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Conserved domains on  [gi|157830769]
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Chain A, CYCLODEXTRIN GLUCANOTRANSFERASE

Protein Classification

AmyAc_AmyMalt_CGTase_like and CBM20_CGTase domain-containing protein( domain architecture ID 10183102)

protein containing domains AmyAc_AmyMalt_CGTase_like, Aamy_C, IPT_CGTD, and CBM20_CGTase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
8-396 0e+00

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: 601.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   8 NFTSDVVYQIVVDRFVDGNTSNNPSG--ALFSSGCTNLRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVFSVMN 85
Cdd:cd11320    1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  86 DAsGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsYMENGRLYDNGTLLGGYTN 165
Cdd:cd11320   79 GG-GNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYPN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 166 DANMYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN 244
Cdd:cd11320  153 DDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 245 YRPVFTFGEWFL-SENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11320  233 KKPVFTFGEWFLgSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNH 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157830769 324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGN----GDPNNRKMMSSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11320  313 DMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
578-678 2.06e-61

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


:

Pssm-ID: 99882 [Multi-domain]  Cd Length: 101  Bit Score: 200.09  E-value: 2.06e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWE 657
Cdd:cd05807    1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80
                         90       100
                 ....*....|....*....|.
gi 157830769 658 SGSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05807   81 SGSNHTYTAPSSTTGTIRVNW 101
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
495-576 4.00e-34

IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown.


:

Pssm-ID: 238338 [Multi-domain]  Cd Length: 81  Bit Score: 124.76  E-value: 4.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 495 PIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYdNFEV 574
Cdd:cd00604    1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGY-NFEV 79

                 ..
gi 157830769 575 LT 576
Cdd:cd00604   80 LT 81
Aamy_C smart00632
Aamy_C domain;
406-490 6.44e-18

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 78.82  E-value: 6.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   406 EQRWINGD-VYVYERqfgKDVVLVAVNRSSSsnYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGsVNAFDLGPGE-V 483
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74

                   ....*..
gi 157830769   484 GVWAYSA 490
Cdd:smart00632  75 AIHVDAK 81
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
8-396 0e+00

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: 601.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   8 NFTSDVVYQIVVDRFVDGNTSNNPSG--ALFSSGCTNLRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVFSVMN 85
Cdd:cd11320    1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  86 DAsGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsYMENGRLYDNGTLLGGYTN 165
Cdd:cd11320   79 GG-GNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYPN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 166 DANMYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN 244
Cdd:cd11320  153 DDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 245 YRPVFTFGEWFL-SENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11320  233 KKPVFTFGEWFLgSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNH 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157830769 324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGN----GDPNNRKMMSSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11320  313 DMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
49-368 1.99e-88

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: 279.63  E-value: 1.99e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   49 GDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:pfam00128   1 GDLQGIIEKLD--YLKELGVTAIWLSPIFDS----------PQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  129 IIDFAPNHTSPASE-TNPSYMENGRLYDNGTLL---GGYTNDANMYFhHNGGTTFS----SLEDGIYRNLFDLADLNHQN 200
Cdd:pfam00128  69 ILDLVVNHTSDEHAwFQESRSSKDNPYRDYYFWrpgGGPIPPNNWRS-YFGGSAWTydekGQEYYLHLFVAGQPDLNWEN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  201 PVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPF----------GWQKSLMDEIDNY----RPVFTFGEWFLSENE---VDA 263
Cdd:pfam00128 148 PEVRNELYDVVRFWLDKGIDGFRIDVVKHISKvpglpfenngPFWHEFTQAMNETvfgyKDVMTVGEVFHGDGEwarVYT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  264 NNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAY-DEVLDQVTFIDNHDMDRFMID-GGDPRKVDMA 341
Cdd:pfam00128 228 TEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDALpDTNGWNFTFLGNHDQPRFLSRfGDDRASAKLL 307
                         330       340
                  ....*....|....*....|....*..
gi 157830769  342 LAVLLTSRGVPNIYYGTEQYMTGNGDP 368
Cdd:pfam00128 308 AVFLLTLRGTPYIYQGEEIGMTGGNDP 334
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
578-678 2.06e-61

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99882 [Multi-domain]  Cd Length: 101  Bit Score: 200.09  E-value: 2.06e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWE 657
Cdd:cd05807    1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80
                         90       100
                 ....*....|....*....|.
gi 157830769 658 SGSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05807   81 SGSNHTYTAPSSTTGTIRVNW 101
AmyA COG0366
Glycosidase [Carbohydrate transport and metabolism];
13-433 2.99e-53

Glycosidase [Carbohydrate transport and metabolism];


Pssm-ID: 223443 [Multi-domain]  Cd Length: 505  Bit Score: 190.97  E-value: 2.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNPSgalfssgctnlrKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVfsvmndasgsAS 92
Cdd:COG0366    2 VIYQIYPDRFADSNGSNGPD------------YDGGGDLKGITEKL--DYLKELGVDAIWLSPIFESP----------QA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  93 YHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNG-----TLLGGYTNDA 167
Cdd:COG0366   58 DHGYDVSDYTKVDPHFGTEEDFKELVEEAHKRGIKVILDLVFNHTSDEHPWFKEARSSKPNPKRSdyyiwRDPDPDGTPP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 168 NMYFHHNGGTTFSSLEDG-IYRNLFD--LADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM--PFG--------- 233
Cdd:COG0366  138 NNWFSVFGGDAWTWGNTGeYYLHLFSseQPDLNWENPEVREELLDVVKFWLDKGVDGFRLDAAKHIskDFGlppseenlt 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 234 --------WQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNsdNWYGFNQMIQD 305
Cdd:COG0366  218 fleeiheyLREENPDVLIYGEAITDVGEAPGAVKEDFADNTSFTNPELSMLFDFSHVGLDFEALAPL--DAEELKEILAD 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 306 TASAYDEVLDQ-VTFIDNHDMDRFM-----IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMS---- 375
Cdd:COG0366  296 WPLAVNLNDGWnNLFLSNHDQPRLLsrfgdDVGGRDASAKLLAALLFLLPGTPFIYYGDELGLTNFKDPPIKYYDDveld 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 376 -----------------------SFNKNTRA-------------------------YQVIQKLSSLRR-NNPALAYGDTE 406
Cdd:COG0366  376 siillsrdgcrtpmpwdenglnaGFTGGKPWlsvnpndllginveaqladelpeslFNFYRRLIALRKqHSALLANGEDF 455
                        490       500
                 ....*....|....*....|....*....
gi 157830769 407 QRWINGD--VYVYERQFGKDVVLVAVNRS 433
Cdd:COG0366  456 VLLADDDpsLLAFLRESGGETLLVVNNLS 484
Aamy smart00642
Alpha-amylase domain;
16-139 4.06e-38

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 139.00  E-value: 4.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769    16 QIVVDRFVDGNTSNnpsgalfssgctnlrkycGGDWQGIINKINdgYLTDMGVTAIWISQPVENVfsvmndaSGSASYHG 95
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESP-------QGYPSYHG 53
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 157830769    96 YWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:smart00642  54 YDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTSD 97
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
13-436 1.45e-37

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 148.23  E-value: 1.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNN-PSGALF--SSGCTNLRK--------------YCGGDWQGIINKIndGYLTDMGVTAIWISq 75
Cdd:PRK10785 123 VFYQIFPDRFARSLPREAvQDHVYYhhAAGQEIILRdwdepvtaqaggstFYGGDLDGISEKL--PYLKKLGVTALYLN- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  76 PVenvFSvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasETNPSYMENGRlyd 155
Cdd:PRK10785 200 PI---FT-------APSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTG---DSHPWFDRHNR--- 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 156 ngTLLGGYTNDA----NMYFHHNGGTTFSSLedGIYrnlfDLADLNHQNP-VIDR-YLKD--AVKMWID--MGIDGIRMD 225
Cdd:PRK10785 264 --GTGGACHHPDspwrDWYSFSDDGRALDWL--GYA----SLPKLDFQSEeVVNEiYRGEdsIVRHWLKapYNIDGWRLD 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 226 AVkHM-------------------------P--------FG----W-QKSLMDEIDNYRPvFTFGEW-FLSENEVDANNH 266
Cdd:PRK10785 336 VV-HMlgegggarnnlqhvagitqaakeenPeayvlgehFGdarqWlQADVEDAAMNYRG-FAFPLRaFLANTDIAYHPQ 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 267 YFANESGMSLLD-FR----FGQKLRQvlrnnsdnwygFNQMiqdtasaydevldqvtfiDNHDMDRFM-IDGGDPRKVDM 340
Cdd:PRK10785 414 QIDAQTCAAWMDeYRaglpHQQQLRQ-----------FNQL------------------DSHDTARFKtLLGGDKARMPL 464
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 341 ALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM----SSFNKNTRAYqvIQKLSSLRRNNPALAYGDTEQRWINGDVYV 416
Cdd:PRK10785 465 ALVWLFTWPGVPCIYYGDEVGLDGGNDPFCRKPFpwdeAKQDGALLAL--YQRMIALRKKSQALRRGGCQVLYAEGNVVV 542
                        490       500
                 ....*....|....*....|
gi 157830769 417 YERQFGKDVVLVAVNRSSSS 436
Cdd:PRK10785 543 FARVLQQQRVLVAINRGEAC 562
CBM_20 pfam00686
Starch binding domain;
580-676 1.52e-34

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 126.25  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIgPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:pfam00686   1 VSVTFNVN-ATTQYGQSVYIVGSIPELGNWNPKKAI-ALSASEYSSYPLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESG 78
                          90
                  ....*....|....*..
gi 157830769  660 SNHVYTTPTNTTGKIIV 676
Cdd:pfam00686  79 PNRSYTVPASGASTTTT 95
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
495-576 4.00e-34

IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown.


Pssm-ID: 238338 [Multi-domain]  Cd Length: 81  Bit Score: 124.76  E-value: 4.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 495 PIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYdNFEV 574
Cdd:cd00604    1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGY-NFEV 79

                 ..
gi 157830769 575 LT 576
Cdd:cd00604   80 LT 81
CBM_2 smart01065
Starch binding domain;
580-668 5.09e-28

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 107.82  E-value: 5.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgPMfNQVVYSYPTWYIDVSVPE-GKTIEFKFIKKDSQGNVTWES 658
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAV-PL-SPDTDGYPLWKGTVSLPPaGTTIEYKYVKVDEDGSVTWES 78
                           90
                   ....*....|
gi 157830769   659 GSNHVYTTPT 668
Cdd:smart01065  79 GPNRRLTVPE 88
Aamy_C smart00632
Aamy_C domain;
406-490 6.44e-18

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 78.82  E-value: 6.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   406 EQRWINGD-VYVYERqfgKDVVLVAVNRSSSsnYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGsVNAFDLGPGE-V 483
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74

                   ....*..
gi 157830769   484 GVWAYSA 490
Cdd:smart00632  75 AIHVDAK 81
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
495-573 1.78e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 426462 [Multi-domain]  Cd Length: 84  Bit Score: 57.46  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  495 PIIGHVGPMMGQV--GHQVTIDGEGFGTNTG--TVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYD 570
Cdd:pfam01833   1 PVITSISPSSGPAsgGTTITITGSNFGTDSSdvKVTIGGTPCTVISVSSTTIVCTTPPGVSGLVNVSVTVGGDGISSSPL 80

                  ...
gi 157830769  571 NFE 573
Cdd:pfam01833  81 TFT 83
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
62-407 1.20e-09

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: 61.18  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   62 YLTDMGVTAIWIsQPVeNVFSVMNDASGSASYH-GYWARDFKKPNPFFGT--------LSDFQRLVDAAHAKGIKVIIDF 132
Cdd:TIGR02104 172 YLKELGVTHVQL-LPV-FDFAGVDEEDPNNAYNwGYDPLNYNVPEGSYSTnpydpatrIRELKQMIQALHENGIRVIMDV 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  133 APNHT-----SPASETNPSYmengrlydngtllggytndanmYFHHNggttfsslEDGIYRNLFDLA-DLNHQNPVIDRY 206
Cdd:TIGR02104 250 VYNHTysreeSPFEKTVPGY----------------------YYRYN--------EDGTLSNGTGVGnDTASEREMMRKF 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  207 LKDAVKMWI-DMGIDGIRMDA-----VKHMpfgwqKSLMDEIDNYRP-VFTFGE-WFLS---ENEVDANNhyfANESGMS 275
Cdd:TIGR02104 300 IVDSVLYWVkEYNIDGFRFDLmgihdIETM-----NEIRKALNKIDPnILLYGEgWDLGtplPPEQKATK---ANAYQMP 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  276 LLDFrFGQKLRQVLRNN----------SDNWYGFNQMI----------QDTASAYD--EVLDQVTFIDNHDM-DRFMIDG 332
Cdd:TIGR02104 372 GIAF-FNDEFRDALKGSvfhlkkkgfvSGNPGTEEIVKkgilgsieldAVKPSALDpsQSINYVECHDNHTLwDKLSLAN 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  333 GD------PRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMSSFN------KNTRAYQV--IQKLSSLRRNNP 398
Cdd:TIGR02104 451 PDeteeqlKKRQKLATAILLLSQGIPFLHAGQEFMRTKQGDENSYNSPDSINqldwdrKATFKDDVnyIKGLIALRKAHP 530

                  ....*....
gi 157830769  399 ALAYGDTEQ 407
Cdd:TIGR02104 531 AFRLSSAED 539
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
409-489 3.82e-06

Alpha amylase, C-terminal all-beta 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: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 45.79  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  409 WINGD-----VYVYERQFGKDVVLVAVNRSSSSNYsiTGLFTALP-AGTYTDQL-------GGLLDGNTIQVGSNGSVNA 475
Cdd:pfam02806   1 WIDGDdaennVIAFERGDDGGKLLVVFNFTPSVSY--TDYRTGLPeAGTYCEVLntddeeyGGSNTGEVVTVDGPGHPNS 78
                          90
                  ....*....|....*.
gi 157830769  476 --FDLGPGEVGVWAYS 489
Cdd:pfam02806  79 ltLTLPPLSALVLKVE 94
PLN02950 PLN02950
4-alpha-glucanotransferase
572-663 4.09e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 47.02  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 572 FEVLTNDQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKaiGPMFNQVVysYPTWYIDVSVPEGK-TIEFKFIKKDS 650
Cdd:PLN02950 145 NKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDD--GLKLNYTG--DSIWEADCLVPKSDfPIKYKYALQTA 220
                         90
                 ....*....|...
gi 157830769 651 QGNVTWESGSNHV 663
Cdd:PLN02950 221 EGLVSLELGVNRE 233
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
8-396 0e+00

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: 601.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   8 NFTSDVVYQIVVDRFVDGNTSNNPSG--ALFSSGCTNLRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVFSVMN 85
Cdd:cd11320    1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  86 DAsGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsYMENGRLYDNGTLLGGYTN 165
Cdd:cd11320   79 GG-GNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYPN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 166 DANMYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN 244
Cdd:cd11320  153 DDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 245 YRPVFTFGEWFL-SENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11320  233 KKPVFTFGEWFLgSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNH 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157830769 324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGN----GDPNNRKMMSSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11320  313 DMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
10-397 1.07e-89

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: 283.38  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  10 TSDVVYQIVVDRFVDGNTSNNPSGA--LFSSGCTNLRKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvMNDA 87
Cdd:cd11339    1 REETIYFVMTDRFYDGDPSNDNGGGdgDPRSNPTDNGPYHGGDFKGLIDKLD--YIKDLGFTAIWITPVVKN----RSVQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  88 SGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasetnpsymengrlydngtllggytnda 167
Cdd:cd11339   75 AGSAGYHGYWGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG----------------------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 168 nmyfhhnggttfssledgiyrnlfdlaDLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN--- 244
Cdd:cd11339  126 ---------------------------DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQaag 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 245 YRPVFTFGEWFLSENEVDANnhYFANESGMSLLDFRFGQKLRQVLRNNS-----DNWYGFNQMIQDTASaydevldQVTF 319
Cdd:cd11339  179 KPDFFMFGEVYDGDPSYIAP--YTTTAGGDSVLDFPLYGAIRDAFAGGGsgdllQDLFLSDDLYNDATE-------LVTF 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 320 IDNHDMDRFM-----IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM------------SSFNKNTR 382
Cdd:cd11339  250 LDNHDMGRFLsslkdGSADGTARLALALALLFTSRGIPCIYYGTEQGFTGGGDPDNGRRNmfastgdltsadDNFDTDHP 329
                        410
                 ....*....|....*
gi 157830769 383 AYQVIQKLSSLRRNN 397
Cdd:cd11339  330 LYQYIARLNRIRRAY 344
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
49-368 1.99e-88

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: 279.63  E-value: 1.99e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   49 GDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:pfam00128   1 GDLQGIIEKLD--YLKELGVTAIWLSPIFDS----------PQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  129 IIDFAPNHTSPASE-TNPSYMENGRLYDNGTLL---GGYTNDANMYFhHNGGTTFS----SLEDGIYRNLFDLADLNHQN 200
Cdd:pfam00128  69 ILDLVVNHTSDEHAwFQESRSSKDNPYRDYYFWrpgGGPIPPNNWRS-YFGGSAWTydekGQEYYLHLFVAGQPDLNWEN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  201 PVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPF----------GWQKSLMDEIDNY----RPVFTFGEWFLSENE---VDA 263
Cdd:pfam00128 148 PEVRNELYDVVRFWLDKGIDGFRIDVVKHISKvpglpfenngPFWHEFTQAMNETvfgyKDVMTVGEVFHGDGEwarVYT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  264 NNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAY-DEVLDQVTFIDNHDMDRFMID-GGDPRKVDMA 341
Cdd:pfam00128 228 TEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDALpDTNGWNFTFLGNHDQPRFLSRfGDDRASAKLL 307
                         330       340
                  ....*....|....*....|....*..
gi 157830769  342 LAVLLTSRGVPNIYYGTEQYMTGNGDP 368
Cdd:pfam00128 308 AVFLLTLRGTPYIYQGEEIGMTGGNDP 334
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
11-396 8.85e-69

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: 230.18  E-value: 8.85e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  11 SDVVYQIVVDRFVDGNTSN-NPSGALFSSGCTNLRKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvmndASG 89
Cdd:cd11340    3 SDVIYLIMPDRFANGDPSNdSVPGMLEKADRSNPNGRHGGDIQGIIDHLD--YLQDLGVTAIWLTPLLEN-------DMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  90 SASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAsetNPsYMENGRLYD--NGTLLGGYTNda 167
Cdd:cd11340   74 SYSYHGYAATDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSE---HW-WMKDLPTKDwiNQTPEYTQTN-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 168 nmyfhHNggttFSSLEDgIY------RNLFD------LADLNHQNPVIDRYLKDAVKMWIDM-GIDGIRMD----AVKHM 230
Cdd:cd11340  148 -----HR----RTALQD-PYasqadrKLFLDgwfvptMPDLNQRNPLVARYLIQNSIWWIEYaGLDGIRVDtypySDKDF 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 231 PFGWQKSLMDEIDNYrpvFTFGE-WFLSENEV----DANNHYFANESGM-SLLDFRFGQKLRQVLrnNSDNWYG------ 298
Cdd:cd11340  218 MSEWTKAIMEEYPNF---NIVGEeWSGNPAIVaywqKGKKNPDGYDSHLpSVMDFPLQDALRDAL--NEEEGWDtglnrl 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 299 FNQMIQDtaSAYDEVLDQVTFIDNHDMDRFM-IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTG---NGDPNNRKMM 374
Cdd:cd11340  293 YETLAND--FLYPDPNNLVIFLDNHDTSRFYsQVGEDLDKFKLALALLLTTRGIPQLYYGTEILMKGtkkKDDGAIRRDF 370
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 157830769 375 ---------SSFNKNTR------AYQVIQKLSSLRRN 396
Cdd:cd11340  371 pggwagdkvNAFTAAGRtpeqneAFDFVRKLLNWRKN 407
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
13-396 1.03e-64

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: 218.59  E-value: 1.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNPSgalfssgCTNL-RKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENVFSvmNDASGSA 91
Cdd:cd11319   10 SIYQVLTDRFARTDGSSTAP-------CDTAdRTYCGGTWKGIINKLD--YIQGMGFDAIWISPIVKNIEG--NTAYGEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  92 sYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGTllggytndanmYF 171
Cdd:cd11319   79 -YHGYWAQDLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDYSSFVPFNDSS-----------YY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 172 HH----NGGTTFSSLEDG-IYRNLFDLADLNHQNPVIDRYLKDAVKMWI-DMGIDGIRMDAVKHMPFGWQKSLMDEIDny 245
Cdd:cd11319  147 HPycwiTDYNNQTSVEDCwLGDDVVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLRIDTAKHVRKDFWPGFVEAAG-- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 246 rpVFTFGEWFlsenevDANNHYFAN--ESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11319  225 --VFAIGEVF------DGDPNYVCPyqNYLDGVLNYPLYYPLVDAFQSTKGSMSALVDTINSVQSSCKDPTLLGTFLENH 296
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157830769 324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM--SSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11319  297 DNPRFLSYTSDQALAKNALAFTLLSDGIPIIYYGQEQGFNGGNDPYNREALwlSGYDTSSPLYKFIKTLNAIRKA 371
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
13-404 1.99e-62

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: 212.73  E-value: 1.99e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYC--------------GGDWQGIINKIndGYLTDMGVTAIWISqPVe 78
Cdd:cd11338    3 VFYQIFPDRFANGDPSNDPKGGEYNYFGWPDLPDYpppwggeptrrdfyGGDLQGIIEKL--DYLKDLGVNAIYLN-PI- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  79 nvFSvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRlydngt 158
Cdd:cd11338   79 --FE-------APSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGE------ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 159 lLGGYtndaNMYFHHNGGTTFSSLEDGIYR---NLFDLADLNHQNPVIDRYLKDAVKMWIDMG-IDGIRMDAVKHMPFGW 234
Cdd:cd11338  144 -SSAY----QDWFSIYYFWPYFTDEPPNYEswwGVPSLPKLNTENPEVREYLDSVARYWLKEGdIDGWRLDVADEVPHEF 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 235 QKSLMDEIDNYRP-VFTFGE-W-----FLSENEVDAN-NHYFANesgmSLLDFrfgqklrqvLRNNSDNWYGFNQMIQDT 306
Cdd:cd11338  219 WREFRKAVKAVNPdAYIIGEvWedarpWLQGDQFDSVmNYPFRD----AVLDF---------LAGEEIDAEEFANRLNSL 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 307 ASAY-DEVLD-QVTFIDNHDMDRFM-IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM--SSFNKNT 381
Cdd:cd11338  286 RANYpKQVLYaMMNLLDSHDTPRILtLLGGDKARLKLALALQFTLPGAPCIYYGDEIGLEGGKDPDNRRPMpwDEEKWDQ 365
                        410       420
                 ....*....|....*....|...
gi 157830769 382 RAYQVIQKLSSLRRNNPALAYGD 404
Cdd:cd11338  366 DLLEFYKKLIALRKEHPALRTGG 388
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
578-678 2.06e-61

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99882 [Multi-domain]  Cd Length: 101  Bit Score: 200.09  E-value: 2.06e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWE 657
Cdd:cd05807    1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80
                         90       100
                 ....*....|....*....|.
gi 157830769 658 SGSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05807   81 SGSNHTYTAPSSTTGTIRVNW 101
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
12-403 6.84e-56

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: 195.49  E-value: 6.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  12 DVVYQIVVDRFVDGNtsnnpsgalfssgctnlrkycG---GDWQGIINKINdgYLTDMGVTAIWISqPVenvfsvmndaS 88
Cdd:cd11316    1 GVFYEIFVRSFYDSD---------------------GdgiGDLNGLTEKLD--YLNDLGVNGIWLM-PI----------F 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  89 GSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS---P-----ASETNPSYmengRLY-----D 155
Cdd:cd11316   47 PSPSYHGYDVTDYYAIEPDYGTMEDFERLIAEAHKRGIKVIIDLVINHTSsehPwfqeaASSPDSPY----RDYyiwadD 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 156 NGTLLGGYtnDANMYFHHNGGttfssledGIYRNLFD--LADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFG 233
Cdd:cd11316  123 DPGGWSSW--GGNVWHKAGDG--------GYYYGAFWsgMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYEN 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 234 ------------WQKSLMDEIDNYRP-VFTFGEWFLSENEVDAnnhYFANESGmSLLDFRFGQKLRQVLRNNSDNwYGFN 300
Cdd:cd11316  193 gegqadqeenieFWKEFRDYVKSVKPdAYLVGEVWDDPSTIAP---YYASGLD-SAFNFDLAEAIIDSVKNGGSG-AGLA 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 301 QMIQDTASAYDEVLDQV---TFIDNHDMDRFMID-GGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNG-DPNNRKMMS 375
Cdd:cd11316  268 KALLRVYELYAKYNPDYidaPFLSNHDQDRVASQlGGDEAKAKLAAALLLTLPGNPFIYYGEEIGMLGSKpDENIRTPMS 347
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157830769 376 -----------------SFNKNTRA-----------YQVIQKLSSLRRNNPALAYG 403
Cdd:cd11316  348 wdadsgagfttwipprpNTNATTASveaqeadpdslLNHYKRLIALRNEYPALARG 403
AmyA COG0366
Glycosidase [Carbohydrate transport and metabolism];
13-433 2.99e-53

Glycosidase [Carbohydrate transport and metabolism];


Pssm-ID: 223443 [Multi-domain]  Cd Length: 505  Bit Score: 190.97  E-value: 2.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNPSgalfssgctnlrKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVfsvmndasgsAS 92
Cdd:COG0366    2 VIYQIYPDRFADSNGSNGPD------------YDGGGDLKGITEKL--DYLKELGVDAIWLSPIFESP----------QA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  93 YHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNG-----TLLGGYTNDA 167
Cdd:COG0366   58 DHGYDVSDYTKVDPHFGTEEDFKELVEEAHKRGIKVILDLVFNHTSDEHPWFKEARSSKPNPKRSdyyiwRDPDPDGTPP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 168 NMYFHHNGGTTFSSLEDG-IYRNLFD--LADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM--PFG--------- 233
Cdd:COG0366  138 NNWFSVFGGDAWTWGNTGeYYLHLFSseQPDLNWENPEVREELLDVVKFWLDKGVDGFRLDAAKHIskDFGlppseenlt 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 234 --------WQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNsdNWYGFNQMIQD 305
Cdd:COG0366  218 fleeiheyLREENPDVLIYGEAITDVGEAPGAVKEDFADNTSFTNPELSMLFDFSHVGLDFEALAPL--DAEELKEILAD 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 306 TASAYDEVLDQ-VTFIDNHDMDRFM-----IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMS---- 375
Cdd:COG0366  296 WPLAVNLNDGWnNLFLSNHDQPRLLsrfgdDVGGRDASAKLLAALLFLLPGTPFIYYGDELGLTNFKDPPIKYYDDveld 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 376 -----------------------SFNKNTRA-------------------------YQVIQKLSSLRR-NNPALAYGDTE 406
Cdd:COG0366  376 siillsrdgcrtpmpwdenglnaGFTGGKPWlsvnpndllginveaqladelpeslFNFYRRLIALRKqHSALLANGEDF 455
                        490       500
                 ....*....|....*....|....*....
gi 157830769 407 QRWINGD--VYVYERQFGKDVVLVAVNRS 433
Cdd:COG0366  456 VLLADDDpsLLAFLRESGGETLLVVNNLS 484
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
13-393 1.78e-49

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: 179.05  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDG-------NTSNNPSGALFSSGCTN---LRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVfs 82
Cdd:cd11352    1 VLYFLLVDRFSDGkerprplFDGNDPAVATWEDNFGWesqGQRFQGGTLKGVRSKL--GYLKRLGVTALWLSPVFKQR-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  83 vmndaSGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-----PASETNPSYME---NGRLY 154
Cdd:cd11352   77 -----PELETYHGYGIQNFLDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSGdvfsyDDDRPYSSSPGyyrGFPNY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 155 DNGTLLGGYTNDANMYFHHNGG---------TTFS-----SLEDG----IYRNLFDLADLNHQNPVID----RYLKDAVK 212
Cdd:cd11352  152 PPGGWFIGGDQDALPEWRPDDAiwpaelqnlEYYTrkgriRNWDGypeyKEGDFFSLKDFRTGSGSIPsaalDILARVYQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 213 MWI---DmgIDGIRMDAVKHMPFGWQKSLMDEIDNY------RPVFTFGEWflsenevdANNHYFANESGMSL------L 277
Cdd:cd11352  232 YWIayaD--IDGFRIDTVKHMEPGAARYFCNAIKEFaqsigkDNFFLFGEI--------TGGREAAAYEDLDVtgldaaL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 278 DFRFGQ-KLRQVLRNNSD-NWY--GFNQMIQDTASAYDEVLDQ-VTFIDNHDM------DRFMIDGGDPRKVDMALAVLL 346
Cdd:cd11352  302 DIPEIPfKLENVAKGLAPpAEYfqLFENSKLVGMGSHRWYGKFhVTFLDDHDQvgrfykKRRAADAAGDAQLAAALALNL 381
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157830769 347 TSRGVPNIYYGTEQYMTGNGD---------------PNNRKMMSSFNKNTRAYQVIQKLSSL 393
Cdd:cd11352  382 FTLGIPCIYYGTEQGLDGSGDsdryvreamfggdfgAFRSRGRHFFNEEHPIYRRIAALSEL 443
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
13-356 1.09e-46

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: 166.19  E-value: 1.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENVfsvmndaSGSAS 92
Cdd:cd00551    1 VIYQLFPDRFTDGDSSGG---------------DGGGDLKGIIDKLD--YLKDLGVTAIWLTPIFESP-------EYDGY 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  93 YHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHtspasetnpsymengrlydngtllggytndanmyfh 172
Cdd:cd00551   57 DKDDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH------------------------------------ 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 173 hnggttfssledgiyrnlfdladlnhqnpVIDRYlkdavkmWIDMGIDGIRMDAVKHMPFGWQKSLMDEI-----DNYRP 247
Cdd:cd00551  101 -----------------------------DILRF-------WLDEGVDGFRLDAAKHVPKPEPVEFLREIrkdakLAKPD 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 248 VFTFGEWFlsENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDtasaYDEVLDQVTFIDNHDMDR 327
Cdd:cd00551  145 TLLLGEAW--GGPDELLAKAGFDDGLDSVFDFPLLEALRDALKGGEGALAILAALLLL----NPEGALLVNFLGNHDTFR 218
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 157830769 328 FM------IDGGDPRKVDMALAVLLTSRGVPNIYY 356
Cdd:cd00551  219 LAdlvsykIVELRKARLKLALALLLTLPGTPMIYY 253
Aamy smart00642
Alpha-amylase domain;
16-139 4.06e-38

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 139.00  E-value: 4.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769    16 QIVVDRFVDGNTSNnpsgalfssgctnlrkycGGDWQGIINKINdgYLTDMGVTAIWISQPVENVfsvmndaSGSASYHG 95
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESP-------QGYPSYHG 53
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 157830769    96 YWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:smart00642  54 YDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTSD 97
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
42-403 6.32e-38

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: 143.84  E-value: 6.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  42 NLRKYCG-GDWQGIINKIndGYLTDMGVTAIWIS--QPVenvfSVMNDASGSASYhgYWARDFKKPNPFFGTLSDFQRLV 118
Cdd:cd11313   11 NVRQFTPeGTFKAVTKDL--PRLKDLGVDILWLMpiHPI----GEKNRKGSLGSP--YAVKDYRAVNPEYGTLEDFKALV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 119 DAAHAKGIKVIIDFAPNHTSPASETNPSYMEngrlydngtllggytndanmYFHHNggttfsslEDGIYRNLF----DLA 194
Cdd:cd11313   83 DEAHDRGMKVILDWVANHTAWDHPLVEEHPE--------------------WYLRD--------SDGNITNKVfdwtDVA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 195 DLNHQNPVIDRYLKDAVKMWIDM-GIDGIRMDAVKHMPFGWQKSLMDEIDNYRP-VFTFGEW-----FLSENEVDAnnHY 267
Cdd:cd11313  135 DLDYSNPELRDYMIDAMKYWVREfDVDGFRCDVAWGVPLDFWKEARAELRAVKPdVFMLAEAeprddDELYSAFDM--TY 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 268 fanesgmsllDFRFGQKLRQVLRNNSDnwygfnqmiqdtASAYDEVLDQ-----------VTFIDNHDMDRFMIDGGDPR 336
Cdd:cd11313  213 ----------DWDLHHTLNDVAKGKAS------------ASDLLDALNAqeagypknavkMRFLENHDENRWAGTVGEGD 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157830769 337 KVDMALAVLLTSRGVPNIYYGTEQYMTG-----NGDPnnrkmmSSFNKNTRAYQVIQKLSSLRRNNPALAYG 403
Cdd:cd11313  271 ALRAAAALSFTLPGMPLIYNGQEYGLDKrpsffEKDP------IDWTKNHDLTDLYQKLIALKKENPALRGG 336
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
13-436 1.45e-37

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 148.23  E-value: 1.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNN-PSGALF--SSGCTNLRK--------------YCGGDWQGIINKIndGYLTDMGVTAIWISq 75
Cdd:PRK10785 123 VFYQIFPDRFARSLPREAvQDHVYYhhAAGQEIILRdwdepvtaqaggstFYGGDLDGISEKL--PYLKKLGVTALYLN- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  76 PVenvFSvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasETNPSYMENGRlyd 155
Cdd:PRK10785 200 PI---FT-------APSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTG---DSHPWFDRHNR--- 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 156 ngTLLGGYTNDA----NMYFHHNGGTTFSSLedGIYrnlfDLADLNHQNP-VIDR-YLKD--AVKMWID--MGIDGIRMD 225
Cdd:PRK10785 264 --GTGGACHHPDspwrDWYSFSDDGRALDWL--GYA----SLPKLDFQSEeVVNEiYRGEdsIVRHWLKapYNIDGWRLD 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 226 AVkHM-------------------------P--------FG----W-QKSLMDEIDNYRPvFTFGEW-FLSENEVDANNH 266
Cdd:PRK10785 336 VV-HMlgegggarnnlqhvagitqaakeenPeayvlgehFGdarqWlQADVEDAAMNYRG-FAFPLRaFLANTDIAYHPQ 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 267 YFANESGMSLLD-FR----FGQKLRQvlrnnsdnwygFNQMiqdtasaydevldqvtfiDNHDMDRFM-IDGGDPRKVDM 340
Cdd:PRK10785 414 QIDAQTCAAWMDeYRaglpHQQQLRQ-----------FNQL------------------DSHDTARFKtLLGGDKARMPL 464
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 341 ALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM----SSFNKNTRAYqvIQKLSSLRRNNPALAYGDTEQRWINGDVYV 416
Cdd:PRK10785 465 ALVWLFTWPGVPCIYYGDEVGLDGGNDPFCRKPFpwdeAKQDGALLAL--YQRMIALRKKSQALRRGGCQVLYAEGNVVV 542
                        490       500
                 ....*....|....*....|
gi 157830769 417 YERQFGKDVVLVAVNRSSSS 436
Cdd:PRK10785 543 FARVLQQQRVLVAINRGEAC 562
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
62-405 9.20e-36

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: 137.66  E-value: 9.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISqPVenvFSvmndasgsASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTspas 141
Cdd:cd11337   36 HLKELGCNALYLG-PV---FE--------SDSHGYDTRDYYRIDRRLGTNEDFKALVAALHERGIRVVLDGVFNHV---- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 142 etnpsymenGRlydnGTLLGGYtndanmyfhhnggttfssledgiyrnlFDLADLNHQNPVIDRYLKDAVKMWIDMG-ID 220
Cdd:cd11337  100 ---------GR----DFFWEGH---------------------------YDLVKLNLDNPAVVDYLFDVVRFWIEEFdID 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 221 GIRMDAVKHMPFGWQKSLMDEIDNYRPVFtfgeWFLSEneV---DANnhYFANESGM--------------SLLDFRFGQ 283
Cdd:cd11337  140 GLRLDAAYCLDPDFWRELRPFCRELKPDF----WLMGE--VihgDYN--RWVNDSMLdsvtnyelykglwsSHNDHNFFE 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 284 --KLRQVLRNNSDNWYGFNQMiqdtasaydevldqvTFIDNHDMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQY 361
Cdd:cd11337  212 iaHSLNRLFRHNGLYRGFHLY---------------TFVDNHDVTRIASILGDKAHLPLAYALLFTMPGIPSIYYGSEWG 276
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157830769 362 MTG---NGDPNNRKMM-----SSFNKNTRAYQVIQKLSSLRRNNPALAYGDT 405
Cdd:cd11337  277 IEGvkeEGSDADLRPLplrpaELSPLGNELTRLIQALIALRRRSPALCYGSY 328
CBM_20 pfam00686
Starch binding domain;
580-676 1.52e-34

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 126.25  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIgPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:pfam00686   1 VSVTFNVN-ATTQYGQSVYIVGSIPELGNWNPKKAI-ALSASEYSSYPLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESG 78
                          90
                  ....*....|....*..
gi 157830769  660 SNHVYTTPTNTTGKIIV 676
Cdd:pfam00686  79 PNRSYTVPASGASTTTT 95
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
13-359 2.80e-34

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: 136.15  E-value: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNtsnnpsgalfSSGCtnlrkycgGDWQGIINKINdgYLTDMGVTAIWIS--QPvenvfSVMNDAsgs 90
Cdd:cd11334    6 VIYQLDVRTFMDSN----------GDGI--------GDFRGLTEKLD--YLQWLGVTAIWLLpfYP-----SPLRDD--- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  91 asyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPA---------------------SETNPSYME 149
Cdd:cd11334   58 ----GYDIADYYGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTSDQhpwfqaarrdpdspyrdyyvwSDTPPKYKD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 150 NGRLYdNGTLLGGYTND--ANMYFHHnggtTFSSLEdgiyrnlfdlADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAV 227
Cdd:cd11334  134 ARIIF-PDVEKSNWTWDevAGAYYWH----RFYSHQ----------PDLNFDNPAVREEILRIMDFWLDLGVDGFRLDAV 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 228 KHM-------------PFGWQKSLMDEIDNYRPvftfGEWFLSENEVDANN--HYFANESGMSLL-DFRFGQKLRQVLRN 291
Cdd:cd11334  199 PYLieregtncenlpeTHDFLKRLRAFVDRRYP----DAILLAEANQWPEEvrEYFGDGDELHMAfNFPLNPRLFLALAR 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 292 nsdnwygfnqmiQDTASAYDeVLDQ----------VTFIDNHD---------------MDRFMID--------------- 331
Cdd:cd11334  275 ------------EDAFPIID-ALRQtppipegcqwANFLRNHDeltlemltdeerdyvYAAFAPDprmriynrgirrrla 341
                        410       420       430
                 ....*....|....*....|....*....|.
gi 157830769 332 ---GGDPRKVDMALAVLLTSRGVPNIYYGTE 359
Cdd:cd11334  342 pmlGGDRRRIELAYSLLFSLPGTPVIYYGDE 372
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
495-576 4.00e-34

IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown.


Pssm-ID: 238338 [Multi-domain]  Cd Length: 81  Bit Score: 124.76  E-value: 4.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 495 PIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYdNFEV 574
Cdd:cd00604    1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGY-NFEV 79

                 ..
gi 157830769 575 LT 576
Cdd:cd00604   80 LT 81
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
581-678 1.38e-33

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 123.56  E-value: 1.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 581 SVRFVVNNaTTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQvvySYPTWYIDVSVP--EGKTIEFKFIKKDSQGNVTWES 658
Cdd:cd05467    1 QVRFQVRC-TTQFGQSVYVVGSHPELGNWDPAKALRLNTSN---SYPLWTGEIPLPapEGQVIEYKYVIVDDDGNVQWES 76
                         90       100
                 ....*....|....*....|
gi 157830769 659 GSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05467   77 GSNRVLTVPSTSSLIVVDDW 96
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
13-374 2.29e-32

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: 130.27  E-value: 2.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSnnpsgalfssgctnlrkycG-GDWQGIINKIndGYLTDMGVTAIWISqPVenvF-SVMNDasgs 90
Cdd:cd11333    4 VVYQIYPRSFKDSNGD-------------------GiGDLPGIISKL--DYLKDLGVDAIWLS-PI---YpSPQVD---- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  91 asyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS---P------ASETNPsYM--------ENGRL 153
Cdd:cd11333   55 ---NGYDISDYRAIDPEFGTMEDFDELIKEAHKRGIKIIMDLVVNHTSdehPwfqesrSSRDNP-YRdyyiwrdgKDGKP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 154 YDN-GTLLGG----YTNDANMYFHHnggttfssledgiyrnLFDL--ADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDA 226
Cdd:cd11333  131 PNNwRSFFGGsaweYDPETGQYYLH----------------LFAKeqPDLNWENPEVRQEIYDMMRFWLDKGVDGFRLDV 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 227 VKHM----------------PFGWQ------------KSLMDEIDNYRPVFTFGE-WFLSENE----VDANNHYF----- 268
Cdd:cd11333  195 INLIskdpdfpdappgdgdgLSGHKyyangpgvheylQELNREVFSKYDIMTVGEaPGVDPEEalkyVGPDRGELsmvfn 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 269 --------ANESGMSLLDFRFgQKLRQVLrnnsDNWYgfNQMIQDTASAYdevldqvtFIDNHDM----DRFmidgGDPR 336
Cdd:cd11333  275 fehldldyGPGGKWKPKPWDL-EELKKIL----SKWQ--KALQGDGWNAL--------FLENHDQprsvSRF----GNDG 335
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 157830769 337 KVDM----ALA-VLLTSRGVPNIYYGTEQYMTgNGDPNNRKMM 374
Cdd:cd11333  336 EYRVesakMLAtLLLTLRGTPFIYQGEEIGMT-NSRDNARTPM 377
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
579-680 1.06e-31

Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99893  Cd Length: 103  Bit Score: 118.86  E-value: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 579 QVSVRFVVNNA-TTNLGQNIYIVGNVYELGNW--DTSKAIGPMFNQvvySYPTWYIDVSVPEGKTIEFKFIKKDSQGNVT 655
Cdd:cd05820    2 QIPVIFTVQNTpETAPGEFLYLTGSVPELGNWstSTDQAVGPLLCP---NWPDWFVVASVPAGTYIEFKFLKAPADGTGT 78
                         90       100
                 ....*....|....*....|....*
gi 157830769 656 WESGSNHVYTTPTNTTGKIIVDWQN 680
Cdd:cd05820   79 WEGGSNHAYTTPSGGTGTVTVTWQR 103
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-363 3.34e-31

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: 127.06  E-value: 3.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNtsnnpsgalfSSGCtnlrkycgGDWQGIINKIndGYLTDMGVTAIWISqPVenvF-SVMNDAsgsa 91
Cdd:cd11331    7 VIYQIYPRSFQDSN----------GDGV--------GDLRGIISRL--DYLSDLGVDAVWLS-PI---YpSPMADF---- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  92 syhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS---P------ASETNPS---YmengrLYDNGTL 159
Cdd:cd11331   59 ---GYDVSDYCGIDPLFGTLEDFDRLVAEAHARGLKVILDFVPNHTSdqhPwflesrSSRDNPKrdwY-----IWRDPAP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 160 LGGYTNDANMYFhhnGGT--TFSSLEDGIYRNLF--DLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMpfGWQ 235
Cdd:cd11331  131 DGGPPNNWRSEF---GGSawTWDERTGQYYLHAFlpEQPDLNWRNPEVRAAMHDVLRFWLDRGVDGFRVDVLWLL--IKD 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 236 KSLMDEIDN--YRPVFTFGEWFL---SENEVDAnnHYFAneSGMSLLDFRFGQK---------LRQVLRnnsdnWYG--- 298
Cdd:cd11331  206 PQFRDNPPNpdWRGGMPPHERLLhiyTADQPET--HEIV--REMRRVVDEFGDRvligeiylpLDRLVA-----YYGagr 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 299 ------FN----------QMIQDTASAYDEVLDQVT----FIDNHDMDRFMIDGGdPRKVDMALAVLLTSRGVPNIYYGT 358
Cdd:cd11331  277 dglhlpFNfhlislpwdaAALARAIEEYEAALPAGAwpnwVLGNHDQPRIASRVG-PAQARVAAMLLLTLRGTPTLYYGD 355

                 ....*
gi 157830769 359 EQYMT 363
Cdd:cd11331  356 ELGME 360
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
55-404 2.84e-30

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: 122.67  E-value: 2.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  55 INKIND--GYLTDMGVTAIWISqPVenvFSvmndasgsASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDF 132
Cdd:cd11353   29 ILKLEDwiPHLKKLGINAIYFG-PV---FE--------SDSHGYDTRDYYKIDRRLGTNEDFKAVCKKLHENGIKVVLDG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 133 APNHTS---PASETNPSYMENGRlydngtllggYTNdanmYFHhngGTTF---SSLEDGIY----RNLFDLADLNHQNPV 202
Cdd:cd11353   97 VFNHVGrdfFAFKDVQENRENSP----------YKD----WFK---GVNFdgnSPYNDGFSyegwEGHYELVKLNLHNPE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 203 IDRYLKDAVKMWID-MGIDGIRMDAVKHMPFGWQKSLMDEIDNYRPVFtfgeWFLSenEV---DANnhYFANE------- 271
Cdd:cd11353  160 VVDYLFDAVRFWIEeFDIDGLRLDVADCLDFDFLRELRDFCKSLKPDF----WLMG--EVihgDYN--RWANDemldsvt 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 272 ---------SGMSLLD-FRFGQKLRQvlRNNSDNWYGFNQMiqdtasaydevldqVTFIDNHDMDRFMIDGGDPRKVDMA 341
Cdd:cd11353  232 nyecykglySSHNDHNyFEIAHSLNR--QFGLEGIYRGKHL--------------YNFVDNHDVNRIASILKNKEHLPPI 295
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 342 LAVLLTSRGVPNIYYGTEQYMTG----NGDPNNR---KMMSSFNKNTRAYQVIQKLSSLRRNNPALAYGD 404
Cdd:cd11353  296 YALLFTMPGIPSIYYGSEWGIEGvkgnGSDAALRpalDEPELSGENNELTDLIAKLARIRRASPALCYGS 365
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
49-400 1.86e-29

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: 120.84  E-value: 1.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  49 GDWQGIINKINdgYLTDMGVTAIWIsQPVENVfsVMNDASGSASYHgYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:cd11350   30 GDFKGVIDKLD--YLQDLGVNAIEL-MPVQEF--PGNDSWGYNPRH-YFA-----LDKAYGTPEDLKRLVDECHQRGIAV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 129 IIDFAPNHtspASETNPSYmengRLYDNGtllGGYTNDANMYFHHNGGTTFSSledgiyrnlfDLADLNHQNPVIDRYLK 208
Cdd:cd11350   99 ILDVVYNH---AEGQSPLA----RLYWDY---WYNPPPADPPWFNVWGPHFYY----------VGYDFNHESPPTRDFVD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 209 DAVKMWID-MGIDGIRMDAVKHMpfgWQK-SLMDEIDNYRP-VFTFGEWFLSENEVDANNHYF-------------ANES 272
Cdd:cd11350  159 DVNRYWLEeYHIDGFRFDLTKGF---TQKpTGGGAWGGYDAaRIDFLKRYADEAKAVDKDFYViaehlpdnpeeteLATY 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 273 GMSLLDFRFGQKLRQVLRNNSDN------WYGFNQMIQDTASAydevldqVTFIDNHDMDRFM------------IDGGD 334
Cdd:cd11350  236 GMSLWGNSNYSFSQAAMGYQGGSllldysGDPYQNGGWSPKNA-------VNYMESHDEERLMyklgaygngnsyLGINL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157830769 335 P---RKVDMALAVLLTSRGVPNIY------YGTEQYMTGNGDPNNRKMMSSF---NKNTRAYQVIQKLSSLRRNNPAL 400
Cdd:cd11350  309 EtalKRLKLAAAFLFTAPGPPMIWqggefgYDYSIPEDGRGTTLPKPIRWDYlydPERKRLYELYRKLIKLRREHPAL 386
malS PRK09505
alpha-amylase; Reviewed
14-429 8.64e-29

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 122.08  E-value: 8.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  14 VYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENVFS-VMNDASGSA- 91
Cdd:PRK09505 192 VYFVLTDRFENGDPSNDHSYGRHKDGMQEIGTFHGGDLRGLTEKLD--YLQQLGVNALWISSPLEQIHGwVGGGTKGDFp 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  92 --SYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGT----LLGGYTN 165
Cdd:PRK09505 270 hyAYHGYYTLDWTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTGYATLADMQEFQFGALYLSGDenkkTLGERWS 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 166 D----ANMYFHH------------------------NGGTTFSSLEDGIYRNLFDLADL--NHQNPV------------- 202
Cdd:PRK09505 350 DwqpaAGQNWHSfndyinfsdstawdkwwgkdwirtDIGDYDNPGFDDLTMSLAFLPDIktESTQASglpvfyankpdtr 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 203 ---IDRYLK-DAVKMWI-----DMGIDGIRMDAVKHM-PFGWQKsLMDEIDNyrpvfTFGEW-------------FLSEN 259
Cdd:PRK09505 430 akaIDGYTPrDYLTHWLsqwvrDYGIDGFRVDTAKHVeLPAWQQ-LKQEASA-----ALAEWkkanpdkalddapFWMTG 503
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 260 EVDAN----NHYFANesGM-SLLDFRF-GQKLRQV--LRNNSDNWYGFNQMIQDtasaydevLDQVTFIDNHDMDRFMID 331
Cdd:PRK09505 504 EAWGHgvmkSDYYRH--GFdAMINFDYqEQAAKAVdcLAQMDPTYQQMAEKLQD--------FNVLSYLSSHDTRLFFEG 573
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 332 GGDPRKVDMALAVLLTSRGVPNIYYGTE--QYMTGNGDPNNRKMMSSFN----KNTRAYQVI--QKLSSLRRNNPALAYG 403
Cdd:PRK09505 574 GQSYAKQRRAAELLLLAPGAVQIYYGDEsaRPFGPTGSDPLQGTRSDMNwqevSGKSAALLAhwQKLGQFRARHPAIGAG 653
                        490       500
                 ....*....|....*....|....*..
gi 157830769 404 dtEQRWI-NGDVYVYERQFGKDVVLVA 429
Cdd:PRK09505 654 --KQTTLsLKQYYAFVREHGDDKVMVV 678
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
49-230 2.34e-28

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: 118.87  E-value: 2.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  49 GDWQGIINKIndGYLTDMGVTAIWISQPVEnvfSVMNDAsgsasyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:cd11328   27 GDLKGITEKL--DYFKDIGIDAIWLSPIFK---SPMVDF-------GYDISDFTDIDPIFGTMEDFEELIAEAKKLGLKV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 129 IIDFAPNHTSPASE-------TNPSYME-----NGRLYDNGTLL---------GG----YTNDANMYFHHNggttFSSle 183
Cdd:cd11328   95 ILDFVPNHSSDEHEwfqksvkRDEPYKDyyvwhDGKNNDNGTRVppnnwlsvfGGsawtWNEERQQYYLHQ----FAV-- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157830769 184 dgiyrnlfDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM 230
Cdd:cd11328  169 --------KQPDLNYRNPKVVEEMKNVLRFWLDKGVDGFRIDAVPHL 207
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
580-677 4.09e-28

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 108.51  E-value: 4.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:cd05811    7 VAVTFNER-VTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKESDGSVTWESD 85
                         90
                 ....*....|....*...
gi 157830769 660 SNHVYTTPTNTTGKIIVD 677
Cdd:cd05811   86 PNRSYTVPSGCGTTATVD 103
CBM_2 smart01065
Starch binding domain;
580-668 5.09e-28

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 107.82  E-value: 5.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgPMfNQVVYSYPTWYIDVSVPE-GKTIEFKFIKKDSQGNVTWES 658
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAV-PL-SPDTDGYPLWKGTVSLPPaGTTIEYKYVKVDEDGSVTWES 78
                           90
                   ....*....|
gi 157830769   659 GSNHVYTTPT 668
Cdd:smart01065  79 GPNRRLTVPE 88
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-359 6.95e-28

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: 117.36  E-value: 6.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNtsnnpsgalfssgctnlrkycG---GDWQGIINKINdgYLTDMGVTAIWISqPVenvF-SVMNDas 88
Cdd:cd11330    7 VIYQIYPRSFLDSN---------------------GdgiGDLPGITEKLD--YIASLGVDAIWLS-PF---FkSPMKD-- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  89 gsasyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP---------ASETNPS---YM-----ENG 151
Cdd:cd11330   58 -----FGYDVSDYCAVDPLFGTLDDFDRLVARAHALGLKVMIDQVLSHTSDqhpwfeesrQSRDNPKadwYVwadpkPDG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 152 RLYDNG-TLLGG----YTNDANMYFHHNggttFssledgiyrnLFDLADLNHQNP-VIDRYLkDAVKMWIDMGIDGIRMD 225
Cdd:cd11330  133 SPPNNWlSVFGGsawqWDPRRGQYYLHN----F----------LPSQPDLNFHNPeVQDALL-DVARFWLDRGVDGFRLD 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 226 AVK-HM------------------------PFGWQ---------------KSLMDEIDNYRPVFTFGEwFLSENEVDANN 265
Cdd:cd11330  198 AVNfYMhdpalrdnpprppderedgvaptnPYGMQlhihdksqpenlaflERLRALLDEYPGRFLVGE-VSDDDPLEVMA 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 266 HYFANESGM------SLLDFRFGQKlrqVLRNnsdnwygfnqMIQDTASAYDEVLDQVTFiDNHDM----DRFMIDGGDP 335
Cdd:cd11330  277 EYTSGGDRLhmaysfDLLGRPFSAA---VVRD----------ALEAFEAEAPDGWPCWAF-SNHDVpravSRWAGGADDP 342
                        410       420
                 ....*....|....*....|....
gi 157830769 336 RKVDMALAVLLTSRGVPNIYYGTE 359
Cdd:cd11330  343 ALARLLLALLLSLRGSVCLYQGEE 366
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
580-671 1.38e-26

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 103.98  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIgPMFNQvvySYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:cd05808    1 VAVTFNVT-ATTVWGQNVYVVGNVPELGNWSPANAV-ALSAA---TYPVWSGTVDLPAGTAIEYKYIKKDGSGTVTWESG 75
                         90
                 ....*....|..
gi 157830769 660 SNHVYTTPTNTT 671
Cdd:cd05808   76 PNRTATTPASGT 87
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-230 9.25e-25

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: 108.13  E-value: 9.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKIndGYLTDMGVTAIWISqPvenvF--SVMNDasgs 90
Cdd:cd11332    7 VVYQVYPRSFADANGDGI------------------GDLAGIRARL--PYLAALGVDAIWLS-P----FypSPMAD---- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  91 asyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-------------PASETNPSYM-ENGRlYDN 156
Cdd:cd11332   58 ---GGYDVADYRDVDPLFGTLADFDALVAAAHELGLRVIVDIVPNHTSdqhpwfqaalaagPGSPERARYIfRDGR-GPD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 157 GTLLggyTNDANMYFhhnGG-----TTFSSLEDG-IYRNLFDLA--DLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDaVK 228
Cdd:cd11332  134 GELP---PNNWQSVF---GGpawtrVTEPDGTDGqWYLHLFAPEqpDLNWDNPEVRAEFEDVLRFWLDRGVDGFRID-VA 206

                 ..
gi 157830769 229 HM 230
Cdd:cd11332  207 HG 208
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
13-230 8.65e-24

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: 105.13  E-value: 8.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKIndGYLTDMGVTAIWISqPVENvfSVMNDAsgsas 92
Cdd:cd11359    7 VIYQIYPRSFKDSNGDGN------------------GDLKGIREKL--DYLKYLGVKTVWLS-PIYK--SPMKDF----- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  93 yhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASE--------TNPsymengrlYDNGTLLGGYT 164
Cdd:cd11359   59 --GYDVSDFTDIDPMFGTMEDFERLLAAMHDRGMKLIMDFVPNHTSDKHEwfqlsrnsTNP--------YTDYYIWADCT 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157830769 165 NDANMYFHHN-----GGTTFSSLE--DGIYRNLFDLA--DLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM 230
Cdd:cd11359  129 ADGPGTPPNNwvsvfGNSAWEYDEkrNQCYLHQFLKEqpDLNFRNPDVQQEMDDVLRFWLDKGVDGFRVDAVKHL 203
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
49-362 1.12e-23

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: 104.31  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  49 GDWQGIINKINdgYLTDMGVTAIWISQPVENVFSvmnDAsgsasyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:cd11348   19 GDLQGIISKLD--YIKSLGCNAIWLNPCFDSPFK---DA-------GYDVRDYYKVAPRYGTNEDLVRLFDEAHKRGIHV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 129 IIDFAPNHTspaSETNPSYMENGRLYDNgtllgGYTND---ANMYFHHNGGTTFSSLE---DGIYR-NLFDLAD-LNH-- 198
Cdd:cd11348   87 LLDLVPGHT---SDEHPWFKESKKAENN-----EYSDRyiwTDSIWSGGPGLPFVGGEaerNGNYIvNFFSCQPaLNYgf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 199 --------QNPVID-------RYLKDAVKMWIDMGIDGIRMDA----VKHMPFG------WQKsLMDEIDNYRPVFTF-G 252
Cdd:cd11348  159 ahpptepwQQPVDApgpqatrEAMKDIMRFWLDKGADGFRVDMadslVKNDPGNketiklWQE-IRAWLDEEYPEAVLvS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 253 EWFLSENEVDANNH-----YFANESGMSLLdfrfgQKLRQVLRNNSDNWYgFNQ----MIQDTASAYDEVLDQVT---FI 320
Cdd:cd11348  238 EWGNPEQSLKAGFDmdfllHFGGNGYNSLF-----RNLNTDGGHRRDNCY-FDAsgkgDIKPFVDEYLPQYEATKgkgYI 311
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 157830769 321 D----NHDMDRfMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYM 362
Cdd:cd11348  312 SlptcNHDTPR-LNARLTEEELKLAFAFLLTMPGVPFIYYGDEIGM 356
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
90-405 2.54e-23

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: 102.02  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  90 SASyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTspaSETNPSYMEngrlydngTLLGGYTNDANM 169
Cdd:cd11354   56 SAS-HGYDTLDHYRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV---GRSHPAVAQ--------ALEDGPGSEEDR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 170 YFHHNGGTTFSSLEDGIyrnlfDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMP--FgWQKSLMDEIDNYRP 247
Cdd:cd11354  124 WHGHAGGGTPAVFEGHE-----DLVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPpeF-WARVLPRVRERHPD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 248 VFTFGEwflsenEVDANNHYFANESGM-SLLDFRFGQKLRQVLRNNsdNWYGFNQMIQDTASAYDEVLDQvTFIDNHDMD 326
Cdd:cd11354  198 AWILGE------VIHGDYAGIVAASGMdSVTQYELWKAIWSSIKDR--NFFELDWALGRHNEFLDSFVPQ-TFVGNHDVT 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 327 RFMIDGGdPRKVDMALAVLLTSRGVPNIYYGTEQYMTG------NGDPNNRKMM-----SSFNKNTRAYQVIQKLSSLRR 395
Cdd:cd11354  269 RIASQVG-DDGAALAAAVLFTVPGIPSIYYGDEQGFTGvkeeraGGDDAVRPAFpaspaELAPLGEWIYRLHQDLIGLRR 347
                        330
                 ....*....|
gi 157830769 396 NNPALAYGDT 405
Cdd:cd11354  348 RHPWLHRART 357
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
65-355 4.04e-23

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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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: 200454 [Multi-domain]  Cd Length: 352  Bit Score: 101.20  E-value: 4.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  65 DMGVTAIWISqPVEnvFSVMNDASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetn 144
Cdd:cd11315   24 AAGYTAIQTS-PPQ--KSKEGGNEGGNWWYRYQPTDYRIGNNQLGTEDDFKALCAAAHKYGIKIIVDVVFNHMANEG--- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 145 psymeNGRLYDNGTLLGGYTNDANmYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIR 223
Cdd:cd11315   98 -----SAIEDLWYPSADIELFSPE-DFHGNGGISnWNDRWQVTQGRLGGLPDLNTENPAVQQQQKAYLKALVALGVDGFR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 224 MDAVKHMP----FGWQKSLMDEI---DNYRPVFTFGEwFLSENEvDANNHYFANESGMSLLDFRFGQKLRQVLRNNsdNW 296
Cdd:cd11315  172 FDAAKHIElpdePSKASDFWTNIlnnLDKDGLFIYGE-VLQDGG-SRDSDYASYLSLGGVTASAYGFPLRGALKNA--FL 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157830769 297 YGFNQMIQDTASAYDEvlDQ-VTFIDNHDM---DRFMIDGGDPRKVDMALAVLLtSR--GVPNIY 355
Cdd:cd11315  248 FGGSLDPASYGQALPS--DRaVTWVESHDTynnDGFESTGLDDEDERLAWAYLA-ARdgGTPLFF 309
CBM20_beta_amylase cd05809
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ...
580-671 9.57e-23

Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 14, which hydrolyzes the alpha-1,4-glucosidic bonds of starch, yielding beta-maltose from the nonreducing end of the substrate. Beta-amylase is found in both plants and microorganisms, however the plant members lack a C-terminal CBM20 domain and are not included in this group. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99884  Cd Length: 99  Bit Score: 93.08  E-value: 9.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSkaIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQG-NVTWES 658
Cdd:cd05809    3 VPQTFVVKNVPTTIGETVYITGSRAELGNWDTK--QYPIQLYYNSHSNDWRGTVHLPAGRNIEFKAIKKSKDGtNKSWQG 80
                         90
                 ....*....|...
gi 157830769 659 GSNHVYTTPTNTT 671
Cdd:cd05809   81 GQQSWYPVPLGTT 93
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
51-487 3.91e-22

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 99.96  E-value: 3.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  51 WQGIINKINDgyLTDMGVTAIWI---SQPVENVFSVmndasgsasyhGYWARDFKKPNPF---------FGTLSDFQRLV 118
Cdd:PRK09441  21 WNRLAERAPE--LAEAGITAVWLppaYKGTSGGYDV-----------GYGVYDLFDLGEFdqkgtvrtkYGTKEELLNAI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 119 DAAHAKGIKVIIDFAPNHTSPA--SETNPSYM--ENGRLYDNGTLLG--GYTN-----DANMY------FHHNGGTTFSS 181
Cdd:PRK09441  88 DALHENGIKVYADVVLNHKAGAdeKETFRVVEvdPDDRTQIISEPYEieGWTRftfpgRGGKYsdfkwhWYHFSGTDYDE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 182 L--EDGIYRNLFD-------------------LADLNHQNPVIDRYLKDAVKMWID-MGIDGIRMDAVKHMPFGWQKSLM 239
Cdd:PRK09441 168 NpdESGIFKIVGDgkgwddqvddengnfdylmGADIDFRHPEVREELKYWAKWYMEtTGFDGFRLDAVKHIDAWFIKEWI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 240 DEIDNY--RPVFTFGE-WflsENEVDANNHYFAN-ESGMSLLDFRFGQKLRQVLRNNSDnwYGFNQMIQDTASAYDEVLd 315
Cdd:PRK09441 248 EHVREVagKDLFIVGEyW---SHDVDKLQDYLEQvEGKTDLFDVPLHYNFHEASKQGRD--YDMRNIFDGTLVEADPFH- 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 316 QVTFIDNHDMDRfmIDGGDPRKVD----MALAVLLT-SRGVPNI----YYGTEQYMTGNGDPNnrkmmssfnkntrayqV 386
Cdd:PRK09441 322 AVTFVDNHDTQP--GQALESPVEPwfkpLAYALILLrEEGYPCVfygdYYGASGYYIDMPFKE----------------K 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 387 IQKLSSLRRNnpaLAYGDTEQRWINGDVYVYERQ---FGKDVVLVAVNRSSSSNYSITGlfTALPAGTYTDQLGGLldGN 463
Cdd:PRK09441 384 LDKLLLARKN---FAYGEQTDYFDHPNCIGWTRSgdeENPGLAVVISNGDAGEKTMEVG--ENYAGKTWRDYTGNR--QE 456
                        490       500
                 ....*....|....*....|....
gi 157830769 464 TIQVGSNGSVNaFDLGPGEVGVWA 487
Cdd:PRK09441 457 TVTIDEDGWGT-FPVNGGSVSVWV 479
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
580-670 4.73e-20

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 85.15  E-value: 4.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAI--GPMfnqvvySYPTWYIDVSVPEGKTIEFKFIKKDSQG---NV 654
Cdd:cd05810    1 VSVTFSCNNGTTQLGQSVYVVGNVPQLGNWSPADAVklDPT------AYPTWSGSISLPASTNVEWKCLKRNETNptaGV 74
                         90
                 ....*....|....*.
gi 157830769 655 TWESGSNHVYTTPTNT 670
Cdd:cd05810   75 QWQGGGNNQLTTGNST 90
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
42-404 7.81e-20

bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 94.57  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   42 NLRkycgGDWQGIINKINDGYLTDMGVTAIWISQPVENVFSVMNDASGSASYHGYWARDFKKPNPFFGTLS--DFQRLVD 119
Cdd:PRK14510  179 NLR----GTFAKLAAPEAISYLKKLGVSIVELNPIFASVDEHHLPQLGLSNYWGYNTVAFLAPDPRLAPGGeeEFAQAIK 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  120 AAHAKGIKVIIDFAPNHTSPASETNPSymengrlydngtlLGGYTNDANMYFHHNGGTTFSSLEDGIYRNLFDLadlnHQ 199
Cdd:PRK14510  255 EAQSAGIAVILDVVFNHTGESNHYGPT-------------LSAYGSDNSPYYRLEPGNPKEYENWWGCGNLPNL----ER 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  200 NPVIdRYLKDAVKMWIDMGIDGIR---------------------MDAVKHMPFGWQKSLMDE----------IDNYRPv 248
Cdd:PRK14510  318 PFIL-RLPMDVLRSWAKRGVDGFRldladelarepdgfidefrqfLKAMDQDPVLRRLKMIAEvwddglggyqYGKFPQ- 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  249 fTFGEWflSENEVDANNHYFANESGMSlldfrfGQKLRQVLrNNSDNW-----YGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:PRK14510  396 -YWGEW--NDPLRDIMRRFWLGDIGMA------GELATRLA-GSADIFphrrrNFSRSINFITAHDGFTLLDLVSFNHKH 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  324 DMDRFM--IDGGDP--------------------RKVDMA--LAVLLTSRGVPNIYYGTEQYMTGNG------DPNNRKM 373
Cdd:PRK14510  466 NEANGEdnRDGTPDnqswncgvegytldaairslRRRRLRllLLTLMSFPGVPMLYYGDEAGRSQNGnnngyaQDNNRGT 545
                         410       420       430
                  ....*....|....*....|....*....|.
gi 157830769  374 MSSFNKNTRAYQVIQKLSSLRRNNPALAYGD 404
Cdd:PRK14510  546 YPWGNEDEELLSFFRRLIKLRREYGVLRQGE 576
Aamy_C smart00632
Aamy_C domain;
406-490 6.44e-18

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 78.82  E-value: 6.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   406 EQRWINGD-VYVYERqfgKDVVLVAVNRSSSsnYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGsVNAFDLGPGE-V 483
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74

                   ....*..
gi 157830769   484 GVWAYSA 490
Cdd:smart00632  75 AIHVDAK 81
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
13-227 2.15e-17

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 85.96  E-value: 2.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKINdgYLTDMGVTAIW-----ISQPVENVFSVMNda 87
Cdd:PRK10933  12 VIYQIYPKSFQDTTGSGT------------------GDLRGVTQRLD--YLQKLGVDAIWltpfyVSPQVDNGYDVAN-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  88 sgsasyhgYWARDfkkpnPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-----------PASETNPSYM----ENGR 152
Cdd:PRK10933  70 --------YTAID-----PTYGTLDDFDELVAQAKSRGIRIILDMVFNHTStqhawfrealnKESPYRQFYIwrdgEPET 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 153 LYDN-GTLLGG----YTNDANMYFHHnggttfssledgiyrnLF--DLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMD 225
Cdd:PRK10933 137 PPNNwRSKFGGsawrWHAESEQYYLH----------------LFapEQADLNWENPAVRAELKKVCEFWADRGVDGLRLD 200

                 ..
gi 157830769 226 AV 227
Cdd:PRK10933 201 VV 202
AmyAc_GTHase cd11325
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called ...
48-400 2.51e-17

Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase); Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase


Pssm-ID: 200464 [Multi-domain]  Cd Length: 436  Bit Score: 84.91  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  48 GGDWQGIINKIndGYLTDMGVTAIWIsQPVenvfsvmNDASGSASYhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIK 127
Cdd:cd11325   51 EGTFDAAIERL--DYLADLGVTAIEL-MPV-------AEFPGERNW-GYDGVLPFAPESSYGGPDDLKRLVDAAHRRGLA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 128 VIIDFAPNHTSPasetnpsymengrlydNGTLLGGYTNDanmYFHHNGGTTFSsleDGIyrNlFDLADlnhqNPViDRYL 207
Cdd:cd11325  120 VILDVVYNHFGP----------------DGNYLWQFAGP---YFTDDYSTPWG---DAI--N-FDGPG----DEV-RQFF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 208 KDAVKMWI-DMGIDGIRMDAVKHMPFGWQKSLMDEI-------DNYRPVFTFGewflsenEVDANNH-----YFANESGM 274
Cdd:cd11325  170 IDNALYWLrEYHVDGLRLDAVHAIRDDSGWHFLQELarevraaAAGRPAHLIA-------EDDRNDPrlvrpPELGGAGF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 275 SLL---DFRfgQKLRQVLRNNSDNWYGFNQMIQDTASAYDEV-LDQ-----------------------VTFIDNHD--- 324
Cdd:cd11325  243 DAQwndDFH--HALHVALTGEREGYYADFGPAEDLARALAEGfVYQgqyspfrgrrhgrpsadlpptrfVVFLQNHDqvg 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 325 ----MDRfMIDGGDPRKVDMALAVLLTSRGVPNIYYGTE-------QYMTGNGDPNNRKMMSSFNKNTRAYQVIQKLSSL 393
Cdd:cd11325  321 nraaGER-LSSLAAPARLRLAAALLLLSPGIPMLFMGEEfgedtpfLFFTDHDDPELAEAVREGRRREFAAGWDRDLIPD 399

                 ....*..
gi 157830769 394 RRNNPAL 400
Cdd:cd11325  400 PQAPETF 406
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
48-356 8.72e-16

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: 78.42  E-value: 8.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  48 GGDWQGIIN-KINDgyLTDMGVTAIWISQPVEnvfsvmndaSGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGI 126
Cdd:cd11314   13 DGTWWNHLEsKAPE--LAAAGFTAIWLPPPSK---------SVSGSSMGYDPGDLYDLNSRYGSEAELRSLIAALHAKGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 127 KVIIDFAPNHtspasetnpsymENGrlYDNGTLLGGYTN-DanmyfHHNggttfssleDGIYRNLFDLAdlnhqnpvidR 205
Cdd:cd11314   82 KVIADIVINH------------RSG--PDTGEDFGGAPDlD-----HTN---------PEVQNDLKAWL----------N 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 206 YLKDavkmwiDMGIDGIRMDAVKHMPFGWQKSLMDEIDNYrpvFTFGEWFLSENEVDANNHY-----FANESGM--SLLD 278
Cdd:cd11314  124 WLKN------DIGFDGWRFDFVKGYAPSYVKEYNEATSPS---FSVGEYWDGLSYENQDAHRqrlvdWIDATGGgsAAFD 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 279 FRFGQKLRQVLrnNSDNWYGFNQMiQDTASAYDEVLDQ--VTFIDNHDMDRfmIDGGDP---RKVDMALAVLLTSRGVPN 353
Cdd:cd11314  195 FTTKYILQEAV--NNNEYWRLRDG-QGKPPGLIGWWPQkaVTFVDNHDTGS--TQGHWPfptDNVLQGYAYILTHPGTPC 269

                 ...
gi 157830769 354 IYY 356
Cdd:cd11314  270 VFW 272
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
49-230 9.75e-16

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


Pssm-ID: 223373 [Multi-domain]  Cd Length: 628  Bit Score: 80.82  E-value: 9.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  49 GDWQGIINKINdgYLTDMGVTAIWIsQPVENVfsvmndaSGSASYhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:COG0296  162 GYFELAIELLP--YLKELGITHIEL-MPVAEH-------PGDRSW-GYQGTGYYAPTSRYGTPEDFKALVDAAHQAGIGV 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 129 IIDFAPNHTSPASETNPSYmengrlydNGTLLGGYTnDANMYFHHNGGTTfssledgiyrnLFDladlNHQNPViDRYLK 208
Cdd:COG0296  231 ILDWVPNHFPPDGNYLARF--------DGTFLYEHE-DPRRGEHTDWGTA-----------IFN----YGRNEV-RNFLL 285
                        170       180
                 ....*....|....*....|...
gi 157830769 209 DAVKMWID-MGIDGIRMDAVKHM 230
Cdd:COG0296  286 ANALYWLEeYHIDGLRVDAVASM 308
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
62-357 1.56e-15

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: 79.10  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISqPvenvfsvMNDASGSASYHGYWARDF--------------KkpnpfFGTLSDFQRLVDAAHAKGIK 127
Cdd:cd11318   28 ELAELGITAVWLP-P-------AYKGASGTEDVGYDVYDLydlgefdqkgtvrtK-----YGTKEELLEAIKALHENGIQ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 128 VIIDFAPNH--------TSPASETNPSYmENGRLYDNGTLLG--GYT--NDANMY------FHHNGGTTF--SSLEDGIY 187
Cdd:cd11318   95 VYADAVLNHkagadeteTVKAVEVDPND-RNKEISEPYEIEAwtKFTfpGRGGKYsdfkwnWQHFSGVDYdqKTKKKGIF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 188 RNLFDL-------------------ADLNHQNPVIDRYLKDAVKmWI--DMGIDGIRMDAVKHMPFGWQKSLMDEIDNY- 245
Cdd:cd11318  174 KINFEGkgwdedvddengnydylmgADIDYSNPEVREELKRWGK-WYinTTGLDGFRLDAVKHISASFIKDWIDHLRREt 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 246 -RPVFTFGEWFlsENEVDANNHYFANESG-MSLLDFrfgqKLRQVLRNNSDNWYGFN--QMIQDTASAYDEVlDQVTFID 321
Cdd:cd11318  253 gKDLFAVGEYW--SGDLEALEDYLDATDGkMSLFDV----PLHYNFHEASKSGGNYDlrKIFDGTLVQSRPD-KAVTFVD 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 157830769 322 NHD------MDRFMIdggDPRKVdMALAV-LLTSRGVPNIYYG 357
Cdd:cd11318  326 NHDtqpgqsLESWVE---PWFKP-LAYALiLLRKDGYPCVFYG 364
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
108-378 2.36e-15

Alpha amylase catalytic domain found in bacterial and 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 77.60  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 108 FGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpaseTNPSYMENGRLYDngtllggytndanmyfhhnggttfssledgiy 187
Cdd:cd11317   62 SGTEAEFRDMVNRCNAAGVRVYVDAVINHMA----GDANEVRNCELVG-------------------------------- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 188 rnlfdLADLNHQNP-VIDR---YLKDAvkmwIDMGIDGIRMDAVKHMP-------FGWQKSLMDEIDNYRPvFTFGEWFL 256
Cdd:cd11317  106 -----LADLNTESDyVRDKiadYLNDL----ISLGVAGFRIDAAKHMWpedlaaiLARLKDLNGGPLGSRP-YIYQEVID 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 257 SENEVDANNHYFANesGMsLLDFRFGQKLRQVLRNNSDNWYGFNqmiQDTASAYDEVLDQVTFIDNHDMDRfmiDGG--- 333
Cdd:cd11317  176 GGGEAIQPSEYTGN--GD-VTEFRYARGLSNAFRGKIKLLLLKN---FGEGWGLLPSERAVVFVDNHDNQR---GHGggg 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157830769 334 ------DPRKVDMALAVLLTSRgvpniyYGTeqymtgngdpnnRKMMSSFN 378
Cdd:cd11317  247 dmltykDGRRYKLANAFMLAWP------YGT------------PRVMSSYY 279
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
581-678 1.20e-14

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 70.05  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 581 SVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgpmfnQVVY-SYPTWYIDVSVPEGKT-IEFKFIKKDS-QGNVTWE 657
Cdd:cd05816    1 VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKAL-----KLSDvGFPIWEADIDISKDSFpFEYKYIIANKdSGVVSWE 75
                         90       100
                 ....*....|....*....|....
gi 157830769 658 SGSNHVYTTPTNTTGKIIV---DW 678
Cdd:cd05816   76 NGPNRELSAPSLKGESSTLivsDG 99
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
13-359 7.06e-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 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: 74.25  E-value: 7.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  13 VVYQIVVDRFVDGNTSNNPSGALFSSGCtnlrkycggdwqGIINKIND---GYLTDMGVTAIW----ISQPVENVFSVMN 85
Cdd:cd11349    2 IIYQLLPRLFGNKNTTNIPNGTIEENGV------------GKFNDFDDtalKEIKSLGFTHVWytgvIRHATQTDYSAYG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  86 DAS----------GSAsyhgYWARDFKKPNPFFGT-----LSDFQRLVDAAHAKGIKVIIDFAPNHTSPA--SETNPSYM 148
Cdd:cd11349   70 IPPddpdivkgraGSP----YAIKDYYDVDPDLATdptnrMEEFEALVERTHAAGLKVIIDFVPNHVARQyhSDAKPEGV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 149 ENGRLYDNGTLlgGYTNDANMY------FHHNGGTTFSSLEDGIYR---------NLFDLA----------DLN------ 197
Cdd:cd11349  146 KDFGANDDTSK--AFDPSNNFYylpgepFVLPFSLNGSPATDGPYHespakatgnDCFSAApsindwyetvKLNygvdyd 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 198 -----HQNPVIDRYLK--DAVKMWIDMGIDGIRMDAVkHM---PFgWQKsLMDEIDNYRPVFTfgewFLSENEVDANNHY 267
Cdd:cd11349  224 gggsfHFDPIPDTWIKmlDILLFWAAKGVDGFRCDMA-EMvpvEF-WHW-AIPEIKARYPELI----FIAEIYNPGLYRD 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 268 FANESGMSLLDFRFG--QKLRQVLRNNSDNwYGFNQMIQDTASAYDEVLDqvtFIDNHDMDRFMID--GGDPRKVDMALA 343
Cdd:cd11349  297 YLDEGGFDYLYDKVGlyDTLRAVICGGGSA-SEITVWWQESDDIADHMLY---FLENHDEQRIASPffAGNAEKALPAMV 372
                        410
                 ....*....|....*..
gi 157830769 344 VLLT-SRGVPNIYYGTE 359
Cdd:cd11349  373 VSATlSTGPFMLYFGQE 389
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
48-236 3.14e-11

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: 66.05  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  48 GGDWQGIINKINdgYLTDMGVTaiwisqpvenVFSVM---------NDAsgsasyhGYWARDFKKPNPFFGTLSDFQRLV 118
Cdd:cd11324   82 AGDLKGLAEKIP--YLKELGVT----------YLHLMpllkppegdNDG-------GYAVSDYREVDPRLGTMEDLRALA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 119 DAAHAKGIKVIIDFAPNHTS-------PASETNPSYMENGRLYDNGTLL----------------GGYTNDANMyfhhnG 175
Cdd:cd11324  143 AELRERGISLVLDFVLNHTAdehewaqKARAGDPEYQDYYYMFPDRTLPdayertlpevfpdtapGNFTWDEEM-----G 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157830769 176 G---TTFSSLEdgiyrnlfdlADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVkhmPFGWQK 236
Cdd:cd11324  218 KwvwTTFNPFQ----------WDLNYANPAVFNEMLDEMLFLANQGVDVLRLDAV---AFIWKR 268
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
591-666 1.65e-10

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 58.25  E-value: 1.65e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157830769 591 TNLGQNIYIVGNVYELGNWDTSKAIGPMFNQvvysYPTWYIDVSVPEGKTIEFKFI--KKDSQGNVTWESGSNHVYTT 666
Cdd:cd05817   10 TQFGEAVYISGNCNQLGNWNPSKAKRMQWNE----GDLWTVDVGIPESVYIEYKYFvsNYDDPNTVLWESGPNRVLRT 83
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
495-573 1.78e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 426462 [Multi-domain]  Cd Length: 84  Bit Score: 57.46  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  495 PIIGHVGPMMGQV--GHQVTIDGEGFGTNTG--TVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYD 570
Cdd:pfam01833   1 PVITSISPSSGPAsgGTTITITGSNFGTDSSdvKVTIGGTPCTVISVSSTTIVCTTPPGVSGLVNVSVTVGGDGISSSPL 80

                  ...
gi 157830769  571 NFE 573
Cdd:pfam01833  81 TFT 83
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
62-230 2.06e-10

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: 63.31  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISQPVENVFSvmndasGSASYH--GYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:cd11322   67 YVKEMGYTHVELMPVMEHPFD------GSWGYQvtGYFA-----PTSRYGTPDDFKYFVDACHQAGIGVILDWVPGHFPK 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 140 AsetnpsymENGrLYD-NGTLLGGYTnDANMYFHHNGGTtfssledgiyrNLFDLADlnhqnPVIDRYLKDAVKMWID-M 217
Cdd:cd11322  136 D--------DHG-LARfDGTPLYEYP-DPRKGEHPDWGT-----------LNFDYGR-----NEVRSFLISNALYWLEeY 189
                        170
                 ....*....|...
gi 157830769 218 GIDGIRMDAVKHM 230
Cdd:cd11322  190 HIDGLRVDAVSSM 202
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
15-132 4.97e-10

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: 62.31  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  15 YQIVVDRFVDGNTSNNP-SGALFSSGC--TNLRKycGGDWQGIINKINdgYLTDMGVTAI------WISQPvenvfsvmn 85
Cdd:cd11323   59 YTIFLDRFVNGDPTNDDaNGTVFEQDIyeTQLRH--GGDIVGLVDSLD--YLQGMGIKGIyiagtpFINMP--------- 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157830769  86 dasgsASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDF 132
Cdd:cd11323  126 -----WGADGYSPLDFTLLDHHFGTIADWRAAIDEIHRRGMYVVLDN 167
PRK14706 PRK14706
glycogen branching enzyme; Provisional
62-230 8.03e-10

glycogen branching enzyme; Provisional


Pssm-ID: 237795 [Multi-domain]  Cd Length: 639  Bit Score: 61.92  E-value: 8.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISQPVENVFsvmnDASGSASYHGYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTsPAS 141
Cdd:PRK14706 176 YVTYMGYTHVELLGVMEHPF----DGSWGYQVTGYYA-----PTSRLGTPEDFKYLVNHLHGLGIGVILDWVPGHF-PTD 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 142 ETNPSYMENGRLYDNGTLLGGYTNDANMYfhhnggttfssledgiyrnLFDLAdlnhQNPVIDRYLKDAVKMWIDMGIDG 221
Cdd:PRK14706 246 ESGLAHFDGGPLYEYADPRKGYHYDWNTY-------------------IFDYG----RNEVVMFLIGSALKWLQDFHVDG 302

                 ....*....
gi 157830769 222 IRMDAVKHM 230
Cdd:PRK14706 303 LRVDAVASM 311
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
105-242 1.05e-09

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: 61.24  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 105 NPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP-------ASETNPSYmenGRLYDNGTLLGGYTndANMYFHHNGGT 177
Cdd:cd11329  108 NNSYGVESDLKELVKTAKQKDIKVILDLTPNHSSKqhplfkdSVLKEPPY---RSAFVWADGKGHTP--PNNWLSVTGGS 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157830769 178 TFSSLED-GIYRNLF--DLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHmpFGWQKSLMDEI 242
Cdd:cd11329  183 AWKWVEDrQYYLHQFgpDQPDLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY--LLEDPNLKDEE 248
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
62-407 1.20e-09

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: 61.18  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   62 YLTDMGVTAIWIsQPVeNVFSVMNDASGSASYH-GYWARDFKKPNPFFGT--------LSDFQRLVDAAHAKGIKVIIDF 132
Cdd:TIGR02104 172 YLKELGVTHVQL-LPV-FDFAGVDEEDPNNAYNwGYDPLNYNVPEGSYSTnpydpatrIRELKQMIQALHENGIRVIMDV 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  133 APNHT-----SPASETNPSYmengrlydngtllggytndanmYFHHNggttfsslEDGIYRNLFDLA-DLNHQNPVIDRY 206
Cdd:TIGR02104 250 VYNHTysreeSPFEKTVPGY----------------------YYRYN--------EDGTLSNGTGVGnDTASEREMMRKF 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  207 LKDAVKMWI-DMGIDGIRMDA-----VKHMpfgwqKSLMDEIDNYRP-VFTFGE-WFLS---ENEVDANNhyfANESGMS 275
Cdd:TIGR02104 300 IVDSVLYWVkEYNIDGFRFDLmgihdIETM-----NEIRKALNKIDPnILLYGEgWDLGtplPPEQKATK---ANAYQMP 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  276 LLDFrFGQKLRQVLRNN----------SDNWYGFNQMI----------QDTASAYD--EVLDQVTFIDNHDM-DRFMIDG 332
Cdd:TIGR02104 372 GIAF-FNDEFRDALKGSvfhlkkkgfvSGNPGTEEIVKkgilgsieldAVKPSALDpsQSINYVECHDNHTLwDKLSLAN 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  333 GD------PRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMSSFN------KNTRAYQV--IQKLSSLRRNNP 398
Cdd:TIGR02104 451 PDeteeqlKKRQKLATAILLLSQGIPFLHAGQEFMRTKQGDENSYNSPDSINqldwdrKATFKDDVnyIKGLIALRKAHP 530

                  ....*....
gi 157830769  399 ALAYGDTEQ 407
Cdd:TIGR02104 531 AFRLSSAED 539
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
61-152 2.88e-09

malto-oligosyltrehalose synthase;


Pssm-ID: 237740  Cd Length: 879  Bit Score: 60.38  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  61 GYLTDMGVTAIWISqpvenvfSVMNDASGSAsyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPA 140
Cdd:PRK14511  27 PYFADLGVSHLYLS-------PILAARPGST--HGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVG 97
                         90
                 ....*....|....*
gi 157830769 141 SETNP---SYMENGR 152
Cdd:PRK14511  98 GPDNPwwwDVLEWGR 112
trehalose_TreY TIGR02401
malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan ...
62-152 3.02e-09

malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase, is the TreY enzyme of the TreYZ pathway of trehalose biosynthesis, an alternative to the OtsAB pathway. Trehalose may be incorporated into more complex compounds but is best known as compatible solute. It is one of the most effective osmoprotectants, and unlike the various betaines does not require nitrogen for its synthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274113  Cd Length: 825  Bit Score: 60.11  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   62 YLTDMGVTAIWISqPVEnvfsvmndASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAS 141
Cdd:TIGR02401  24 YLKSLGVSHLYLS-PIL--------TAVPGSTHGYDVVDHSEINPELGGEEGLRRLSEAARARGLGLIVDIVPNHMAVHL 94
                          90
                  ....*....|....
gi 157830769  142 ETNPSYM---ENGR 152
Cdd:TIGR02401  95 EQNPWWWdvlKNGP 108
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
495-576 1.15e-08

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050  Cd Length: 89  Bit Score: 52.46  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 495 PIIGHVGPMMGQV--GHQVTIDGEGFGTN-TGTVKFGT-TAANVVSWSNNQIVVAVP---NVSPGKYNITVQSSSGQTSA 567
Cdd:cd00102    1 PVITSISPSSGPVsgGTEVTITGSNFGSGsNLRVTFGGgVPCSVLSVSSTAIVCTTPpyaNPGPGPVEVTVDRGNGGITS 80

                 ....*....
gi 157830769 568 AYDNFEVLT 576
Cdd:cd00102   81 SPLTFTYVP 89
TreY COG3280
Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];
62-152 1.17e-08

Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];


Pssm-ID: 225819  Cd Length: 889  Bit Score: 58.25  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISqPVenvFSVMndaSGSAsyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAS 141
Cdd:COG3280   27 YLADLGISHLYLS-PI---FTAR---PGST--HGYDVVDPTEINPELGGEEGLERLVAALKSRGLGLIVDIVPNHMAVGG 97
                         90
                 ....*....|....
gi 157830769 142 ETNPSYM---ENGR 152
Cdd:COG3280   98 HENPWWWdvlENGR 111
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
62-152 1.21e-08

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  Cd Length: 660  Bit Score: 58.27  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISqPVenvfsvMNDASGSAsyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAS 141
Cdd:cd11336   22 YLADLGISHLYAS-PI------LTARPGST--HGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVSG 92
                         90
                 ....*....|....
gi 157830769 142 ETNPSYM---ENGR 152
Cdd:cd11336   93 AENPWWWdvlENGP 106
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
592-678 6.75e-08

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99892  Cd Length: 92  Bit Score: 50.58  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 592 NLGQNIYIVGNVYELGNWdtsKAIGPMfnqvVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESGSNHVYTTPTNTT 671
Cdd:cd05818   13 KFGEHVAILGSTKELGSW---KKKVPM----NWTENGWVCDLELDGGELVEYKFVIVKRDGSVIWEGGNNRVLELPKEGN 85

                 ....*..
gi 157830769 672 GKIIVDW 678
Cdd:cd05818   86 FEIVCHW 92
PLN02784 PLN02784
alpha-amylase
63-356 8.98e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 55.40  E-value: 8.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  63 LTDMGVTAIWISQPVENVfsvmndasgsaSYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpase 142
Cdd:PLN02784 530 LSSLGFTVVWLPPPTESV-----------SPEGYMPKDLYNLNSRYGTIDELKDLVKSFHEVGIKVLGDAVLNHRC---- 594
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 143 tnpSYMENgrlyDNGT--LLGGYTN-DA------NMYFHHNGGTTfssleDGiyrnlfdlaDLNHQNPVIDR---YLKDA 210
Cdd:PLN02784 595 ---AHFQN----QNGVwnIFGGRLNwDDravvadDPHFQGRGNKS-----SG---------DNFHAAPNIDHsqdFVRKD 653
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 211 VKMWI-----DMGIDGIRMDAVKHMpfgWQKSLMDEIDNYRPVFTFGEWF--LSEN--EVDANN--HY-----FANESGM 274
Cdd:PLN02784 654 LKEWLcwmrkEVGYDGWRLDFVRGF---WGGYVKDYMEASEPYFAVGEYWdsLSYTygEMDYNQdaHRqrivdWINATNG 730
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 275 SLLDFRFGQK--LRQVLrNNSDNWygfnqMIQDTASAYDEVLD-----QVTFIDNHDMD------RFmidggdPRKVDM- 340
Cdd:PLN02784 731 TAGAFDVTTKgiLHSAL-ERCEYW-----RLSDQKGKPPGVVGwwpsrAVTFIENHDTGstqghwRF------PEGKEMq 798
                        330
                 ....*....|....*.
gi 157830769 341 ALAVLLTSRGVPNIYY 356
Cdd:PLN02784 799 GYAYILTHPGTPAVFY 814
AmyAc_Glg_debranch cd11326
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ...
62-225 1.02e-07

Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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: 200465 [Multi-domain]  Cd Length: 433  Bit Score: 54.78  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAI-------WISQPVENVFSVMNdasgsasYHGYwardfkkpNP--FF-------------GTLSDFQRLVD 119
Cdd:cd11326   52 YLKELGVTAVellpvhaFDDEEHLVERGLTN-------YWGY--------NTlnFFapdpryasddapgGPVDEFKAMVK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 120 AAHAKGIKVIIDFAPNHTSPASETNPSYmeNGRLYDNGTllggY--TNDANMYFHHNGGT--TFssledgiyrnlfdlaD 195
Cdd:cd11326  117 ALHKAGIEVILDVVYNHTAEGGELGPTL--SFRGLDNAS----YyrLDPDGPYYLNYTGCgnTL---------------N 175
                        170       180       190
                 ....*....|....*....|....*....|.
gi 157830769 196 LNHqnPVIDRYLKDAVKMWI-DMGIDGIRMD 225
Cdd:cd11326  176 TNH--PVVLRLILDSLRYWVtEMHVDGFRFD 204
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
100-236 3.34e-07

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: 52.83  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 100 DFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHtspasETNPSYmengrlydngtllggytndanmyfhhnggttf 179
Cdd:cd11345   68 NLTEIDPDLGTLEDFTSLLTAAHKKGISVVLDLTPNY-----RGESSW-------------------------------- 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157830769 180 ssledgiyrnlfdladLNHQNPVIDRYLKDAVKMWIDMGIDGIRM----DAVKHMPFGWQK 236
Cdd:cd11345  111 ----------------AFSDAENVAEKVKEALEFWLNQGVDGIQVsdleNVASSASSEWSN 155
AmyAc_bac_euk_BE cd11321
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching ...
91-230 2.10e-06

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: 50.69  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  91 ASYhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsymENGrlydngtlLGGYTNDANMY 170
Cdd:cd11321   68 ASF-GYQVTNFFAASSRFGTPEDLKYLIDTAHGMGIAVLLDVVHSHASKNV-------LDG--------LNMFDGTDGCY 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157830769 171 FHHNGgttfssledgiyRNLFDLAD---LNHQNPVIDRYLKDAVKMWID-MGIDGIRMDAVKHM 230
Cdd:cd11321  132 FHEGE------------RGNHPLWDsrlFNYGKWEVLRFLLSNLRWWLEeYRFDGFRFDGVTSM 183
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
409-489 3.82e-06

Alpha amylase, C-terminal all-beta 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: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 45.79  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  409 WINGD-----VYVYERQFGKDVVLVAVNRSSSSNYsiTGLFTALP-AGTYTDQL-------GGLLDGNTIQVGSNGSVNA 475
Cdd:pfam02806   1 WIDGDdaennVIAFERGDDGGKLLVVFNFTPSVSY--TDYRTGLPeAGTYCEVLntddeeyGGSNTGEVVTVDGPGHPNS 78
                          90
                  ....*....|....*.
gi 157830769  476 --FDLGPGEVGVWAYS 489
Cdd:pfam02806  79 ltLTLPPLSALVLKVE 94
PRK12313 PRK12313
1,4-alpha-glucan branching protein GlgB;
62-230 7.89e-06

1,4-alpha-glucan branching protein GlgB;


Pssm-ID: 237052 [Multi-domain]  Cd Length: 633  Bit Score: 49.13  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISQPVENVFSvmndasGSASYH--GYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSp 139
Cdd:PRK12313 179 YVKEMGYTHVEFMPLMEHPLD------GSWGYQltGYFA-----PTSRYGTPEDFMYLVDALHQNGIGVILDWVPGHFP- 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 140 aseTNPsymeNGRLYDNGTLLGGYTnDANMYFHHNGGTTfssledgiyrnLFDLAdlnhQNPViDRYLKDAVKMWID-MG 218
Cdd:PRK12313 247 ---KDD----DGLAYFDGTPLYEYQ-DPRRAENPDWGAL-----------NFDLG----KNEV-RSFLISSALFWLDeYH 302
                        170
                 ....*....|..
gi 157830769 219 IDGIRMDAVKHM 230
Cdd:PRK12313 303 LDGLRVDAVSNM 314
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
582-658 9.02e-06

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888 [Multi-domain]  Cd Length: 120  Bit Score: 45.39  E-value: 9.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 582 VRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgPMFNQVVYSYpTWYIDVSVPEGKTIEFKFIK----KDSQGN---- 653
Cdd:cd05814    3 VTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAV-PLEKEDDDCN-LWKASIELPRGVDFQYRYFVavvlNDSGPCqviv 80

                 ....*
gi 157830769 654 VTWES 658
Cdd:cd05814   81 RKWET 85
AmyAc_1 cd11347
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
103-225 1.20e-05

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: 48.00  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 103 KPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHT---SPASETNPSYMENGrlydNGTLLGGYTNdanmYFHHNGGTTF 179
Cdd:cd11347   93 TVNPDLGGEDDLAALRERLAARGLKLMLDFVPNHValdHPWVEEHPEYFIRG----TDEDLARDPA----NYTYYGGNIL 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157830769 180 SSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVkmwidMGI----DGIRMD 225
Cdd:cd11347  165 AHGRDPYFPPWTDTAQLNYANPATRAAMIETL-----LKIasqcDGVRCD 209
PLN00196 PLN00196
alpha-amylase; Provisional
45-356 1.45e-05

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 47.99  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  45 KYCGGDWQGIINKINDgyLTDMGVTAIWISQPvenvfsvmndaSGSASYHGYW-ARDFKKPNPFFGTLSDFQRLVDAAHA 123
Cdd:PLN00196  37 KQNGGWYNFLMGKVDD--IAAAGITHVWLPPP-----------SHSVSEQGYMpGRLYDLDASKYGNEAQLKSLIEAFHG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 124 KGIKVIIDFAPNHTSpasetnPSYMENGRLYdngTLLGGYTNDANMyfhhNGGTTFSSLEDGIYR----NL---FDLA-- 194
Cdd:PLN00196 104 KGVQVIADIVINHRT------AEHKDGRGIY---CLFEGGTPDSRL----DWGPHMICRDDTQYSdgtgNLdtgADFAaa 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 195 -DLNHQNPVIDRYLKDAVKmWI--DMGIDGIRMDAVKhmpfGWQKSLMD-EIDNYRPVFTFGE-WFLSENEVDANNHYFA 269
Cdd:PLN00196 171 pDIDHLNKRVQRELIGWLL-WLksDIGFDAWRLDFAK----GYSAEVAKvYIDGTEPSFAVAEiWTSMAYGGDGKPEYDQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 270 NESGMSLLD--------------FRFGQKLRQVLRNNSDNWygfnQMIQDTASAYDEV----LDQVTFIDNHD------M 325
Cdd:PLN00196 246 NAHRQELVNwvdrvggaaspatvFDFTTKGILNVAVEGELW----RLRGADGKAPGVIgwwpAKAVTFVDNHDtgstqhM 321
                        330       340       350
                 ....*....|....*....|....*....|.
gi 157830769 326 DRFMIDggdprKVDMALAVLLTSRGVPNIYY 356
Cdd:PLN00196 322 WPFPSD-----KVMQGYAYILTHPGNPCIFY 347
PRK14705 PRK14705
glycogen branching enzyme; Provisional
95-230 2.84e-05

glycogen branching enzyme; Provisional


Pssm-ID: 237794 [Multi-domain]  Cd Length: 1224  Bit Score: 47.69  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769   95 GYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTsPASETNPSYMENGRLYDNGtllggytnDANMYFHHN 174
Cdd:PRK14705  798 GYQVTSYFAPTSRFGHPDEFRFLVDSLHQAGIGVLLDWVPAHF-PKDSWALAQFDGQPLYEHA--------DPALGEHPD 868
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157830769  175 GGTTfssledgiyrnLFDLADLNHQNPVIDRYLkdavkMWID-MGIDGIRMDAVKHM 230
Cdd:PRK14705  869 WGTL-----------IFDFGRTEVRNFLVANAL-----YWLDeFHIDGLRVDAVASM 909
PLN02950 PLN02950
4-alpha-glucanotransferase
572-663 4.09e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 47.02  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 572 FEVLTNDQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKaiGPMFNQVVysYPTWYIDVSVPEGK-TIEFKFIKKDS 650
Cdd:PLN02950 145 NKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDD--GLKLNYTG--DSIWEADCLVPKSDfPIKYKYALQTA 220
                         90
                 ....*....|...
gi 157830769 651 QGNVTWESGSNHV 663
Cdd:PLN02950 221 EGLVSLELGVNRE 233
PRK05402 PRK05402
1,4-alpha-glucan branching protein GlgB;
108-136 4.69e-05

1,4-alpha-glucan branching protein GlgB;


Pssm-ID: 235445 [Multi-domain]  Cd Length: 726  Bit Score: 46.71  E-value: 4.69e-05
                         10        20
                 ....*....|....*....|....*....
gi 157830769 108 FGTLSDFQRLVDAAHAKGIKVIIDFAPNH 136
Cdd:PRK05402 311 FGTPDDFRYFVDACHQAGIGVILDWVPAH 339
PRK12568 PRK12568
glycogen branching enzyme; Provisional
62-230 7.93e-05

glycogen branching enzyme; Provisional


Pssm-ID: 139075 [Multi-domain]  Cd Length: 730  Bit Score: 45.71  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  62 YLTDMGVTAIWISQPVENVFSvmndasGSASYH--GYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHtsp 139
Cdd:PRK12568 278 YVQQLGFTHIELLPITEHPFG------GSWGYQplGLYA-----PTARHGSPDGFAQFVDACHRAGIGVILDWVSAH--- 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 140 asetnpsymengrlydngtllggYTNDANMYFHHNGGTTFSSLE--DGIYRNlFDLADLNHQNPVIDRYLKDAVKMWID- 216
Cdd:PRK12568 344 -----------------------FPDDAHGLAQFDGAALYEHADprEGMHRD-WNTLIYNYGRPEVTAYLLGSALEWIEh 399
                        170
                 ....*....|....
gi 157830769 217 MGIDGIRMDAVKHM 230
Cdd:PRK12568 400 YHLDGLRVDAVASM 413
PLN02447 PLN02447
1,4-alpha-glucan-branching enzyme
95-263 1.35e-04

1,4-alpha-glucan-branching enzyme


Pssm-ID: 215246 [Multi-domain]  Cd Length: 758  Bit Score: 45.05  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  95 GYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasetnpsymengrlydNGTL--LGGYTNDANMYFH 172
Cdd:PLN02447 283 GYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHAS-----------------KNTLdgLNGFDGTDGSYFH 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 173 hnggttfsSLEDGiYRNLFDLADLNHQNPVIDRYLKDAVKMWID-MGIDGIRMDAVKHMPFGWQKSLMDEIDNYrpvftf 251
Cdd:PLN02447 346 --------SGPRG-YHWLWDSRLFNYGNWEVLRFLLSNLRWWLEeYKFDGFRFDGVTSMLYHHHGLQMAFTGNY------ 410
                        170
                 ....*....|..
gi 157830769 252 GEWFLSENEVDA 263
Cdd:PLN02447 411 NEYFGMATDVDA 422
AmyAc_plant_IsoA cd11346
Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching ...
49-221 2.31e-04

Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like 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: 200484 [Multi-domain]  Cd Length: 347  Bit Score: 44.00  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769  49 GDWQGIINKIndGYLTDMGVTAIwISQPVenvFSVMNDASGSASYHGYWArdfkkPNPFF------GTLSDFQRLVDAAH 122
Cdd:cd11346   29 GTFLGVLEKV--DHLKSLGVNTV-LLQPI---FAFARVKGPYYPPSFFSA-----PDPYGagdsslSASAELRAMVKGLH 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 123 AKGIKVIIDFAPNHTSPASETNPSyMENGRLYDNGTLLggYTNDANMYFHHNGGTTfssledgiyrnlfdlADLNHQNPV 202
Cdd:cd11346   98 SNGIEVLLEVVLTHTAEGTDESPE-SESLRGIDAASYY--ILGKSGVLENSGVPGA---------------AVLNCNHPV 159
                        170       180
                 ....*....|....*....|
gi 157830769 203 IDRYLKDAVKMWI-DMGIDG 221
Cdd:cd11346  160 TQSLILDSLRHWAtEFGVDG 179
AmyAc_GlgE_like cd11344
Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan: ...
105-136 5.92e-04

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: 42.59  E-value: 5.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 157830769 105 NPFFGTLSDFQRLVDAAHAKGIKVIIDFA----PNH 136
Cdd:cd11344   84 HPELGTLEDFDRLVAEARELGIEVALDIAlqcsPDH 119
PLN02950 PLN02950
4-alpha-glucanotransferase
580-679 8.84e-04

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 42.40  E-value: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIgPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVT-WES 658
Cdd:PLN02950   9 VTLSFRIP-YYTQWGQSLLVCGSEPLLGSWNVKKGL-LLSPVHQGDELVWEGSVSVPEGFSCEYSYYVVDDNKNVLrWEA 86
                         90       100
                 ....*....|....*....|....*
gi 157830769 659 GSNHVYTTPTNTTGKIIVD----WQ 679
Cdd:PLN02950  87 GKKRKLVLPEGLQGGELVElhdlWQ 111
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
582-662 2.12e-03

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99881  Cd Length: 112  Bit Score: 38.27  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 582 VRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAI--GPMFNQVVYSYPT-WYIDVSVPEG---KTIEFKFIKKDSqGNVT 655
Cdd:cd05806    3 FRFGVVLTFADRDTELLVLGSRPELGSWDPQRAVpmRPARKALSPQEPSlWLGEVELSEPgseDTFWYKFLKREA-GALI 81

                 ....*...
gi 157830769 656 WE-SGSNH 662
Cdd:cd05806   82 WEgNGPHH 89
CBM20_DPE2_repeat1 cd05815
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
591-672 2.98e-03

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 1. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 starch binding domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal carbohydrate-binding domains. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99889  Cd Length: 101  Bit Score: 37.42  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157830769 591 TNLGQNIYIVGNVYELGNWDTSKAIGPM----FNQVVysyptWYIDVSVPEGKTIEFKFIKKDSQGNV-TWESGSNHVYT 665
Cdd:cd05815   10 TQWGQSLLICGSDPLLGSWNVKKGLLLKpshqGDVLV-----WSGSISVPPGFSSEYNYYVVDDRKSVlRSESGEKRKLV 84

                 ....*..
gi 157830769 666 TPTNTTG 672
Cdd:cd05815   85 LPEGLQG 91
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
411-433 6.95e-03

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


Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 35.60  E-value: 6.95e-03
                          10        20
                  ....*....|....*....|...
gi 157830769  411 NGDVYVYERQFGKDVVLVAVNRS 433
Cdd:pfam16657  10 NRKVLAYLREYEDETILVVANRS 32
PLN02960 PLN02960
alpha-amylase
95-139 7.83e-03

alpha-amylase


Pssm-ID: 215519 [Multi-domain]  Cd Length: 897  Bit Score: 39.43  E-value: 7.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 157830769  95 GYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:PLN02960 449 GYKVTNFFAVSSRFGTPDDFKRLVDEAHGLGLLVFLDIVHSYAAA 493
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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