value: 1.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  18 TIYQIYPASFK--DSNND---------------GW--GDLKGITSKLQYIKDLGVDAIWVCPFY--DSPQQDM-GYDISN 75
Cdd:cd11340    5 VIYLIMPDRFAngDPSNDsvpgmlekadrsnpnGRhgGDIQGIIDHLDYLQDLGVTAIWLTPLLenDMPSYSYhGYAATD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  76 YEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTEHEWFKESrssktnPKRDWFfwrppkgydaegkpippNNWK 155
Cdd:cd11340   85 FYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSEHWWMKDL------PTKDWI-----------------NQTP 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365967 156 SF----FGGSAWT--------FDETTNEFylrlFASRQVDLNWENEDCRRAIFESAVgFWLDH-GVDGFRIDT 215
Cdd:cd11340  142 EYtqtnHRRTALQdpyasqadRKLFLDGW----FVPTMPDLNQRNPLVARYLIQNSI-WWIEYaGLDGIRVDT 209
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
18-390 4.57e-25

Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 107.37  E-value: 4.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  18 TIYQIYPASFKD---SNNDG----------------WG-DLKGITSKLQYIKDLGVDAIWVCPFYD---SPQQDM----- 69
Cdd:cd11320    6 VIYQILTDRFYDgdtSNNPPgspglydpthsnlkkyWGgDWQGIIDKLPYLKDLGVTAIWISPPVEninSPIEGGgntgy 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  70 -GYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHcstehewfkesrsskTNPkrdWFFWRPPKGYDaEGKP 148
Cdd:cd11320   86 hGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNH---------------SSP---ADYAEDGALYD-NGTL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 149 IP--PNNWKSFFGGSAWTfDETTNEFYLR---LFAsrQVDLNWENEDCRRAIFESAVgFWLDHGVDGFRIDTAglyskrp 223
Cdd:cd11320  147 VGdyPNDDNGWFHHNGGI-DDWSDREQVRyknLFD--LADLNQSNPWVDQYLKDAIK-FWLDHGIDGIRVDAV------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 224 glpdspifdktsKLQHPNWgshngpriheyhqeLHRFMkNRVKDGREIMTVGEVAHGSDNALY----TSAARYEVSEV-- 297
Cdd:cd11320  216 ------------KHMPPGW--------------QKSFA-DAIYSKKPVFTFGEWFLGSPDPGYedyvKFANNSGMSLLdf 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 298 -FSFTHVELgtspfFRYNivPFTLKQWKEAIASNFLFINGtDSWATTYIENHDqarsITRFADDSPKYRKISGKLLTLLe 376
Cdd:cd11320  269 pLNQAIRDV-----FAGF--TATMYDLDAMLQQTSSDYNY-ENDLVTFIDNHD----MPRFLTLNNNDKRLHQALAFLL- 335
                        410
                 ....*....|....
gi 398365967 377 cSLTGTLYVYQGQE 390
Cdd:cd11320  336 -TSRGIPVIYYGTE 348
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
36-224 3.75e-24

Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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: 200463  Cd Length: 536  Bit Score: 106.50  E-value: 3.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  36 GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQ--QDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCS 113
Cdd:cd11324   83 GDLKGLAEKIPYLKELGVTYLHLMPLLKPPEgdNDGGYAVSDYREVDPRLGTMEDLRALAAELRERGISLVLDFVLNHTA 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 114 TEHEWFKESRSSktNPK-RDWFFWRP----PKGYDAEGKPIPPNN------WKSFFGGSAWTfdeTTNEFylrlfasrQV 182
Cdd:cd11324  163 DEHEWAQKARAG--DPEyQDYYYMFPdrtlPDAYERTLPEVFPDTapgnftWDEEMGKWVWT---TFNPF--------QW 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 398365967 183 DLNWENEDCRRAIFESAVgFWLDHGVDGFRIDTAGLYSKRPG 224
Cdd:cd11324  230 DLNYANPAVFNEMLDEML-FLANQGVDVLRLDAVAFIWKRLG 270
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
5-224 4.75e-24

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 106.24  E-value: 4.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   5 DHPETEPKWWKEATIYQIYPASFKDSN--------------------NDGW---------------GDLKGITSKLQYIK 49
Cdd:PRK10785 110 DVPDQGPQWVADQVFYQIFPDRFARSLpreavqdhvyyhhaagqeiiLRDWdepvtaqaggstfygGDLDGISEKLPYLK 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  50 DLGVDAIWVCPFYDSPQqDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTEHEWFKesrssktnp 129
Cdd:PRK10785 190 KLGVTALYLNPIFTAPS-VHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTGDSHPWFD--------- 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 130 krdwffwRPPKGYD-AEGKPIPPnnWKSFFggsawTFDETTNEFYLRLFASRQVdLNWENEDCRRAIF---ESAVGFWLD 205
Cdd:PRK10785 260 -------RHNRGTGgACHHPDSP--WRDWY-----SFSDDGRALDWLGYASLPK-LDFQSEEVVNEIYrgeDSIVRHWLK 324
                        250       260
                 ....*....|....*....|.
gi 398365967 206 --HGVDGFRIDTAGLYSKRPG 224
Cdd:PRK10785 325 apYNIDGWRLDVVHMLGEGGG 345
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
4-286 7.09e-20

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: 92.38  E-value: 7.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   4 SDHPETEPKWWKEA--TIYQIYPASFKDSNNDGW--GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDM---GYDISNY 76
Cdd:cd11352   11 SDGKERPRPLFDGNdpAVATWEDNFGWESQGQRFqgGTLKGVRSKLGYLKRLGVTALWLSPVFKQRPELEtyhGYGIQNF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  77 EKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHC--------------STEHEWFKESRSSKTNPKRDWFFwrPPKGY 142
Cdd:cd11352   91 LDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSgdvfsydddrpyssSPGYYRGFPNYPPGGWFIGGDQD--ALPEW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 143 DAEGKPIP-----PNNWKSFFGGSAWTFDETTNE---FYLRlfasrqvDLNWENEDCR---RAIFESAVGFWL---DhgV 208
Cdd:cd11352  169 RPDDAIWPaelqnLEYYTRKGRIRNWDGYPEYKEgdfFSLK-------DFRTGSGSIPsaaLDILARVYQYWIayaD--I 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365967 209 DGFRIDTAglyskrpglpdspifdktsKLQHPNWGSHNGPRIHEYHQELHRfmknrvkdgREIMTVGEVAHGSDNALY 286
Cdd:cd11352  240 DGFRIDTV-------------------KHMEPGAARYFCNAIKEFAQSIGK---------DNFFLFGEITGGREAAAY 289
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
18-352 2.16e-19

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: 89.62  E-value: 2.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  18 TIYQIYPASFKD---SNN---------------DGW--GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDM------GY 71
Cdd:cd11339    4 TIYFVMTDRFYDgdpSNDngggdgdprsnptdnGPYhgGDFKGLIDKLDYIKDLGFTAIWITPVVKNRSVQAgsagyhGY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  72 DISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCStehewfkesrssktnpkrdwffwrppkgydaegkpipp 151
Cdd:cd11339   84 WGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG-------------------------------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 152 nnwksffggsawtfdettnefylrlfasrqvDLNWENEDCRRAiFESAVGFWLDHGVDGFRIDTAGlyskrpglpdspif 231
Cdd:cd11339  126 -------------------------------DLNTENPEVVDY-LIDAYKWWIDTGVDGFRIDTVK-------------- 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 232 dktsKLQHPNWgshngpriHEYHQELhrfMKNRVKDGreIMTVGEVAHGSDNalYTSaaryevsevfSFTHVELGTSPF- 310
Cdd:cd11339  160 ----HVPREFW--------QEFAPAI---RQAAGKPD--FFMFGEVYDGDPS--YIA----------PYTTTAGGDSVLd 210
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 398365967 311 --FRYNIVPFTLKQWKEAIASNFLFING---TDSWATTYIENHDQAR 352
Cdd:cd11339  211 fpLYGAIRDAFAGGGSGDLLQDLFLSDDlynDATELVTFLDNHDMGR 257
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
16-216 8.66e-17

Alpha amylase catalytic domain found in eukaryotic and 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 mainly 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: 200490 [Multi-domain]  Cd Length: 366  Bit Score: 82.22  E-value: 8.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  16 EATIYQIYPASFKDS--NNDGWGD----LKGITSKLQYIKDLGVDAIWVCPFYDSPQQdmGYDISNYEKVWPTYGTNEDC 89
Cdd:cd11353    1 EAVFYHIYPLGFCGApkENDFDGEtehrILKLEDWIPHLKKLGINAIYFGPVFESDSH--GYDTRDYYKIDRRLGTNEDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  90 FELIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTN-PKRDWFfwrppKGYDAEGKpippNNWKSFFGGSAWtfdet 168
Cdd:cd11353   79 KAVCKKLHENGIKVVLDGVFNHVGRDFFAFKDVQENRENsPYKDWF-----KGVNFDGN----SPYNDGFSYEGW----- 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 398365967 169 tnEFYLRLfasrqVDLNWENEDCRRAIFEsAVGFWLDH-GVDGFRIDTA 216
Cdd:cd11353  145 --EGHYEL-----VKLNLHNPEVVDYLFD-AVRFWIEEfDIDGLRLDVA 185
AmyAc_Sucrose_phosphorylase-like cd11343
Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose ...
23-224 1.30e-15

Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase); Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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: 200481  Cd Length: 445  Bit Score: 79.46  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  23 YPASFKdsnNDGWGDLKGITSKLQ-YIKDLgVDAIWVCPFYDSpQQDMGYDISNYEKVWPTYGTNEDcFELIDKTHKLgM 101
Cdd:cd11343    9 YGDSLG---REGEKPLKTLNKFLDeHLKGA-IGGVHILPFFPY-SSDDGFSVIDYTEVDPRLGDWDD-IEALAEDYDL-M 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 102 kfiTDLVINHCSTEHEWFKESRsSKTNPKRDWFFWRPPKgYDAEG----KPIPPNNWKSFFGGSAW---TFDETtnefyl 174
Cdd:cd11343   82 ---FDLVINHISSQSPWFQDFL-AGGDPSKDYFIEADPE-EDLSKvvrpRTSPLLTEFETAGGTKHvwtTFSED------ 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 398365967 175 rlfasrQVDLNWENEDCRRAiFESAVGFWLDHGVDGFRIDTAGLYSKRPG 224
Cdd:cd11343  151 ------QIDLNFRNPEVLLE-FLDILLFYAANGARIIRLDAVGYLWKELG 193
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
36-393 1.39e-14

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: 75.77  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  36 GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQ-DMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCST 114
Cdd:cd11350   30 GDFKGVIDKLDYLQDLGVNAIELMPVQEFPGNdSWGYNPRHYFALDKAYGTPEDLKRLVDECHQRGIAVILDVVYNHAEG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 115 EhewfkesrssktNP--KRDWFFWRPPKGYDaegkPIPPNNWKSFFGgsawtfdettNEFYlrlfasrqvDLNWENEdCR 192
Cdd:cd11350  110 Q------------SPlaRLYWDYWYNPPPAD----PPWFNVWGPHFY----------YVGY---------DFNHESP-PT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 193 RAIFESAVGFWLD-HGVDGFRID-TAGLYSKRPGlpdspifdktsklqhPNWGSHNGPRIHEYHQELHRFMKNRVKDgre 270
Cdd:cd11350  154 RDFVDDVNRYWLEeYHIDGFRFDlTKGFTQKPTG---------------GGAWGGYDAARIDFLKRYADEAKAVDKD--- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 271 IMTVGEvaHGSDNALYTSAARYEVS----EVFSFTHVELGTSPFFRYNIVPFTLKQWKEAIASNFLfingtdswatTYIE 346
Cdd:cd11350  216 FYVIAE--HLPDNPEETELATYGMSlwgnSNYSFSQAAMGYQGGSLLLDYSGDPYQNGGWSPKNAV----------NYME 283
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 398365967 347 NHDQARSITRFADDSPKYRKISGKLLTLLE-CSLTGTLY--------VYQGQEIGQ 393
Cdd:cd11350  284 SHDEERLMYKLGAYGNGNSYLGINLETALKrLKLAAAFLftapgppmIWQGGEFGY 339
malS PRK09505
alpha-amylase; Reviewed
8-216 2.10e-13

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 73.16  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   8 ETEPKWWKEATIYQIYPASFK--DSNND--------------GW--GDLKGITSKLQYIKDLGVDAIWVCPFY------- 62
Cdd:PRK09505 181 AAAPFDWHNATVYFVLTDRFEngDPSNDhsygrhkdgmqeigTFhgGDLRGLTEKLDYLQQLGVNALWISSPLeqihgwv 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  63 ------DSPQQDM-GYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHC--STEHE---------WFKESRS 124
Cdd:PRK09505 261 gggtkgDFPHYAYhGYYTLDWTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTgyATLADmqefqfgalYLSGDEN 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 125 SKTNPKRdWFFWRPPKGydaegkpippNNWKSF-----FG---------GSAWT-----------FD------------- 166
Cdd:PRK09505 341 KKTLGER-WSDWQPAAG----------QNWHSFndyinFSdstawdkwwGKDWIrtdigdydnpgFDdltmslaflpdik 409
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365967 167 -ETTN-----EFYLRLFASRQVDLnwENEDCRRAIFEsavgfWL-----DHGVDGFRIDTA 216
Cdd:PRK09505 410 tESTQasglpVFYANKPDTRAKAI--DGYTPRDYLTH-----WLsqwvrDYGIDGFRVDTA 463
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
14-111 1.91e-12

Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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: 200458 [Multi-domain]  Cd Length: 375  Bit Score: 69.13  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  14 WKEATIYQIYPASFKDSNNDGW------------GDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGYD-------IS 74
Cdd:cd11319    6 WRSRSIYQVLTDRFARTDGSSTapcdtadrtycgGTWKGIINKLDYIQGMGFDAIWISPIVKNIEGNTAYGeayhgywAQ 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365967  75 NYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINH 111
Cdd:cd11319   86 DLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNH 122
AmyAc_Sucrose_phosphorylase-like_1 cd11356
Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called ...
46-224 3.34e-11

Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase); Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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: 200493  Cd Length: 458  Bit Score: 65.61  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  46 QYIKDLgVDAIWVCPFYDSPQQDmGYDISNYEKVWPTYGTNEDcFELIDKTHKLgMkfiTDLVINHCSTEHEWFKESRSS 125
Cdd:cd11356   32 EHLKDT-ISGVHILPFFPYSSDD-GFSVIDYRQVNPELGDWED-IEALAKDFRL-M---FDLVINHVSSSSPWFQQFLAG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 126 KtNPKRDWFFwrppkgydaegKPIPPNNWKSFF--------------GGSAWTFdeTTnefylrlFASRQVDLNWENEDC 191
Cdd:cd11356  105 E-PPYKDYFI-----------EADPDTDLSQVVrprtsplltpfetaDGTKHVW--TT-------FSPDQVDLNFRNPEV 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 398365967 192 RRAIFESAVgFWLDHGVDGFRIDTAGLYSKRPG 224
Cdd:cd11356  164 LLEFLDILL-FYLERGARIIRLDAVAFLWKEPG 195
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
19-216 7.44e-11

Alpha amylase catalytic domain found in 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 mainly 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: 200476 [Multi-domain]  Cd Length: 328  Bit Score: 63.70  E-value: 7.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  19 IYQIYPASF--KDSNNDGWGD----LKGITSKLQYIKDLGVDAIWVCPFYDSPQQdmGYDISNYEKVWPTYGTNEDCFEL 92
Cdd:cd11337    2 FYHIYPLGFcgAPIRNDFDGPpehrLLKLEDWLPHLKELGCNALYLGPVFESDSH--GYDTRDYYRIDRRLGTNEDFKAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  93 IDKTHKLGMKFITDLVINHCStehewfkesrssktnpkRDwFFWrppkgydaEGkpippnnwksffggsawtfdettnef 172
Cdd:cd11337   80 VAALHERGIRVVLDGVFNHVG-----------------RD-FFW--------EG-------------------------- 107
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 398365967 173 YLRLfasrqVDLNWENEDCRRAIFEsAVGFWLDHG-VDGFRIDTA 216
Cdd:cd11337  108 HYDL-----VKLNLDNPAVVDYLFD-VVRFWIEEFdIDGLRLDAA 146
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
10-119 1.48e-10

Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. 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: 200483 [Multi-domain]  Cd Length: 326  Bit Score: 62.84  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  10 EPKWWKEATIYQIY-PASFKDSNNdgwgdLKGITSKLQYIKDLGVDAIWVCPFYDSPQQDMGydISNYEKVWPTYGTNED 88
Cdd:cd11345    9 EMNWWNEGPLYQIGdLQAFSEAGG-----LKGVEGKLDYLSQLKVKGLVLGPIHVVQADQPG--ELNLTEIDPDLGTLED 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 398365967  89 CFELIDKTHKLGMKFITDLVINHCStEHEWF 119
Cdd:cd11345   82 FTSLLTAAHKKGISVVLDLTPNYRG-ESSWA 111
AmyAc_Sucrose_phosphorylase cd11355
Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose ...
36-255 2.70e-09

Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase); Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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: 200492  Cd Length: 433  Bit Score: 59.55  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  36 GDLKGITSKLQ-YIKDLgVDAIWVCPFYdSPQQDMGYDISNYEKVWPTYGTNEDcFELIDKTHKLgmkfITDLVINHCST 114
Cdd:cd11355   15 GNLKDLNTVLDtYFKGV-FGGVHILPFF-PSSDDRGFDPIDYTEVDPRFGTWDD-IEALGEDYEL----MADLMVNHISA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 115 EHEWFKESRSSKTNPK------RDWFFWRPPKGYDAE------GKPIPPNnwksffggSAWTFDETTNEFYLRLFASRQV 182
Cdd:cd11355   88 QSPYFQDFLAKGDASEyadlflTYKDFWFPGGPTEEDldkiyrRRPGAPF--------TTITFADGSTEKVWTTFTEEQI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 183 DLNWeNEDCRRAIFESAVGFWLDHGVDGFRIDTAGLYSKRPG------LPDspIFDKTSKLQ---HPnWGSHNGPRIHEY 253
Cdd:cd11355  160 DIDV-RSDVGKEYLESILEFLAANGVKLIRLDAFGYAIKKAGtscffvEPE--TWEFLDELAqiaKP-LGIEVLPEIHSH 235

                 ..
gi 398365967 254 HQ 255
Cdd:cd11355  236 YS 237
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
13-216 1.95e-07

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: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 53.48  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  13 WWkeatiyQIYPASF-------KDSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFYDSPQQdmGYDISNYEKVWPTYGT 85
Cdd:cd11354    4 WW------HVYPLGFvgapirpREPEAAVEHRLDRLEPWLDYAVELGCNGLLLGPVFESASH--GYDTLDHYRIDPRLGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  86 NEDCFELIDKTHKLGMKFITDLVINHCSTEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEgkpippnnwksfFGGSAWTf 165
Cdd:cd11354   76 DEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALEDGPGSEEDRWHGHAGGGTPAV------------FEGHEDL- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398365967 166 dettnefylrlfasrqVDLNWENEDCRRAIFEsAVGFWLDHGVDGFRIDTA 216
Cdd:cd11354  143 ----------------VELDHSDPAVVDMVVD-VMCHWLDRGIDGWRLDAA 176
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
3-218 4.89e-07

pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.


Pssm-ID: 273975 [Multi-domain]  Cd Length: 605  Bit Score: 52.70  E-value: 4.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967    3 ISDHPETEPKWWK-----------EATIYQIYPASFKDSNNDGW---GDLKGITSK-----------LQYIKDLGVDAIW 57
Cdd:TIGR02104 103 VIDLEETNPEGWEkdhgprlenpeDAIIYELHIRDFSIHENSGVknkGKYLGLTETgtkgpngvstgLDYLKELGVTHVQ 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   58 VCPFYD---------SPQQDMGYDISNYEKVWPTYGTN--------EDCFELIDKTHKLGMKFITDLVINHC-STEHEWF 119
Cdd:TIGR02104 183 LLPVFDfagvdeedpNNAYNWGYDPLNYNVPEGSYSTNpydpatriRELKQMIQALHENGIRVIMDVVYNHTySREESPF 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  120 KesrssKTNPkrDWFFwRppkgYDAEGkpippnnwkSFFGGSAwtfdeTTNEFylrlfASrqvdlnwENEDCRRAIFESa 199
Cdd:TIGR02104 263 E-----KTVP--GYYY-R----YNEDG---------TLSNGTG-----VGNDT-----AS-------EREMMRKFIVDS- 303
                         250       260
                  ....*....|....*....|
gi 398365967  200 VGFWL-DHGVDGFRIDTAGL 218
Cdd:TIGR02104 304 VLYWVkEYNIDGFRFDLMGI 323
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
511-583 6.76e-07

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 47.16  E-value: 6.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365967  511 DFQFIDLDSDQIFSFTKEYEDKTLFAALNFSGEEIEFSLPR-EGASLsfilgnyddTDVSSRVLKPWEGRIYLV 583
Cdd:pfam16657   2 DFRFLEPDNRKVLAYLREYEDETILVVANRSAQPVELDLSAfEGRVP---------VELFGGEPFPPIGGLYFL 66
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
29-128 8.41e-07

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 51.81  E-value: 8.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  29 DSNNDG--WgdlKGITSKLQYIKDLGVDAIWVCPFY--DSPQQDMGYDISNY---------EKVWPTYGTNEDCFELIDK 95
Cdd:PRK09441  13 YLPNDGklW---NRLAERAPELAEAGITAVWLPPAYkgTSGGYDVGYGVYDLfdlgefdqkGTVRTKYGTKEELLNAIDA 89
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 398365967  96 THKLGMKFITDLVINHCS--TEHEWFKESRSSKTN 128
Cdd:PRK09441  90 LHENGIKVYADVVLNHKAgaDEKETFRVVEVDPDD 124
AmyAc_GlgE_like cd11344
Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan: ...
17-214 1.20e-06

Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. 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: 200482 [Multi-domain]  Cd Length: 355  Bit Score: 50.68  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  17 ATIYQIYPASFKdSNNDGWGDLKGITSKLQYIKDLGVDAIWVCPFY-----------DSPQQDMG-----YDISNYE--- 77
Cdd:cd11344    2 SAWYEFFPRSAG-ADPGRHGTFRDAEARLPRIAAMGFDVLYLPPIHpigrtnrkgknNALVAGPGdpgspWAIGSEEggh 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  78 -KVWPTYGTNEDCFELIDKTHKLGMKFITDLVINhCSTEHEWFKEsrssktNPkrDWFFWR----------PPKGYdaeg 146
Cdd:cd11344   81 dAIHPELGTLEDFDRLVAEARELGIEVALDIALQ-CSPDHPYVKE------HP--EWFRHRpdgsiqyaenPPKKY---- 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365967 147 KPIPPnnwksffggsawtfdettnefylrlfasrqvdLNWENEDcRRAIFE---SAVGFWLDHGVDGFRID 214
Cdd:cd11344  148 QDIYP--------------------------------LDFETED-WKGLWQelkRVFLFWIEHGVRIFRVD 185
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
41-111 1.33e-06

Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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: 200453 [Multi-domain]  Cd Length: 302  Bit Score: 50.30  E-value: 1.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365967  41 ITSKLQYIKDLGVDAIWVCPFYDSPQQD-MGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINH 111
Cdd:cd11314   20 LESKAPELAAAGFTAIWLPPPSKSVSGSsMGYDPGDLYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINH 91
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
19-216 1.58e-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 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: 200487 [Multi-domain]  Cd Length: 456  Bit Score: 50.75  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  19 IYQIYPASF--KDSNNDGWGDLK--------GITSK-LQYIKDLGVDAIWVC-----------PFYDSPQQD-------M 69
Cdd:cd11349    3 IYQLLPRLFgnKNTTNIPNGTIEengvgkfnDFDDTaLKEIKSLGFTHVWYTgvirhatqtdySAYGIPPDDpdivkgrA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  70 G--YDISNYEKVWPTYGTN------EdcFE-LIDKTHKLGMKFITDLVINHCSTEHewfkesRS-SKTNPKRDW------ 133
Cdd:cd11349   83 GspYAIKDYYDVDPDLATDptnrmeE--FEaLVERTHAAGLKVIIDFVPNHVARQY------HSdAKPEGVKDFganddt 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 134 ---------FFWRPPKGYDAEGKPIPPNNWKSFFGGSA--WT----FDET--TNEFYlrlfasRQVDLNW-----ENEDC 191
Cdd:cd11349  155 skafdpsnnFYYLPGEPFVLPFSLNGSPATDGPYHESPakATgndcFSAApsINDWY------ETVKLNYgvdydGGGSF 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 398365967 192 R-----------RAIFEsavgFWLDHGVDGFRIDTA 216
Cdd:cd11349  229 HfdpipdtwikmLDILL----FWAAKGVDGFRCDMA 260
AmyAc_MTase_N cd11335
Alpha amylase catalytic domain found in maltosyltransferase; Maltosyltransferase (MTase), a ...
5-220 3.53e-06

Alpha amylase catalytic domain found in maltosyltransferase; Maltosyltransferase (MTase), a maltodextrin glycosyltransferase, acts on starch and maltooligosaccharides. It catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or maltooligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose. MTase is a homodimer. The catalytic core domain has the (beta/alpha) 8 barrel fold with the active-site cleft formed at the C-terminal end of the barrel. Substrate binding experiments have led to the location of two distinct maltose-binding sites: one lies in the active-site cleft and the other is located in a pocket adjacent to the active-site cleft. It is a member of the alpha-amylase family, but unlike typical alpha-amylases, MTase does not require calcium for activity and lacks two histidine residues which are predicted to be critical for binding the glucose residue adjacent to the scissile bond in the substrates. The common reaction chemistry of the alpha-amylase family of 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. 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: 200474 [Multi-domain]  Cd Length: 538  Bit Score: 50.00  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   5 DHPETEPKWWKEATIYQIYP---ASFkDSNNDGW---GDLKGITSK---------LQYIKDLGVDAIWVCPF-------- 61
Cdd:cd11335   34 LKGASKGDWIKSSSVYSLFVrttTAW-DHDGDGAlepENLYGFRETgtflkmialLPYLKRMGINTIYLLPItkiskkfk 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  62 ---YDSPqqdmgYDISNYEKVWPTYG--------TNEDCFELIDKTHKLGMKFITDLVINHCSTEHEWFKEsrssktNPk 130
Cdd:cd11335  113 kgeLGSP-----YAVKNFFEIDPLLHdpllgdlsVEEEFKAFVEACHMLGIRVVLDFIPRTAARDSDLILE------HP- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 131 rDWFFWRPPKGYDAEGKPIPPNNWKSFFggsawtFDETTNEFY--------LRLFASRQVDLNWENEDCRRAIFESAVGF 202
Cdd:cd11335  181 -EWFYWIKVDELNNYHPPKVPGLGFVLP------SQETLPLIYesedvkehLKLFRWSPNKIDPEKWRNFFKENPKPEGD 253
                        250
                 ....*....|....*...
gi 398365967 203 WLDHGVDGFRIDTAGLYS 220
Cdd:cd11335  254 FLGEIEKEFGCTTAPAFS 271
AmyAc_bac_euk_BE cd11321
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching ...
45-219 1.21e-05

Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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: 200460 [Multi-domain]  Cd Length: 406  Bit Score: 48.00  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  45 LQYIKDLGVDAIWVC-----PFYDSpqqdMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTEHE-- 117
Cdd:cd11321   45 LPRIKKLGYNAIQLMaimehAYYAS----FGYQVTNFFAASSRFGTPEDLKYLIDTAHGMGIAVLLDVVHSHASKNVLdg 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 118 --WFKESRSSktnpkrdwFFWRPPKGYDAEgkpippnnWKSffggsawtfdettnefylRLFasrqvdlNWENEDCRRAI 195
Cdd:cd11321  121 lnMFDGTDGC--------YFHEGERGNHPL--------WDS------------------RLF-------NYGKWEVLRFL 159
                        170       180
                 ....*....|....*....|....*..
gi 398365967 196 FeSAVGFWLD-HGVDGFRID--TAGLY 219
Cdd:cd11321  160 L-SNLRWWLEeYRFDGFRFDgvTSMLY 185
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
36-216 1.53e-05

Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase); Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. 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: 200462 [Multi-domain]  Cd Length: 569  Bit Score: 47.67  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  36 GDLKGITSKLQYIKDLGVDAIWVC--PFYDSPQQDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVI---- 109
Cdd:cd11323   94 GDIVGLVDSLDYLQGMGIKGIYIAgtPFINMPWGADGYSPLDFTLLDHHFGTIADWRAAIDEIHRRGMYVVLDNTVatmg 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 110 ------NHCST-------EHE--WfkesrssKTNPK-RDWFF---WRP----PKGYDAEGKPIPPNNWKSFFGGSAWTFD 166
Cdd:cd11323  174 dligfeGYLNTsapfslkEYKaeW-------KTPRRyVDFNFtntYNEtceyPRFWDEDGTPVTADVTETLTGCYDSDFD 246
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365967 167 E--TTNEF--------YLRLFASRQVDLNWENEDCRRAI--FESAVGFWLDhgVDGFRIDTA 216
Cdd:cd11323  247 QygDVEAFgvhpdwqrQLSKFASVQDRLREWRPSVAQKLkhFSCLTIQMLD--IDGFRIDKA 306
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
29-111 4.17e-05

Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 45.97  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  29 DSNNDG--WGDLKGITSKLqyiKDLGVDAIWVCPFY--DSPQQDMGYDIsnYEkVW-----------PT-YGTNEDCFEL 92
Cdd:cd11318   11 YLPADGqhWKRLAEDAPEL---AELGITAVWLPPAYkgASGTEDVGYDV--YD-LYdlgefdqkgtvRTkYGTKEELLEA 84
                         90
                 ....*....|....*....
gi 398365967  93 IDKTHKLGMKFITDLVINH 111
Cdd:cd11318   85 IKALHENGIQVYADAVLNH 103
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
47-141 1.23e-04

malto-oligosyltrehalose synthase;


Pssm-ID: 237740 [Multi-domain]  Cd Length: 879  Bit Score: 44.97  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  47 YIKDLGVDAIWVCPFYDS-PQQDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINHCSTEH---EWF--- 119
Cdd:PRK14511  28 YFADLGVSHLYLSPILAArPGSTHGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVGGpdnPWWwdv 107
                         90       100
                 ....*....|....*....|....*
gi 398365967 120 -KESRSSktnPKRDWF--FWRPPKG 141
Cdd:PRK14511 108 lEWGRSS---PYADFFdiDWDSGEG 129
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
14-111 3.94e-04

1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 440065 [Multi-domain]  Cd Length: 625  Bit Score: 43.20  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  14 WKEATIYQIYPASFKDSNNDGWGDLKGITSKL-QYIKDLGVDAIWV-----CPFYDSpqqdMGYDISNYEKVWPTYGTNE 87
Cdd:COG0296  141 DAPMSIYEVHLGSWRRKEGGRFLTYRELAERLvPYLKELGFTHIELmpvaeHPFDGS----WGYQPTGYFAPTSRYGTPD 216
                         90       100
                 ....*....|....*....|....
gi 398365967  88 DCFELIDKTHKLGMKFITDLVINH 111
Cdd:COG0296  217 DFKYFVDACHQAGIGVILDWVPNH 240
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
42-111 7.39e-04

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 42.78  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   42 TSKLQYIKDLGV-DAIWVCPF---------YDSPQQDM------GYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFIT 105
Cdd:PRK14507  746 TYRLQFHKDFTFaDAEAILPYlaalgishvYASPILKArpgsthGYDIVDHSQINPEIGGEEGFERFCAALKAHGLGQLL 825

                  ....*.
gi 398365967  106 DLVINH 111
Cdd:PRK14507  826 DIVPNH 831
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
18-111 1.44e-03

Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme); The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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: 200461 [Multi-domain]  Cd Length: 402  Bit Score: 41.36  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  18 TIYQIYPASFKDSNNDGWGDLKGITSKL-QYIKDLG---VDAIWVC--PFYDSpqqdMGYDISNYEKVWPTYGTNEDCFE 91
Cdd:cd11322   37 NIYEVHLGSWKRKEDGRFLSYRELADELiPYVKEMGythVELMPVMehPFDGS----WGYQVTGYFAPTSRYGTPDDFKY 112
                         90       100
                 ....*....|....*....|
gi 398365967  92 LIDKTHKLGMKFITDLVINH 111
Cdd:cd11322  113 FVDACHQAGIGVILDWVPGH 132
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
47-214 2.30e-03

Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. 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: 200475 [Multi-domain]  Cd Length: 660  Bit Score: 40.94  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  47 YIKDLGVDAIWVCPFYDS-PQQDMGYDISNYEKVWPTYGTNEDCFELIDKTHKLGMKFITDLVINH--CSTEHEWF---- 119
Cdd:cd11336   22 YLADLGISHLYASPILTArPGSTHGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHmaVSGAENPWwwdv 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967 120 -KESRSSktnPKRDWF--FWRPPKGydAEGKPIPPnnwksFFGGSAW--------TFDETTNEFYLRLFA---------S 179
Cdd:cd11336  102 lENGPDS---PYAGFFdiDWEPPKE--LRGKVLLP-----VLGDPYGevleagelKLVFDGGGFVLRYYDhrfplapllE 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365967 180 RQV-----------DLNWenedcRR---------------AIFESA---VGFWLDHG-VDGFRID 214
Cdd:cd11336  172 RQHyrlahwrvaddEINY-----RRffdvndlaglrvedpEVFDAThalILRLVREGlVDGLRID 231
PLN02784 PLN02784
alpha-amylase
43-111 2.69e-03

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 40.76  E-value: 2.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365967  43 SKLQYIKDLGVDAIWVCPFYDS--PQQDMGYDISNYEKvwpTYGTNEDCFELIDKTHKLGMKFITDLVINH 111
Cdd:PLN02784 525 EKAAELSSLGFTVVWLPPPTESvsPEGYMPKDLYNLNS---RYGTIDELKDLVKSFHEVGIKVLGDAVLNH 592
pullulan_Gpos TIGR02102
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ...
15-217 2.87e-03

pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.


Pssm-ID: 273973 [Multi-domain]  Cd Length: 1111  Bit Score: 40.61  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967    15 KEATIYQIYPASF-KDSNNDG-----WGDLKGITSKLQYIKDLGVDAIWVCP----FY----DSPQQ-----------DM 69
Cdd:TIGR02102  450 EDAIIYEAHVRDFtSDPAIAGdltaqFGTFAAFVEKLDYLQDLGVTHIQLLPvlsyFFvnefKNKERmldyassntnyNW 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967    70 GYDISNYEKVWPTYGTNEDCFE--------LIDKTHKLGMKFITDLVINHCStehewfkesrssktnpKRDWFFWRPPKG 141
Cdd:TIGR02102  530 GYDPQNYFALSGMYSEDPKDPElriaefknLINEIHKRGMGVILDVVYNHTA----------------KVYIFEDLEPNY 593
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967   142 Y---DAEGKPippnnWKSFFGGSAWTFDETTnefylrlfasrqvdlnwenedcRRAIFESaVGFWLD-HGVDGFRIDTAG 217
Cdd:TIGR02102  594 YhfmDADGTP-----RTSFGGGRLGTTHEMS----------------------RRILVDS-IKYLVDeFKVDGFRFDMMG 645
AmyAc_1 cd11347
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
43-118 4.19e-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: 200485 [Multi-domain]  Cd Length: 391  Bit Score: 39.91  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365967  43 SKLQYIKDLGVDAIW---------------------------VCPFYD------SPqqdmgYDISNYeKVWPTYGTNEDC 89
Cdd:cd11347   31 EEFDRLAALGFDYVWlmgvwqrgpygraiarsnpglraeyreVLPDLTpddiigSP-----YAITDY-TVNPDLGGEDDL 104
                         90       100
                 ....*....|....*....|....*....
gi 398365967  90 FELIDKTHKLGMKFITDLVINHCSTEHEW 118
Cdd:cd11347  105 AALRERLAARGLKLMLDFVPNHVALDHPW 133
 
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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