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Conserved domains on  [gi|39625|emb|CAA41773|]
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cyclomaltodextrin glucanotransferase [Paenibacillus macerans]

Protein Classification

alpha-amylase family protein; alpha-amylase family glycosyl hydrolase( domain architecture ID 10183104)

alpha-amylase family protein catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides; alpha-amylase family glycosyl hydrolase functions as a glycoside hydrolase that may act on starch, glycogen, and related oligo- and polysaccharides

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, ...
 38-428 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: 579.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     38 NFSTDVIYQIVTDRFADGDRTNNPAGDA--FSGDRSNLKLYFGGDWQGIIDKIndGYLTGMGVTALWISQPVENITSVIk 115
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGSPglYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPI- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    116 ySGVNNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPADrdnpgFAENGGMYDNGSLLGAYS 195
Cdd:cd11320  78 -EGGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    196 NDTAGLFHHNGGTD-FSTIEDGIYKNLYDLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHMPFGWQKSFVSSIY 274
Cdd:cd11320 152 NDDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIY 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    275 GgDHPVFTFGEWYLG-ADQTDGDNIKFANESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLASTESQYDYINNMVTFID 353
Cdd:cd11320 232 S-KKPVFTFGEWFLGsPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFID 310

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39625    354 NHDMDRFQVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGD----GDPNNRAMMTSFNTGTTAYKVIQALAPLRKS 428
Cdd:cd11320 311 NHDMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
CBM20 super family cl15347
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 613-712 9.21e-51

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.


The actual alignment was detected with superfamily member cd05807:

Pssm-ID: 449530 [Multi-domain]  Cd Length: 101  Bit Score: 171.97  E-value: 9.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    613 DQVTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAIGPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVTWE 691
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKnGDNTVTWE 80

                        90       100
                ....*....|....*....|.
gi 39625    692 GGGNHTYTTPASGVGTVTVDW 712
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
 527-611 5.92e-27

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: 104.35  E-value: 5.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    527 PAIGNVGPTMGQPGNIVTIDGRGFGGTAGTVYFGTTAVTgsgIVSWEDTQIKAVIPKVAAGKTGVSVKTSSGTASNTFKs 606
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAE---VLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGYN- 76


                ....*
gi 39625    607 FNVLT 611
Cdd:cd00604  77 FEVLT 81
Aamy_C smart00632
Aamy_C domain;
438-522 3.72e-18

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 79.59  E-value: 3.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       438 TERWVNND-VLIIERKfgsSAALVAINRNSSaaYPISGLLSSLPAGTYSDVLNGLLNGNSITVGSGGaVTNFTLAAGG-T 515
Cdd:smart00632   1 TNWWDNGDnQIAFERG---SKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74


                   ....*..
gi 39625       516 AVWQYTA 522
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, ...
 38-428 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: 579.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     38 NFSTDVIYQIVTDRFADGDRTNNPAGDA--FSGDRSNLKLYFGGDWQGIIDKIndGYLTGMGVTALWISQPVENITSVIk 115
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGSPglYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPI- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    116 ySGVNNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPADrdnpgFAENGGMYDNGSLLGAYS 195
Cdd:cd11320  78 -EGGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    196 NDTAGLFHHNGGTD-FSTIEDGIYKNLYDLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHMPFGWQKSFVSSIY 274
Cdd:cd11320 152 NDDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIY 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    275 GgDHPVFTFGEWYLG-ADQTDGDNIKFANESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLASTESQYDYINNMVTFID 353
Cdd:cd11320 232 S-KKPVFTFGEWFLGsPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFID 310

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39625    354 NHDMDRFQVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGD----GDPNNRAMMTSFNTGTTAYKVIQALAPLRKS 428
Cdd:cd11320 311 NHDMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 79-400 1.81e-74

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: 243.80  E-value: 1.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       79 GDWQGIIDKINdgYLTGMGVTALWISQPVENitsvikysgvnNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIK 158
Cdd:pfam00128   1 GDLQGIIEKLD--YLKELGVTAIWLSPIFDS-----------PQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      159 VVIDFAPNHTSPA-DRDNPGFAENGGMYDNGSLLGAYSNDT--AGLFHHNGGTDFS----TIEDGIYKNLYDLADINHNN 231
Cdd:pfam00128  68 VILDLVVNHTSDEhAWFQESRSSKDNPYRDYYFWRPGGGPIppNNWRSYFGGSAWTydekGQEYYLHLFVAGQPDLNWEN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      232 NAMDAYFKSAIDLWLGMGVDGIRFDAVKHMPF----------GWQKSF---VSSIYGGDHPVFTFGEWYLGAD---QTDG 295
Cdd:pfam00128 148 PEVRNELYDVVRFWLDKGIDGFRIDVVKHISKvpglpfenngPFWHEFtqaMNETVFGYKDVMTVGEVFHGDGewaRVYT 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      296 DNIKFANESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLasTESQYDYINN---MVTFIDNHDMDRF-QVAGSGTRATE 371
Cdd:pfam00128 228 TEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMI--TDWLDALPDTngwNFTFLGNHDQPRFlSRFGDDRASAK 305

                         330       340
                  ....*....|....*....|....*....
gi 39625      372 QALALTLTSRGVPAIYYGTEQYMTGDGDP 400
Cdd:pfam00128 306 LLAVFLLTLRGTPYIYQGEEIGMTGGNDP 334
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
39-406 1.24e-66

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 225.51  E-value: 1.24e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     39 FSTDVIYQIVTDRFADGDrtnnpagdafsGDrsnlklyFGGDWQGIIDKIndGYLTGMGVTALWISqPVenitsvikYSG 118
Cdd:COG0366   6 WKDAVIYQIYPDSFADSN-----------GD-------GGGDLKGIIEKL--DYLKDLGVDAIWLS-PF--------FPS 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    119 VNntSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSP----------------------ADRDNP 176
Cdd:COG0366  57 PM--SDHGYDISDYRDVDPRFGTLADFDELVAEAHARGIKVILDLVLNHTSDehpwfqearagpdspyrdwyvwRDGKPD 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    177 GFAENGGMYDNGSllgAYSND--TAGLFHHNggtDFSTiedgiyknlydLADINHNNNAMDAYFKSAIDLWLGMGVDGIR 254
Cdd:COG0366 135 LPPNNWFSIFGGS---AWTWDpeDGQYYLHL---FFSS-----------QPDLNWENPEVREELLDVLRFWLDRGVDGFR 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    255 FDAVKHM------------PFGWQKSFVSSIYGGDHPVFTFGEWYlgaDQTDGDNIKFANESGMNL-LDFEYAQEVREVF 321
Cdd:COG0366 198 LDAVNHLdkdeglpenlpeVHEFLRELRAAVDEYYPDFFLVGEAW---VDPPEDVARYFGGDELDMaFNFPLMPALWDAL 274

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    322 RDktETMKDLYEVLASTESQYDYINNMVTFIDNHDMDRF--QVAGS-GTRATEQALALTLTSRGVPAIYYGTEQYMTGD- 397
Cdd:COG0366 275 AP--EDAAELRDALAQTPALYPEGGWWANFLRNHDQPRLasRLGGDyDRRRAKLAAALLLTLPGTPYIYYGDEIGMTGDk 352

                       410
                ....*....|....
gi 39625    398 -GDP----NNRAMM 406
Cdd:COG0366 353 lQDPegrdGCRTPM 366
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 613-712 9.21e-51

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: 171.97  E-value: 9.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    613 DQVTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAIGPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVTWE 691
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKnGDNTVTWE 80

                        90       100
                ....*....|....*....|.
gi 39625    692 GGGNHTYTTPASGVGTVTVDW 712
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
Aamy smart00642
Alpha-amylase domain;
46-170 7.14e-37

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 135.92  E-value: 7.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625        46 QIVTDRFADGDRTNnpagdafsgdrsnlklyfGGDWQGIIDKINdgYLTGMGVTALWISQPVENITSvikysgvnNTSYH 125
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESPQG--------YPSYH 52

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 39625       126 GYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSP 170
Cdd:smart00642  53 GYDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTSD 97
CBM_20 pfam00686
Starch binding domain;
615-710 2.85e-29

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 111.61  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      615 VTVRFLVNqANTNYGTNVYLVGNAAELGSWDPNKAIgPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVTWEGG 693
Cdd:pfam00686   1 VSVTFNVN-ATTQYGQSVYIVGSIPELGNWNPKKAI-ALSASEYSSYPLWSGTVSLPAGTTIEYKYIKVdSDGSVTWESG 78

                          90
                  ....*....|....*..
gi 39625      694 GNHTYTTPASGVGTVTV 710
Cdd:pfam00686  79 PNRSYTVPASGASTTTT 95
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
 527-611 5.92e-27

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: 104.35  E-value: 5.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    527 PAIGNVGPTMGQPGNIVTIDGRGFGGTAGTVYFGTTAVTgsgIVSWEDTQIKAVIPKVAAGKTGVSVKTSSGTASNTFKs 606
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAE---VLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGYN- 76


                ....*
gi 39625    607 FNVLT 611
Cdd:cd00604  77 FEVLT 81
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
 43-477 2.13e-26

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 114.33  E-value: 2.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      43 VIYQIVTDRFADGD-RTNNPAG----------------DAFSGDRSNLKLYFGGDWQGIIDKIndGYLTGMGVTALWISq 105
Cdd:PRK10785 123 VFYQIFPDRFARSLpREAVQDHvyyhhaagqeiilrdwDEPVTAQAGGSTFYGGDLDGISEKL--PYLKKLGVTALYLN- 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     106 PVENITSVikysgvnntsyHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPadrDNPGFAENggmy 185
Cdd:PRK10785 200 PIFTAPSV-----------HKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTGD---SHPWFDRH---- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     186 dNGSLLGAYSNDTAGLFHHnggtdFSTIEDGIY---KNLYDLADINHNN----NAMDAYFKSAIDLWLG--MGVDGIRFD 256
Cdd:PRK10785 262 -NRGTGGACHHPDSPWRDW-----YSFSDDGRAldwLGYASLPKLDFQSeevvNEIYRGEDSIVRHWLKapYNIDGWRLD 335

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     257 AVkHMpFGWQKS------FVSSIYG------------GDHpvftFGE---WyLGADQTDGdnikfanesGMNLLDFeyAQ 315
Cdd:PRK10785 336 VV-HM-LGEGGGarnnlqHVAGITQaakeenpeayvlGEH----FGDarqW-LQADVEDA---------AMNYRGF--AF 397

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     316 EVREVFR-----------DKTETMK--DLYEVLASTESQYDYINNMvtfiDNHDMDRFQVAGSGTRATEQ-ALALTLTSR 381
Cdd:PRK10785 398 PLRAFLAntdiayhpqqiDAQTCAAwmDEYRAGLPHQQQLRQFNQL----DSHDTARFKTLLGGDKARMPlALVWLFTWP 473

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     382 GVPAIYYGTEQYMTGDGDPNNRAMM---TSFNTGTTaYKVIQALAPLRKSNPAIAYGTTTERWVNNDVLIIERKFGSSAA 458
Cdd:PRK10785 474 GVPCIYYGDEVGLDGGNDPFCRKPFpwdEAKQDGAL-LALYQRMIALRKKSQALRRGGCQVLYAEGNVVVFARVLQQQRV 552

                        490       500
                 ....*....|....*....|.
gi 39625     459 LVAINRN--SSAAYPISGLLS 477
Cdd:PRK10785 553 LVAINRGeaCEVVLPASPLLN 573
CBM_2 smart01065
Starch binding domain;
615-702 1.50e-22

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 92.03  E-value: 1.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       615 VTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAIgPMyNQVIAKYPSWYYDVSVP-AGTKLDFKFIKKG-GGTVTWEG 692
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAV-PL-SPDTDGYPLWKGTVSLPpAGTTIEYKYVKVDeDGSVTWES 78

                           90
                   ....*....|
gi 39625       693 GGNHTYTTPA 702
Cdd:smart01065  79 GPNRRLTVPE 88
Aamy_C smart00632
Aamy_C domain;
438-522 3.72e-18

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 79.59  E-value: 3.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       438 TERWVNND-VLIIERKfgsSAALVAINRNSSaaYPISGLLSSLPAGTYSDVLNGLLNGNSITVGSGGaVTNFTLAAGG-T 515
Cdd:smart00632   1 TNWWDNGDnQIAFERG---SKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74


                   ....*..
gi 39625       516 AVWQYTA 522
Cdd:smart00632  75 AIHVDAK 81
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 441-521 1.09e-07

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: 50.03  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      441 WVN-----NDVLIIERKFGSSAALVAINRNSSAAYPisGLLSSLP-AGTYSDVLN-------GLLNGNSITVGSGG--AV 505
Cdd:pfam02806   1 WIDgddaeNNVIAFERGDDGGKLLVVFNFTPSVSYT--DYRTGLPeAGTYCEVLNtddeeygGSNTGEVVTVDGPGhpNS 78

                          90
                  ....*....|....*.
gi 39625      506 TNFTLAAGGTAVWQYT 521
Cdd:pfam02806  79 LTLTLPPLSALVLKVE 94
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 527-603 1.64e-06

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: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 46.29  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      527 PAIGNVGPTMGQP--GNIVTIDGRGFGGTAG--TVYFGTTAVTgsgIVSWEDTQIKAVIPKVAAGKTGVSVKTSSGTASN 602
Cdd:pfam01833   1 PVITSISPSSGPAsgGTTITITGSNFGTDSSdlKVTIGGTPCT---VISVSSTTIVCTTPPGTSGLVNVSVTVGGGGISS 77


                  .
gi 39625      603 T 603
Cdd:pfam01833  78 S 78
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
 144-436 5.12e-05

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: 46.54  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      144 DFQNLIDTAHAHNIKVVIDFAPNHT-----SPADRDNPG--FAENG-GMYDNGSLLGaysNDTAglfhhnggtdfSTIEd 215
Cdd:TIGR02104 230 ELKQMIQALHENGIRVIMDVVYNHTysreeSPFEKTVPGyyYRYNEdGTLSNGTGVG---NDTA-----------SERE- 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      216 giyknlydladinhnnnAMDAYFKSAIDLWLG-MGVDGIRFDA-----VKHMpfGWQKSFVSSIyggDHPVFTFGE-WYL 288
Cdd:TIGR02104 295 -----------------MMRKFIVDSVLYWVKeYNIDGFRFDLmgihdIETM--NEIRKALNKI---DPNILLYGEgWDL 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      289 GADQTDGDNIKFANESGMNLLDFeYAQEVR-----EVFRDK----------TEtMKDLYEVLASTE-----SQYDYINNM 348
Cdd:TIGR02104 353 GTPLPPEQKATKANAYQMPGIAF-FNDEFRdalkgSVFHLKkkgfvsgnpgTE-EIVKKGILGSIEldavkPSALDPSQS 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      349 VTFI---DNHDM-DRFQVAGSG------TRATEQALALTLTSRGVPAIYYGTEQYMTGDGDPNnrammtSFNTG------ 412
Cdd:TIGR02104 431 INYVechDNHTLwDKLSLANPDeteeqlKKRQKLATAILLLSQGIPFLHAGQEFMRTKQGDEN------SYNSPdsinql 504

                         330       340       350
                  ....*....|....*....|....*....|....
gi 39625      413 ----------TTAYkvIQALAPLRKSNPAIAYGT 436
Cdd:TIGR02104 505 dwdrkatfkdDVNY--IKGLIALRKAHPAFRLSS 536
PLN02950 PLN02950
4-alpha-glucanotransferase
 571-710 3.71e-04

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 43.94  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     571 SWEDTQIKAVIPKVAAGKTGVSVKTSSGTASNTFKSFNVLTGDQVTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAI 650
Cdd:PLN02950 109 LWQKSGPEALFFRSAFKDVIFRHSWGVNTERPLGALNKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDDGL 188

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39625     651 GPMYnqviAKYPSWYYDVSVPagtKLDFKF-----IKKGGGTVTWEGGGNHTYTTPASGVGTVTV 710
Cdd:PLN02950 189 KLNY----TGDSIWEADCLVP---KSDFPIkykyaLQTAEGLVSLELGVNRELSLDSSSGKPPSY 246
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 38-428 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: 579.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     38 NFSTDVIYQIVTDRFADGDRTNNPAGDA--FSGDRSNLKLYFGGDWQGIIDKIndGYLTGMGVTALWISQPVENITSVIk 115
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGSPglYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPI- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    116 ySGVNNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPADrdnpgFAENGGMYDNGSLLGAYS 195
Cdd:cd11320  78 -EGGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    196 NDTAGLFHHNGGTD-FSTIEDGIYKNLYDLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHMPFGWQKSFVSSIY 274
Cdd:cd11320 152 NDDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIY 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    275 GgDHPVFTFGEWYLG-ADQTDGDNIKFANESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLASTESQYDYINNMVTFID 353
Cdd:cd11320 232 S-KKPVFTFGEWFLGsPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFID 310

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39625    354 NHDMDRFQVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGD----GDPNNRAMMTSFNTGTTAYKVIQALAPLRKS 428
Cdd:cd11320 311 NHDMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 42-429 9.15e-77

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: 250.25  E-value: 9.15e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     42 DVIYQIVTDRFADGDRTNNPAG--DAFSGDRSNLKLYFGGDWQGIIDKINdgYLTGMGVTALWISQPVENitsviKYSGV 119
Cdd:cd11339   3 ETIYFVMTDRFYDGDPSNDNGGgdGDPRSNPTDNGPYHGGDFKGLIDKLD--YIKDLGFTAIWITPVVKN-----RSVQA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    120 NNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadrdnpgfaenggmydngsllgaysndta 199
Cdd:cd11339  76 GSAGYHGYWGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG------------------------------ 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    200 glfhhnggtdfstiedgiyknlydlaDINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHMPFGWQKSFVSSIYGGDHP 279
Cdd:cd11339 126 --------------------------DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGK 179

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    280 --VFTFGEWYLGADQTDGDNIKFAneSGMNLLDFEYAQEVREVFRDKTETmkDLYEVLASTESQYDYINNMVTFIDNHDM 357
Cdd:cd11339 180 pdFFMFGEVYDGDPSYIAPYTTTA--GGDSVLDFPLYGAIRDAFAGGGSG--DLLQDLFLSDDLYNDATELVTFLDNHDM 255

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    358 DRF-----QVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGDGDPNNRAMMTSFNTGTTA------------YKVIQ 420
Cdd:cd11339 256 GRFlsslkDGSADGTARLALALALLFTSRGIPCIYYGTEQGFTGGGDPDNGRRNMFASTGDLTsaddnfdtdhplYQYIA 335


                ....*....
gi 39625    421 ALAPLRKSN 429
Cdd:cd11339 336 RLNRIRRAY 344
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 79-400 1.81e-74

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: 243.80  E-value: 1.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       79 GDWQGIIDKINdgYLTGMGVTALWISQPVENitsvikysgvnNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIK 158
Cdd:pfam00128   1 GDLQGIIEKLD--YLKELGVTAIWLSPIFDS-----------PQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      159 VVIDFAPNHTSPA-DRDNPGFAENGGMYDNGSLLGAYSNDT--AGLFHHNGGTDFS----TIEDGIYKNLYDLADINHNN 231
Cdd:pfam00128  68 VILDLVVNHTSDEhAWFQESRSSKDNPYRDYYFWRPGGGPIppNNWRSYFGGSAWTydekGQEYYLHLFVAGQPDLNWEN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      232 NAMDAYFKSAIDLWLGMGVDGIRFDAVKHMPF----------GWQKSF---VSSIYGGDHPVFTFGEWYLGAD---QTDG 295
Cdd:pfam00128 148 PEVRNELYDVVRFWLDKGIDGFRIDVVKHISKvpglpfenngPFWHEFtqaMNETVFGYKDVMTVGEVFHGDGewaRVYT 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      296 DNIKFANESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLasTESQYDYINN---MVTFIDNHDMDRF-QVAGSGTRATE 371
Cdd:pfam00128 228 TEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMI--TDWLDALPDTngwNFTFLGNHDQPRFlSRFGDDRASAK 305

                         330       340
                  ....*....|....*....|....*....
gi 39625      372 QALALTLTSRGVPAIYYGTEQYMTGDGDP 400
Cdd:pfam00128 306 LLAVFLLTLRGTPYIYQGEEIGMTGGNDP 334
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
39-406 1.24e-66

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 225.51  E-value: 1.24e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     39 FSTDVIYQIVTDRFADGDrtnnpagdafsGDrsnlklyFGGDWQGIIDKIndGYLTGMGVTALWISqPVenitsvikYSG 118
Cdd:COG0366   6 WKDAVIYQIYPDSFADSN-----------GD-------GGGDLKGIIEKL--DYLKDLGVDAIWLS-PF--------FPS 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    119 VNntSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSP----------------------ADRDNP 176
Cdd:COG0366  57 PM--SDHGYDISDYRDVDPRFGTLADFDELVAEAHARGIKVILDLVLNHTSDehpwfqearagpdspyrdwyvwRDGKPD 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    177 GFAENGGMYDNGSllgAYSND--TAGLFHHNggtDFSTiedgiyknlydLADINHNNNAMDAYFKSAIDLWLGMGVDGIR 254
Cdd:COG0366 135 LPPNNWFSIFGGS---AWTWDpeDGQYYLHL---FFSS-----------QPDLNWENPEVREELLDVLRFWLDRGVDGFR 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    255 FDAVKHM------------PFGWQKSFVSSIYGGDHPVFTFGEWYlgaDQTDGDNIKFANESGMNL-LDFEYAQEVREVF 321
Cdd:COG0366 198 LDAVNHLdkdeglpenlpeVHEFLRELRAAVDEYYPDFFLVGEAW---VDPPEDVARYFGGDELDMaFNFPLMPALWDAL 274

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    322 RDktETMKDLYEVLASTESQYDYINNMVTFIDNHDMDRF--QVAGS-GTRATEQALALTLTSRGVPAIYYGTEQYMTGD- 397
Cdd:COG0366 275 AP--EDAAELRDALAQTPALYPEGGWWANFLRNHDQPRLasRLGGDyDRRRAKLAAALLLTLPGTPYIYYGDEIGMTGDk 352

                       410
                ....*....|....
gi 39625    398 -GDP----NNRAMM 406
Cdd:COG0366 353 lQDPegrdGCRTPM 366
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 43-428 2.12e-61

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: 210.11  E-value: 2.12e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDRTNNPAGDAFSGdrsnlkLYFGGDWQGIIDKINdgYLTGMGVTALWISQPVENITSVIKYSGvnnt 122
Cdd:cd11319  10 SIYQVLTDRFARTDGSSTAPCDTADR------TYCGGTWKGIINKLD--YIQGMGFDAIWISPIVKNIEGNTAYGE---- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 SYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPADRDNPGFAENGGMYDNGS------LLGAYSN 196
Cdd:cd11319  78 AYHGYWAQDLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDYSSFVPFNDSSyyhpycWITDYNN 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    197 DTaglfhhnggtdfsTIEDG-IYKNLYDLADINHNNNAMDAYFKSAI-DLWLGMGVDGIRFDAVKHMPFGWQKSFVSSiy 274
Cdd:cd11319 158 QT-------------SVEDCwLGDDVVALPDLNTENPFVVSTLNDWIkNLVSNYSIDGLRIDTAKHVRKDFWPGFVEA-- 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    275 GGdhpVFTFGEWYlgadqtDGDNIKFAN--ESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLASTESQYDYINNMVTFI 352
Cdd:cd11319 223 AG---VFAIGEVF------DGDPNYVCPyqNYLDGVLNYPLYYPLVDAFQSTKGSMSALVDTINSVQSSCKDPTLLGTFL 293

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39625    353 DNHDMDRFQVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGDGDPNNR-AMMTS-FNTGTTAYKVIQALAPLRKS 428
Cdd:cd11319 294 ENHDNPRFLSYTSDQALAKNALAFTLLSDGIPIIYYGQEQGFNGGNDPYNReALWLSgYDTSSPLYKFIKTLNAIRKA 371
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 40-406 5.41e-53

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: 188.19  E-value: 5.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     40 STDVIYQIVTDRFADGDRTN-NPAGDAFSGDRSNLKLYFGGDWQGIIDKINdgYLTGMGVTALWISQPVENitsvikysG 118
Cdd:cd11340   2 SSDVIYLIMPDRFANGDPSNdSVPGMLEKADRSNPNGRHGGDIQGIIDHLD--YLQDLGVTAIWLTPLLEN--------D 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    119 VNNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPA-----DRDNPGFAENGGMYDNGSLLGA 193
Cdd:cd11340  72 MPSYSYHGYAATDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSEhwwmkDLPTKDWINQTPEYTQTNHRRT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    194 YSNDTaglfhHNGGTDFSTIEDGIYKNlyDLADINHNNNAMDAYF-KSAIdLWLGM-GVDGIRFD----AVKHMPFGWQK 267
Cdd:cd11340 152 ALQDP-----YASQADRKLFLDGWFVP--TMPDLNQRNPLVARYLiQNSI-WWIEYaGLDGIRVDtypySDKDFMSEWTK 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    268 SfVSSIYggdhPVFT-FGE-WYLGADQT----DGDNIKFANESGM-NLLDFEYAQEVREVFRDKTET---MKDLYEVLAS 337
Cdd:cd11340 224 A-IMEEY----PNFNiVGEeWSGNPAIVaywqKGKKNPDGYDSHLpSVMDFPLQDALRDALNEEEGWdtgLNRLYETLAN 298

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39625    338 tESQYDYINNMVTFIDNHDMDRF-QVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGD---GDPNNRAMM 406
Cdd:cd11340 299 -DFLYPDPNNLVIFLDNHDTSRFySQVGEDLDKFKLALALLLTTRGIPQLYYGTEILMKGTkkkDDGAIRRDF 370
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 43-435 1.57e-51

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: 183.84  E-value: 1.57e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDRTNNPAGDAFSGDRSNLKL--------------YFGGDWQGIIDKIndGYLTGMGVTALWISqPVe 108
Cdd:cd11338   3 VFYQIFPDRFANGDPSNDPKGGEYNYFGWPDLPdypppwggeptrrdFYGGDLQGIIEKL--DYLKDLGVNAIYLN-PI- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    109 nITSvikysgvnnTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadRDNPGFAENGgmyDNG 188
Cdd:cd11338  79 -FEA---------PSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTG---DDSPYFQDVL---KYG 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    189 SlLGAYSNDtaglFHHNGGTDFSTIEDGIYK---NLYDLADINHNNNAMDAYFKSAIDLWLGMG-VDGIRFDAVKHMPFG 264
Cdd:cd11338 143 E-SSAYQDW----FSIYYFWPYFTDEPPNYEswwGVPSLPKLNTENPEVREYLDSVARYWLKEGdIDGWRLDVADEVPHE 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    265 WQKSFVSSIYGGDHPVFTFGE-W-----YLGADQTDgdnikfaneSGMNlldFEYAQEVREVFRDKTETMKDLYEVLAST 338
Cdd:cd11338 218 FWREFRKAVKAVNPDAYIIGEvWedarpWLQGDQFD---------SVMN---YPFRDAVLDFLAGEEIDAEEFANRLNSL 285

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    339 ESQY--DYINNMVTFIDNHDMDRFQ-VAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTGDGDPNNRAMM----TSFNT 411
Cdd:cd11338 286 RANYpkQVLYAMMNLLDSHDTPRILtLLGGDKARLKLALALQFTLPGAPCIYYGDEIGLEGGKDPDNRRPMpwdeEKWDQ 365

                       410       420
                ....*....|....*....|....
gi 39625    412 GTTAYkvIQALAPLRKSNPAIAYG 435
Cdd:cd11338 366 DLLEF--YKKLIALRKEHPALRTG 387
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 613-712 9.21e-51

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: 171.97  E-value: 9.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    613 DQVTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAIGPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVTWE 691
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKnGDNTVTWE 80

                        90       100
                ....*....|....*....|.
gi 39625    692 GGGNHTYTTPASGVGTVTVDW 712
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 43-388 4.49e-41

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: 150.79  E-value: 4.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDRTNNpagdafsgdrsnlklYFGGDWQGIIDKINdgYLTGMGVTALWISQPVENITsvikysgvNNT 122
Cdd:cd00551   1 VIYQLFPDRFTDGDSSGG---------------DGGGDLKGIIDKLD--YLKDLGVTAIWLTPIFESPE--------YDG 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 SYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHtspadrdnpgfaenggmydngsllgaysndtaglf 202
Cdd:cd00551  56 YDKDDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH----------------------------------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    203 hhnggtdfstiedgiyknlydladinhnnnamdayfkSAIDLWLGMGVDGIRFDAVKHMPFGWQKSFVSSI----YGGDH 278
Cdd:cd00551 101 -------------------------------------DILRFWLDEGVDGFRLDAAKHVPKPEPVEFLREIrkdaKLAKP 143

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    279 PVFTFGEWYLGADqtDGDNIKFANESGMNLLDFEYAQEVREVFRDKTETMKDLYEVLAstesQYDYINNMVTFIDNHDMD 358
Cdd:cd00551 144 DTLLLGEAWGGPD--ELLAKAGFDDGLDSVFDFPLLEALRDALKGGEGALAILAALLL----LNPEGALLVNFLGNHDTF 217

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 39625    359 RF------QVAGSGTRATEQALALTLTSRGVPAIYY 388
Cdd:cd00551 218 RLadlvsyKIVELRKARLKLALALLLTLPGTPMIYY 253
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 43-425 6.06e-41

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: 155.55  E-value: 6.06e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADG---DRTNNPAGDAFSGD-------RSNLKLYFGGDWQGIIDKIndGYLTGMGVTALWISQPVENIts 112
Cdd:cd11352   1 VLYFLLVDRFSDGkerPRPLFDGNDPAVATwednfgwESQGQRFQGGTLKGVRSKL--GYLKRLGVTALWLSPVFKQR-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    113 viKYSgvnnTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS-----PADRDN---PGFAENGGM 184
Cdd:cd11352  77 --PEL----ETYHGYGIQNFLDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSGdvfsyDDDRPYsssPGYYRGFPN 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    185 YDNGSLLGAYSNDTAGLFHHNG------------------GTDFSTIEDGIYKNLYDLADINHNNNamDAYFKSAIDL-- 244
Cdd:cd11352 151 YPPGGWFIGGDQDALPEWRPDDaiwpaelqnleyytrkgrIRNWDGYPEYKEGDFFSLKDFRTGSG--SIPSAALDILar 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    245 ----WLGMG-VDGIRFDAVKHMPFGWQKSFVSSIYG-----GDHPVFTFGEWYLGADQTDGDNIKFANESGMnlLDFEya 314
Cdd:cd11352 229 vyqyWIAYAdIDGFRIDTVKHMEPGAARYFCNAIKEfaqsiGKDNFFLFGEITGGREAAAYEDLDVTGLDAA--LDIP-- 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    315 qEVREVFRDkteTMK-------------DLYEVLASTESQYDyiNNMVTFIDNHDM------DRFQVAGSGTRATEQALA 375
Cdd:cd11352 305 -EIPFKLEN---VAKglappaeyfqlfeNSKLVGMGSHRWYG--KFHVTFLDDHDQvgrfykKRRAADAAGDAQLAAALA 378

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39625    376 LTLTSRGVPAIYYGTEQYMTGDGD---------------PNNRAMMTSFNTGTTAYKVIQALAPL 425
Cdd:cd11352 379 LNLFTLGIPCIYYGTEQGLDGSGDsdryvreamfggdfgAFRSRGRHFFNEEHPIYRRIAALSEL 443
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 42-435 5.85e-37

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: 143.11  E-value: 5.85e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     42 DVIYQIVTDRFADGDrtnnpagdafsGDRSnlklyfgGDWQGIIDKINdgYLTGMGVTALWISqPvenitsvIKYSgvnn 121
Cdd:cd11316   1 GVFYEIFVRSFYDSD-----------GDGI-------GDLNGLTEKLD--YLNDLGVNGIWLM-P-------IFPS---- 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    122 TSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadRDNPGF--AENggmydngSLLGAY----- 194
Cdd:cd11316  49 PSYHGYDVTDYYAIEPDYGTMEDFERLIAEAHKRGIKVIIDLVINHTS---SEHPWFqeAAS-------SPDSPYrdyyi 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    195 --SNDTAGLFHHNGGTDFSTIEDGIYKNLYD--LADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKH---------- 260
Cdd:cd11316 119 waDDDPGGWSSWGGNVWHKAGDGGYYYGAFWsgMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHiyengegqad 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    261 ----MPFgWQK--SFVSSIYGGdhpVFTFGE-WylgadqTDGDNI-KFANESGMNLLDFEYAQEVREVFR------DKTE 326
Cdd:cd11316 199 qeenIEF-WKEfrDYVKSVKPD---AYLVGEvW------DDPSTIaPYYASGLDSAFNFDLAEAIIDSVKnggsgaGLAK 268

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    327 TMKDLYEVLASTESQYdyinNMVTFIDNHDMDRF--QVAGSGTRAtEQALALTLTSRGVPAIYYGTEQYMTG-DGDPNNR 403
Cdd:cd11316 269 ALLRVYELYAKYNPDY----IDAPFLSNHDQDRVasQLGGDEAKA-KLAAALLLTLPGNPFIYYGEEIGMLGsKPDENIR 343

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    404 AMM---TSFNTGTTA-------------------------YKVIQALAPLRKSNPAIAYG 435
Cdd:cd11316 344 TPMswdADSGAGFTTwipprpntnattasveaqeadpdslLNHYKRLIALRNEYPALARG 403
Aamy smart00642
Alpha-amylase domain;
46-170 7.14e-37

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 135.92  E-value: 7.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625        46 QIVTDRFADGDRTNnpagdafsgdrsnlklyfGGDWQGIIDKINdgYLTGMGVTALWISQPVENITSvikysgvnNTSYH 125
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESPQG--------YPSYH 52

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 39625       126 GYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSP 170
Cdd:smart00642  53 GYDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTSD 97
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
 43-435 5.32e-32

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: 127.28  E-value: 5.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGdrtnnpagdafsgdrsnlklyfgGDWQGIIDKIndGYLTGMGVTALWISqPVENITSVIKYSGVNnt 122
Cdd:cd11313   6 VIYEVNVRQFTPE-----------------------GTFKAVTKDL--PRLKDLGVDILWLM-PIHPIGEKNRKGSLG-- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 syHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPadrDNPGFAENGGMYD---NGSLlgaysndta 199
Cdd:cd11313  58 --SPYAVKDYRAVNPEYGTLEDFKALVDEAHDRGMKVILDWVANHTAW---DHPLVEEHPEWYLrdsDGNI--------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    200 glfhHNGGTDFStiedgiyknlyDLADINHNNNAMDAYFKSAIDLWLGM-GVDGIRFDaVKHM---PFgWQKSF--VSSI 273
Cdd:cd11313 124 ----TNKVFDWT-----------DVADLDYSNPELRDYMIDAMKYWVREfDVDGFRCD-VAWGvplDF-WKEARaeLRAV 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    274 yggDHPVFTFGEWYlgadqtdgdnikfanESGMNLL----DFEYAQEVREVFRD---KTETMKDLYEVLASTESQYDYIN 346
Cdd:cd11313 187 ---KPDVFMLAEAE---------------PRDDDELysafDMTYDWDLHHTLNDvakGKASASDLLDALNAQEAGYPKNA 248

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    347 NMVTFIDNHDMDRFQVAGSGTRATEQALALTLTSRGVPAIYYGTEQYMTG-----DGDP---NNRAMMTSFntgttaykv 418
Cdd:cd11313 249 VKMRFLENHDENRWAGTVGEGDALRAAAALSFTLPGMPLIYNGQEYGLDKrpsffEKDPidwTKNHDLTDL--------- 319

                       410
                ....*....|....*..
gi 39625    419 IQALAPLRKSNPAIAYG 435
Cdd:cd11313 320 YQKLIALKKENPALRGG 336
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
 614-714 1.52e-29

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: 112.69  E-value: 1.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    614 QVTVRFLV-NQANTNYGTNVYLVGNAAELGSW--DPNKAIGPMynqVIAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVT 689
Cdd:cd05820   2 QIPVIFTVqNTPETAPGEFLYLTGSVPELGNWstSTDQAVGPL---LCPNWPDWFVVASVPAGTYIEFKFLKApADGTGT 78

                        90       100
                ....*....|....*....|....*
gi 39625    690 WEGGGNHTYTTPASGVGTVTVDWQN 714
Cdd:cd05820  79 WEGGSNHAYTTPSGGTGTVTVTWQR 103
CBM_20 pfam00686
Starch binding domain;
615-710 2.85e-29

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 111.61  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      615 VTVRFLVNqANTNYGTNVYLVGNAAELGSWDPNKAIgPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVTWEGG 693
Cdd:pfam00686   1 VSVTFNVN-ATTQYGQSVYIVGSIPELGNWNPKKAI-ALSASEYSSYPLWSGTVSLPAGTTIEYKYIKVdSDGSVTWESG 78

                          90
                  ....*....|....*..
gi 39625      694 GNHTYTTPASGVGTVTV 710
Cdd:pfam00686  79 PNRSYTVPASGASTTTT 95
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 617-712 1.34e-27

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: 107.00  E-value: 1.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    617 VRFLVNqANTNYGTNVYLVGNAAELGSWDPNKAIGPMYNQViakYPSWYYDVSVPA--GTKLDFKFIKK-GGGTVTWEGG 693
Cdd:cd05467   2 VRFQVR-CTTQFGQSVYVVGSHPELGNWDPAKALRLNTSNS---YPLWTGEIPLPApeGQVIEYKYVIVdDDGNVQWESG 77

                        90
                ....*....|....*....
gi 39625    694 GNHTYTTPASGVGTVTVDW 712
Cdd:cd05467  78 SNRVLTVPSTSSLIVVDDW 96
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
 43-403 5.52e-27

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: 114.48  E-value: 5.52e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKIndGYLTGMGVTALWISqPVenitsvikYS--GVN 120
Cdd:cd11333   4 VVYQIYPRSFKDSN------GDGI------------GDLPGIISKL--DYLKDLGVDAIWLS-PI--------YPspQVD 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    121 NtsyhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS---P------ADRDNP--GF-----AENGGM 184
Cdd:cd11333  55 N----GYDISDYRAIDPEFGTMEDFDELIKEAHKRGIKIIMDLVVNHTSdehPwfqesrSSRDNPyrDYyiwrdGKDGKP 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    185 YDN-GSLLG----AYSNDTaGLFhhnggtdfstiedgiYKNLYDL--ADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDA 257
Cdd:cd11333 131 PNNwRSFFGgsawEYDPET-GQY---------------YLHLFAKeqPDLNWENPEVRQEIYDMMRFWLDKGVDGFRLDV 194

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    258 VKH---------MPFGWQKSFVSSIYGGDHP------------------VFTFGEwylgADQTDGDN-IKFANES--GMN 307
Cdd:cd11333 195 INLiskdpdfpdAPPGDGDGLSGHKYYANGPgvheylqelnrevfskydIMTVGE----APGVDPEEaLKYVGPDrgELS 270

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    308 LL-DFEYA---QEVREVFRDKTETMKDLYEVLASTESQYDYINNMVTFIDNHDM----DRFqvaGSGTRATEQ---ALA- 375
Cdd:cd11333 271 MVfNFEHLdldYGPGGKWKPKPWDLEELKKILSKWQKALQGDGWNALFLENHDQprsvSRF---GNDGEYRVEsakMLAt 347

                       410       420
                ....*....|....*....|....*...
gi 39625    376 LTLTSRGVPAIYYGTEQYMTgdgdpNNR 403
Cdd:cd11333 348 LLLTLRGTPFIYQGEEIGMT-----NSR 370
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
 527-611 5.92e-27

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: 104.35  E-value: 5.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    527 PAIGNVGPTMGQPGNIVTIDGRGFGGTAGTVYFGTTAVTgsgIVSWEDTQIKAVIPKVAAGKTGVSVKTSSGTASNTFKs 606
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAE---VLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGYN- 76


                ....*
gi 39625    607 FNVLT 611
Cdd:cd00604  77 FEVLT 81
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
 43-477 2.13e-26

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 114.33  E-value: 2.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      43 VIYQIVTDRFADGD-RTNNPAG----------------DAFSGDRSNLKLYFGGDWQGIIDKIndGYLTGMGVTALWISq 105
Cdd:PRK10785 123 VFYQIFPDRFARSLpREAVQDHvyyhhaagqeiilrdwDEPVTAQAGGSTFYGGDLDGISEKL--PYLKKLGVTALYLN- 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     106 PVENITSVikysgvnntsyHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPadrDNPGFAENggmy 185
Cdd:PRK10785 200 PIFTAPSV-----------HKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTGD---SHPWFDRH---- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     186 dNGSLLGAYSNDTAGLFHHnggtdFSTIEDGIY---KNLYDLADINHNN----NAMDAYFKSAIDLWLG--MGVDGIRFD 256
Cdd:PRK10785 262 -NRGTGGACHHPDSPWRDW-----YSFSDDGRAldwLGYASLPKLDFQSeevvNEIYRGEDSIVRHWLKapYNIDGWRLD 335

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     257 AVkHMpFGWQKS------FVSSIYG------------GDHpvftFGE---WyLGADQTDGdnikfanesGMNLLDFeyAQ 315
Cdd:PRK10785 336 VV-HM-LGEGGGarnnlqHVAGITQaakeenpeayvlGEH----FGDarqW-LQADVEDA---------AMNYRGF--AF 397

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     316 EVREVFR-----------DKTETMK--DLYEVLASTESQYDYINNMvtfiDNHDMDRFQVAGSGTRATEQ-ALALTLTSR 381
Cdd:PRK10785 398 PLRAFLAntdiayhpqqiDAQTCAAwmDEYRAGLPHQQQLRQFNQL----DSHDTARFKTLLGGDKARMPlALVWLFTWP 473

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     382 GVPAIYYGTEQYMTGDGDPNNRAMM---TSFNTGTTaYKVIQALAPLRKSNPAIAYGTTTERWVNNDVLIIERKFGSSAA 458
Cdd:PRK10785 474 GVPCIYYGDEVGLDGGNDPFCRKPFpwdEAKQDGAL-LALYQRMIALRKKSQALRRGGCQVLYAEGNVVVFARVLQQQRV 552

                        490       500
                 ....*....|....*....|.
gi 39625     459 LVAINRN--SSAAYPISGLLS 477
Cdd:PRK10785 553 LVAINRGeaCEVVLPASPLLN 573
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 615-711 4.95e-24

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: 96.96  E-value: 4.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    615 VTVRFLVNqANTNYGTNVYLVGNAAELGSWDPNKAIGPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKKG-GGTVTWEGG 693
Cdd:cd05811   7 VAVTFNER-VTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKEsDGSVTWESD 85

                        90
                ....*....|....*...
gi 39625    694 GNHTYTTPASGVGTVTVD 711
Cdd:cd05811  86 PNRSYTVPSGCGTTATVD 103
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 615-712 1.15e-23

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: 95.51  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    615 VTVRFLVNqANTNYGTNVYLVGNAAELGSWDPNKAIgPMYNqviAKYPSWYYDVSVPAGTKLDFKFIKK-GGGTVTWEGG 693
Cdd:cd05808   1 VAVTFNVT-ATTVWGQNVYVVGNVPELGNWSPANAV-ALSA---ATYPVWSGTVDLPAGTAIEYKYIKKdGSGTVTWESG 75

                        90
                ....*....|....*....
gi 39625    694 GNHTYTTPASGVGTVTVDW 712
Cdd:cd05808  76 PNRTATTPASGTLTLNDTW 94
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 85-437 2.28e-23

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: 101.83  E-value: 2.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     85 IDKIND--GYLTGMGVTALWISqPVENITSvikysgvnntsyHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVID 162
Cdd:cd11337  27 LLKLEDwlPHLKELGCNALYLG-PVFESDS------------HGYDTRDYYRIDRRLGTNEDFKALVAALHERGIRVVLD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    163 FAPNHTSpadRDNPgfaenggmydngsllgaysndtaglFHHNggtdfstiedgiyknlYDLADINHNNNAMDAYFKSAI 242
Cdd:cd11337  94 GVFNHVG---RDFF-------------------------WEGH----------------YDLVKLNLDNPAVVDYLFDVV 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    243 DLWLGMG-VDGIRFDAVKHMPFGWQK---SFVSSIyggdHPVFtfgeWYLGaDQTDGDNIKFANESGM------------ 306
Cdd:cd11337 130 RFWIEEFdIDGLRLDAAYCLDPDFWRelrPFCREL----KPDF----WLMG-EVIHGDYNRWVNDSMLdsvtnyelykgl 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    307 -------NLldFEYAQEVREVFRDKtetmkDLYEVLastesqydyinNMVTFIDNHDMDRfqVAGSGTRATEQALALTL- 378
Cdd:cd11337 201 wsshndhNF--FEIAHSLNRLFRHN-----GLYRGF-----------HLYTFVDNHDVTR--IASILGDKAHLPLAYALl 260

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    379 -TSRGVPAIYYGTEQYMTG------DGD----PNNRAMMTSFNTGTTAYkvIQALAPLRKSNPAIAYGTT 437
Cdd:cd11337 261 fTMPGIPSIYYGSEWGIEGvkeegsDADlrplPLRPAELSPLGNELTRL--IQALIALRRRSPALCYGSY 328
CBM_2 smart01065
Starch binding domain;
615-702 1.50e-22

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 92.03  E-value: 1.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       615 VTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAIgPMyNQVIAKYPSWYYDVSVP-AGTKLDFKFIKKG-GGTVTWEG 692
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAV-PL-SPDTDGYPLWKGTVSLPpAGTTIEYKYVKVDeDGSVTWES 78

                           90
                   ....*....|
gi 39625       693 GGNHTYTTPA 702
Cdd:smart01065  79 GPNRRLTVPE 88
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
 85-435 3.43e-21

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: 96.09  E-value: 3.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     85 IDKIND--GYLTGMGVTALWISqPVenitsvikysgvNNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVID 162
Cdd:cd11353  29 ILKLEDwiPHLKKLGINAIYFG-PV------------FESDSHGYDTRDYYKIDRRLGTNEDFKAVCKKLHENGIKVVLD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    163 FAPNHTSpadRDNPGFA---ENGgmydNGSllgAYSNDTAGL-FHHNG--GTDFStiedgiYKNL---YDLADINHNNNA 233
Cdd:cd11353  96 GVFNHVG---RDFFAFKdvqENR----ENS---PYKDWFKGVnFDGNSpyNDGFS------YEGWeghYELVKLNLHNPE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    234 MDAYFKSAIDLWLG-MGVDGIRFDAVKHMPFGWQK---SFVSSIyggdHPVFtfgeWYLGaDQTDGDNIKFANEsgmNLL 309
Cdd:cd11353 160 VVDYLFDAVRFWIEeFDIDGLRLDVADCLDFDFLRelrDFCKSL----KPDF----WLMG-EVIHGDYNRWAND---EML 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    310 D----FEYAQEVREVFRDktetmKDLYEVLASTESQYD----YIN-NMVTFIDNHDMDRfqVAGSGTRATEQALALTL-- 378
Cdd:cd11353 228 DsvtnYECYKGLYSSHND-----HNYFEIAHSLNRQFGlegiYRGkHLYNFVDNHDVNR--IASILKNKEHLPPIYALlf 300

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39625    379 TSRGVPAIYYGTEQYMTGD----GDPNNRA-----MMTSFNTGTTAYkvIQALAPLRKSNPAIAYG 435
Cdd:cd11353 301 TMPGIPSIYYGSEWGIEGVkgngSDAALRPaldepELSGENNELTDL--IAKLARIRRASPALCYG 364
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 125-437 1.04e-20

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: 94.32  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    125 HGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadRDNPGFAEnggmydngSLLGAYSNDTAGLFHH 204
Cdd:cd11354  59 HGYDTLDHYRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVG---RSHPAVAQ--------ALEDGPGSEEDRWHGH 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    205 NGGTDFSTIEDGiyknlYDLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHMP--FgWQKsfVSSIYGGDHP-VF 281
Cdd:cd11354 128 AGGGTPAVFEGH-----EDLVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPpeF-WAR--VLPRVRERHPdAW 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    282 TFGEwylgadQTDGDNIKFANESGMN-LLDFEYAQEVREVFRDktetmKDLYEVLASTESQYDYINNMV--TFIDNHDMD 358
Cdd:cd11354 200 ILGE------VIHGDYAGIVAASGMDsVTQYELWKAIWSSIKD-----RNFFELDWALGRHNEFLDSFVpqTFVGNHDVT 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    359 RF--QVagsGTRATEQALALTLTSRGVPAIYYGTEQYMTGD------GD----------PNNRAmmtsfNTGTTAYKVIQ 420
Cdd:cd11354 269 RIasQV---GDDGAALAAAVLFTVPGIPSIYYGDEQGFTGVkeeragGDdavrpafpasPAELA-----PLGEWIYRLHQ 340

                       330
                ....*....|....*..
gi 39625    421 ALAPLRKSNPAIAYGTT 437
Cdd:cd11354 341 DLIGLRRRHPWLHRART 357
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 81-518 1.28e-19

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 92.64  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      81 WQGIIDKINDgyLTGMGVTALWISqPVenitsvikYSGVNNTSYHGYWARD------FKQ---TNDAFGDFADFQNLIDT 151
Cdd:PRK09441  21 WNRLAERAPE--LAEAGITAVWLP-PA--------YKGTSGGYDVGYGVYDlfdlgeFDQkgtVRTKYGTKEELLNAIDA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     152 AHAHNIKVVIDFAPNH--------------TSPADRDNP-----------GFAENGGMydngsllGAYSNDTAGlFHHNG 206
Cdd:PRK09441  90 LHENGIKVYADVVLNHkagadeketfrvveVDPDDRTQIisepyeiegwtRFTFPGRG-------GKYSDFKWH-WYHFS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     207 GTDFSTI--EDGIYKNLYD-------------------LADINHNNNAMD-------AYFKSAidlwlgMGVDGIRFDAV 258
Cdd:PRK09441 162 GTDYDENpdESGIFKIVGDgkgwddqvddengnfdylmGADIDFRHPEVReelkywaKWYMET------TGFDGFRLDAV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     259 KHMPFGWQKSFVSSI--YGGDhPVFTFGE-WylgadQTDGDNIK-FANES--GMNLLDFEYAQEVREVFrdKTETMKDLY 332
Cdd:PRK09441 236 KHIDAWFIKEWIEHVreVAGK-DLFIVGEyW-----SHDVDKLQdYLEQVegKTDLFDVPLHYNFHEAS--KQGRDYDMR 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     333 EVLASTESQYDYiNNMVTFIDNHDMDRFQVAGSG--TRATEQALALTLT-SRGVPAI----YYGTEQYMTGDGDPNnram 405
Cdd:PRK09441 308 NIFDGTLVEADP-FHAVTFVDNHDTQPGQALESPvePWFKPLAYALILLrEEGYPCVfygdYYGASGYYIDMPFKE---- 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     406 mtsfntgttaykVIQALAPLRKSnpaIAYGTTTERWVNNDVLIIERK-FGSSAALVAINRNSSAAYPISGLLSSLPAGTY 484
Cdd:PRK09441 383 ------------KLDKLLLARKN---FAYGEQTDYFDHPNCIGWTRSgDEENPGLAVVISNGDAGEKTMEVGENYAGKTW 447

                        490       500       510
                 ....*....|....*....|....*....|....
gi 39625     485 SDVLNGllNGNSITVGSGGAVTnFTLAAGGTAVW 518
Cdd:PRK09441 448 RDYTGN--RQETVTIDEDGWGT-FPVNGGSVSVW 478
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 43-397 2.68e-19

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: 91.09  E-value: 2.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKINdgYLTGMGVTALWIS----QPVENitsvikysg 118
Cdd:cd11334   6 VIYQLDVRTFMDSN------GDGI------------GDFRGLTEKLD--YLQWLGVTAIWLLpfypSPLRD--------- 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    119 vnntsyHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadRDNPGFAEngGMYDNGSLLGAYS--N 196
Cdd:cd11334  57 ------DGYDIADYYGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTS---DQHPWFQA--ARRDPDSPYRDYYvwS 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    197 DTAGLFHHNgGTDFSTIEDGIYKnlYDLA--------------DINHNNNA-MDAYFKsAIDLWLGMGVDGIRFDAVKHM 261
Cdd:cd11334 126 DTPPKYKDA-RIIFPDVEKSNWT--WDEVagayywhrfyshqpDLNFDNPAvREEILR-IMDFWLDLGVDGFRLDAVPYL 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    262 -------------PFGWQK---SFVSSIYGG-------DHPVFTFGEwYLGadqtDGDNIKFA-NESGMNLLDFEYAQEV 317
Cdd:cd11334 202 ieregtncenlpeTHDFLKrlrAFVDRRYPDaillaeaNQWPEEVRE-YFG----DGDELHMAfNFPLNPRLFLALARED 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    318 REVFRDKTETMKDLYEVlasteSQYdyinnmVTFIDNHD---------------MDRF------QVAGSG---------- 366
Cdd:cd11334 277 AFPIIDALRQTPPIPEG-----CQW------ANFLRNHDeltlemltdeerdyvYAAFapdprmRIYNRGirrrlapmlg 345

                       410       420       430
                ....*....|....*....|....*....|...
gi 39625    367 --TRATEQALALTLTSRGVPAIYYGTEQYMtGD 397
Cdd:cd11334 346 gdRRRIELAYSLLFSLPGTPVIYYGDEIGM-GD 377
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
 43-261 3.82e-19

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: 91.14  E-value: 3.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKIndGYLTGMGVTALWISqPVenitsvikYSGVNNT 122
Cdd:cd11328   9 VFYQIYPRSFKDSD------GDGI------------GDLKGITEKL--DYFKDIGIDAIWLS-PI--------FKSPMVD 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 SyhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS--------PADRDnPGFAE-----NGGMYDNGS 189
Cdd:cd11328  60 F--GYDISDFTDIDPIFGTMEDFEELIAEAKKLGLKVILDFVPNHSSdehewfqkSVKRD-EPYKDyyvwhDGKNNDNGT 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    190 L------LGAYS------NDTAGLFH-HNggtdFStiedgiyknlYDLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFD 256
Cdd:cd11328 137 RvppnnwLSVFGgsawtwNEERQQYYlHQ----FA----------VKQPDLNYRNPKVVEEMKNVLRFWLDKGVDGFRID 202


                ....*
gi 39625    257 AVKHM 261
Cdd:cd11328 203 AVPHL 207
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
 41-261 4.64e-19

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: 90.50  E-value: 4.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     41 TDVIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKIndGYLTGMGVTALWISqpvenitSVIKYSGVN 120
Cdd:cd11359   5 TSVIYQIYPRSFKDSN------GDGN------------GDLKGIREKL--DYLKYLGVKTVWLS-------PIYKSPMKD 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    121 NtsyhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpaDRdNPGFAE---NGGMYDNGSLLGAYSND 197
Cdd:cd11359  58 F----GYDVSDFTDIDPMFGTMEDFERLLAAMHDRGMKLIMDFVPNHTS--DK-HEWFQLsrnSTNPYTDYYIWADCTAD 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39625    198 TAGLFHHN-----GGT--DFSTIEDGIYKNLYDLA--DINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHM 261
Cdd:cd11359 131 GPGTPPNNwvsvfGNSawEYDEKRNQCYLHQFLKEqpDLNFRNPDVQQEMDDVLRFWLDKGVDGFRVDAVKHL 203
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
 41-395 9.43e-19

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: 89.69  E-value: 9.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     41 TDVIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKIndGYLTGMGVTALWIS----QPVENItsviky 116
Cdd:cd11331   5 TGVIYQIYPRSFQDSN------GDGV------------GDLRGIISRL--DYLSDLGVDAVWLSpiypSPMADF------ 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    117 sgvnntsyhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS---P------ADRDNP--------GFA 179
Cdd:cd11331  59 ---------GYDVSDYCGIDPLFGTLEDFDRLVAEAHARGLKVILDFVPNHTSdqhPwflesrSSRDNPkrdwyiwrDPA 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    180 ENGGMYDNG-SLLGAYSndtaglFHHNGGTDFStiedgiYKNLY--DLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFD 256
Cdd:cd11331 130 PDGGPPNNWrSEFGGSA------WTWDERTGQY------YLHAFlpEQPDLNWRNPEVRAAMHDVLRFWLDRGVDGFRVD 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    257 AVKHM----------------PFGWQKSFVSSIYGGDHP------------VFTF------GEWYLGADQ------TDGD 296
Cdd:cd11331 198 VLWLLikdpqfrdnppnpdwrGGMPPHERLLHIYTADQPetheivremrrvVDEFgdrvliGEIYLPLDRlvayygAGRD 277

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    297 NIKFA-NesgMNLLDFEY-AQEVREVFRDktetmkdlYEVLASTESQYDYinnmvtFIDNHDMDRFqVAGSGTRATEQAL 374
Cdd:cd11331 278 GLHLPfN---FHLISLPWdAAALARAIEE--------YEAALPAGAWPNW------VLGNHDQPRI-ASRVGPAQARVAA 339

                       410       420
                ....*....|....*....|.
gi 39625    375 ALTLTSRGVPAIYYGTEQYMT 395
Cdd:cd11331 340 MLLLTLRGTPTLYYGDELGME 360
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 79-432 2.88e-18

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: 87.33  E-value: 2.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     79 GDWQGIIDKINdgYLTGMGVTALWIsQPVENItsvikysgVNNTSYhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIK 158
Cdd:cd11350  30 GDFKGVIDKLD--YLQDLGVNAIEL-MPVQEF--------PGNDSW-GYNPRHYFALDKAYGTPEDLKRLVDECHQRGIA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    159 VVIDFAPNHtspADRDNPgFAEnggMYdngsllgaysNDTAGLFHHNGGTDFSTIEDGIYknlYDLADINHNNNAMDAYF 238
Cdd:cd11350  98 VILDVVYNH---AEGQSP-LAR---LY----------WDYWYNPPPADPPWFNVWGPHFY---YVGYDFNHESPPTRDFV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    239 KSAIDLWLG-MGVDGIRFDAVKHMpfgWQKSF-VSSIYGGDHPVFTFGEWYLGADQTDGDNI-----KFANESGMNLLDF 311
Cdd:cd11350 158 DDVNRYWLEeYHIDGFRFDLTKGF---TQKPTgGGAWGGYDAARIDFLKRYADEAKAVDKDFyviaeHLPDNPEETELAT 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    312 EYAQEVREVFRDKTE-TMKDLYEVLASTESQYDYIN------NMVTFIDNHD----MDRFQVAGSGT-----------RA 369
Cdd:cd11350 235 YGMSLWGNSNYSFSQaAMGYQGGSLLLDYSGDPYQNggwspkNAVNYMESHDeerlMYKLGAYGNGNsylginletalKR 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39625    370 TEQALALTLTSRGVPAIY------YGTEQYMTGDGDPNNRAMMTSFNT---GTTAYKVIQALAPLRKSNPAI 432
Cdd:cd11350 315 LKLAAAFLFTAPGPPMIWqggefgYDYSIPEDGRGTTLPKPIRWDYLYdpeRKRLYELYRKLIKLRREHPAL 386
Aamy_C smart00632
Aamy_C domain;
438-522 3.72e-18

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 79.59  E-value: 3.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       438 TERWVNND-VLIIERKfgsSAALVAINRNSSaaYPISGLLSSLPAGTYSDVLNGLLNGNSITVGSGGaVTNFTLAAGG-T 515
Cdd:smart00632   1 TNWWDNGDnQIAFERG---SKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74


                   ....*..
gi 39625       516 AVWQYTA 522
Cdd:smart00632  75 AIHVDAK 81
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
 43-258 7.20e-18

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: 86.93  E-value: 7.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKINdgYLTGMGVTALWISqPVenITSVIKYsgvnnt 122
Cdd:cd11330   7 VIYQIYPRSFLDSN------GDGI------------GDLPGITEKLD--YIASLGVDAIWLS-PF--FKSPMKD------ 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 syHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSP---------ADRDNPgFA---------ENGGM 184
Cdd:cd11330  58 --FGYDVSDYCAVDPLFGTLDDFDRLVARAHALGLKVMIDQVLSHTSDqhpwfeesrQSRDNP-KAdwyvwadpkPDGSP 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    185 YDNG-SLLG--AYSNDT--AGLFHHNggtdFstiedgiyknLYDLADIN-HNNNAMDAYFKSAiDLWLGMGVDGIRFDAV 258
Cdd:cd11330 135 PNNWlSVFGgsAWQWDPrrGQYYLHN----F----------LPSQPDLNfHNPEVQDALLDVA-RFWLDRGVDGFRLDAV 199
malS PRK09505
alpha-amylase; Reviewed
 44-171 8.19e-18

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 87.80  E-value: 8.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      44 IYQIVTDRFADGDRTNnpagdafsgDRS---------NLKLYFGGDWQGIIDKINdgYLTGMGVTALWISQPVENITSVI 114
Cdd:PRK09505 192 VYFVLTDRFENGDPSN---------DHSygrhkdgmqEIGTFHGGDLRGLTEKLD--YLQQLGVNALWISSPLEQIHGWV 260

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39625     115 kySGVNNTS-----YHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPA 171
Cdd:PRK09505 261 --GGGTKGDfphyaYHGYYTLDWTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTGYA 320
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 107-356 1.02e-17

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: 85.41  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    107 VENITSVIKYSGVNNTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHT---SPADRDNPgfaengg 183
Cdd:cd11315  32 TSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQLGTEDDFKALCAAAHKYGIKIIVDVVFNHManeGSAIEDLW------- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    184 mYDNGSLLGAYSNDtaglFHHNGG-TDFSTIEDGIYKNLYDLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKHMP 262
Cdd:cd11315 105 -YPSADIELFSPED----FHGNGGiSNWNDRWQVTQGRLGGLPDLNTENPAVQQQQKAYLKALVALGVDGFRFDAAKHIE 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    263 ----FGWQKSFVSSIYGGDHP--VFTFGEWYLGADQTDGDNIKFAneSGMNLLDFEYAQEVREVFRDKtetmkdlyEVLA 336
Cdd:cd11315 180 lpdePSKASDFWTNILNNLDKdgLFIYGEVLQDGGSRDSDYASYL--SLGGVTASAYGFPLRGALKNA--------FLFG 249

                       250       260
                ....*....|....*....|....*
gi 39625    337 STESQYDYI-----NNMVTFIDNHD 356
Cdd:cd11315 250 GSLDPASYGqalpsDRAVTWVESHD 274
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
 43-296 1.19e-17

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: 86.56  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKIndGYLTGMGVTALWISqPVenitsvikysgvnnt 122
Cdd:cd11332   7 VVYQVYPRSFADAN------GDGI------------GDLAGIRARL--PYLAALGVDAIWLS-PF--------------- 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 sY------HGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS-------PADRDNPG--------FAEN 181
Cdd:cd11332  51 -YpspmadGGYDVADYRDVDPLFGTLADFDALVAAAHELGLRVIVDIVPNHTSdqhpwfqAALAAGPGsperaryiFRDG 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    182 GGmyDNGSLLgaySNDTAGLFhhnGGTDFS--TIEDGI----YKNLYDLA--DINHNNNAMDAYFKSAIDLWLGMGVDGI 253
Cdd:cd11332 130 RG--PDGELP---PNNWQSVF---GGPAWTrvTEPDGTdgqwYLHLFAPEqpDLNWDNPEVRAEFEDVLRFWLDRGVDGF 201

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 39625    254 RFDA----VKHM-----PFGWQKSFVSsiyGGDHPVF-------TFGEWYLGADQTDGD 296
Cdd:cd11332 202 RIDVahglAKDPglpdaPGGGLPVGER---PGSHPYWdrdevhdIYREWRAVLDEYDPP 257
CBM20_beta_amylase cd05809
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ...
 615-712 4.44e-17

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: 76.90  E-value: 4.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    615 VTVRFLVNQANTNYGTNVYLVGNAAELGSWDpnKAIGPMYNQVIAKYPSWYYDVSVPAGTKLDFKFIKK--GGGTVTWEG 692
Cdd:cd05809   3 VPQTFVVKNVPTTIGETVYITGSRAELGNWD--TKQYPIQLYYNSHSNDWRGTVHLPAGRNIEFKAIKKskDGTNKSWQG 80

                        90       100
                ....*....|....*....|
gi 39625    693 GGNHTYTTPaSGVGTVTVDW 712
Cdd:cd05809  81 GQQSWYPVP-LGTTSYTSSW 99
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 615-707 3.99e-15

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: 71.29  E-value: 3.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    615 VTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAI--GPMYnqviakYPSWYYDVSVPAGTKLDFKFIKK----GGGTV 688
Cdd:cd05810   1 VSVTFSCNNGTTQLGQSVYVVGNVPQLGNWSPADAVklDPTA------YPTWSGSISLPASTNVEWKCLKRnetnPTAGV 74

                        90
                ....*....|....*....
gi 39625    689 TWEGGGNHTYTTPASGVGT 707
Cdd:cd05810  75 QWQGGGNNQLTTGNSTAST 93
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 76-388 7.51e-13

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: 69.94  E-value: 7.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     76 YFGGDWQGII-DKINDgyLTGMGVTALWISQPVEnitSVIKYSgvnntsyHGYWARDFKQTNDAFGDFADFQNLIDTAHA 154
Cdd:cd11314  11 PKDGTWWNHLeSKAPE--LAAAGFTAIWLPPPSK---SVSGSS-------MGYDPGDLYDLNSRYGSEAELRSLIAALHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    155 HNIKVVIDFAPNHTSPADrdnpgfaenggmydngsllgaysndtaglfhhnGGTDFSTIEdgiyknlydlaDINHNN--- 231
Cdd:cd11314  79 KGIKVIADIVINHRSGPD---------------------------------TGEDFGGAP-----------DLDHTNpev 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    232 -NAMDAYFKsaidlWL--GMGVDGIRFDAVKhmpfGWQKSFVSSIYGGDHPVFTFGEWYLGADQTDGDN-----IKFANE 303
Cdd:cd11314 115 qNDLKAWLN-----WLknDIGFDGWRFDFVK----GYAPSYVKEYNEATSPSFSVGEYWDGLSYENQDAhrqrlVDWIDA 185

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    304 SGMN--LLDF---EYAQEV---REVFRDKTETMKDLyeVLASTESQYdyinnMVTFIDNHDMDRFQVAGSG-TRATEQAL 374
Cdd:cd11314 186 TGGGsaAFDFttkYILQEAvnnNEYWRLRDGQGKPP--GLIGWWPQK-----AVTFVDNHDTGSTQGHWPFpTDNVLQGY 258

                       330
                ....*....|....
gi 39625    375 ALTLTSRGVPAIYY 388
Cdd:cd11314 259 AYILTHPGTPCVFW 272
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 92-389 5.65e-12

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: 67.93  E-value: 5.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     92 YLTGMGVTALWISQPvenitsvikYSGVNNTSYHGYWARD------FKQTNDA---FGDFADFQNLIDTAHAHNIKVVID 162
Cdd:cd11318  28 ELAELGITAVWLPPA---------YKGASGTEDVGYDVYDlydlgeFDQKGTVrtkYGTKEELLEAIKALHENGIQVYAD 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    163 FAPNH--------------TSPADRDNPG-------------FAENGGMYD---------NGSLLGAYSNDTAGLFHHNG 206
Cdd:cd11318  99 AVLNHkagadetetvkaveVDPNDRNKEIsepyeieawtkftFPGRGGKYSdfkwnwqhfSGVDYDQKTKKKGIFKINFE 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    207 GTDFSTIEDGIYKNlYD---LADINHNNNAMDAYFKSAIDlWLG--MGVDGIRFDAVKHMPFGWQKSFVSSI--YGGdHP 279
Cdd:cd11318 179 GKGWDEDVDDENGN-YDylmGADIDYSNPEVREELKRWGK-WYIntTGLDGFRLDAVKHISASFIKDWIDHLrrETG-KD 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    280 VFTFGE----------WYLgaDQTDGDnikfanesgMNLLD-------FEYAQEV-----REVFRDkteTMKDLYEVLAs 337
Cdd:cd11318 256 LFAVGEywsgdlealeDYL--DATDGK---------MSLFDvplhynfHEASKSGgnydlRKIFDG---TLVQSRPDKA- 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 39625    338 tesqydyinnmVTFIDNHDMdrfQVAGSGTRATE-----QALALTLTSR-GVPAIYYG 389
Cdd:cd11318 321 -----------VTFVDNHDT---QPGQSLESWVEpwfkpLAYALILLRKdGYPCVFYG 364
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 43-394 1.10e-11

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: 67.33  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDrtnnpaGDAFsgdrsnlklyfgGDWQGIIDKINdgYLTGMGVTALWISqPVenITSVIKYSgvnnt 122
Cdd:cd11348   1 VFYEIYPQSFYDSN------GDGI------------GDLQGIISKLD--YIKSLGCNAIWLN-PC--FDSPFKDA----- 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    123 syhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadRDNPGF-----AENG---GMY---DNGSLL 191
Cdd:cd11348  53 ---GYDVRDYYKVAPRYGTNEDLVRLFDEAHKRGIHVLLDLVPGHTS---DEHPWFkeskkAENNeysDRYiwtDSIWSG 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    192 GAYSNDTAGLFHHNGGT-------------DFSTIEDGIYKNLYDLADINHNNNAMdayfKSAIDLWLGMGVDGIRFDA- 257
Cdd:cd11348 127 GPGLPFVGGEAERNGNYivnffscqpalnyGFAHPPTEPWQQPVDAPGPQATREAM----KDIMRFWLDKGADGFRVDMa 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    258 ---VKHMPFG------WQKsfVSSIYGGDHPVFTF-GEWylgadqtdGDNIKfANESGMN---LLDFE---YAQEVREVF 321
Cdd:cd11348 203 dslVKNDPGNketiklWQE--IRAWLDEEYPEAVLvSEW--------GNPEQ-SLKAGFDmdfLLHFGgngYNSLFRNLN 271

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    322 RDKTETMKDLY----------EVLASTESQYDYI--NNMVTFID-NHDMDRFqvagSGTRATEQ---ALALTLTSRGVPA 385
Cdd:cd11348 272 TDGGHRRDNCYfdasgkgdikPFVDEYLPQYEATkgKGYISLPTcNHDTPRL----NARLTEEElklAFAFLLTMPGVPF 347


                ....*....
gi 39625    386 IYYGTEQYM 394
Cdd:cd11348 348 IYYGDEIGM 356
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
 43-258 2.57e-10

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 63.61  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      43 VIYQIVTDRFAD--GDRTnnpagdafsgdrsnlklyfgGDWQGIIDKINdgYLTGMGVTALWIsqpveniTSVIKYSGVN 120
Cdd:PRK10933  12 VIYQIYPKSFQDttGSGT--------------------GDLRGVTQRLD--YLQKLGVDAIWL-------TPFYVSPQVD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     121 NtsyhGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS--------PADRDNPgfAENGGMYDNGSlLG 192
Cdd:PRK10933  63 N----GYDVANYTAIDPTYGTLDDFDELVAQAKSRGIRIILDMVFNHTStqhawfreALNKESP--YRQFYIWRDGE-PE 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     193 AYSNDTAGLFhhnGGTDFSTIEDG--IYKNLY--DLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAV 258
Cdd:PRK10933 136 TPPNNWRSKF---GGSAWRWHAESeqYYLHLFapEQADLNWENPAVRAELKKVCEFWADRGVDGLRLDVV 202
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 616-703 1.19e-09

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: 55.80  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    616 TVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAIgPMYNqviAKYPSWYYDVSVPAGT-KLDFKFI--KKGGGTVTWEG 692
Cdd:cd05816   1 VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKAL-KLSD---VGFPIWEADIDISKDSfPFEYKYIiaNKDSGVVSWEN 76

                        90
                ....*....|.
gi 39625    693 GGNHTYTTPAS 703
Cdd:cd05816  77 GPNRELSAPSL 87
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
 44-163 1.91e-09

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: 60.77  E-value: 1.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     44 IYQIVTDRFADGDRTNNPA-GDAFSGDRSNLKLYFGGDWQGIIDKINdgYLTGMGVTAL------WISQPvenitsviky 116
Cdd:cd11323  58 FYTIFLDRFVNGDPTNDDAnGTVFEQDIYETQLRHGGDIVGLVDSLD--YLQGMGIKGIyiagtpFINMP---------- 125

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 39625    117 sgvnnTSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDF 163
Cdd:cd11323 126 -----WGADGYSPLDFTLLDHHFGTIADWRAAIDEIHRRGMYVVLDN 167
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 615-696 2.44e-09

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: 55.22  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    615 VTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAI--GPMYNQVIAKYPS-WYYDVSVPAGTKLD---FKFIKKGGGTV 688
Cdd:cd05806   1 MLFRFGVVLTFADRDTELLVLGSRPELGSWDPQRAVpmRPARKALSPQEPSlWLGEVELSEPGSEDtfwYKFLKREAGAL 80


                ....*...
gi 39625    689 TWEGGGNH 696
Cdd:cd05806  81 IWEGNGPH 88
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
76-256 5.45e-09

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


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 59.90  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625       76 YFGGDWQGIIDKI----NDGYLTGMGVTALWISqPVENITSVIKYSGVNNTSYHGYWARDFKQTND--AFGDFADFQNLI 149
Cdd:PRK14510  175 FFPGNLRGTFAKLaapeAISYLKKLGVSIVELN-PIFASVDEHHLPQLGLSNYWGYNTVAFLAPDPrlAPGGEEEFAQAI 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      150 DTAHAHNIKVVIDFAPNHTSPADRDNPGfaenggmydngslLGAYSNDTAGLFHHNGGTDFSTIEDGIYKNLYDLADINH 229
Cdd:PRK14510  254 KEAQSAGIAVILDVVFNHTGESNHYGPT-------------LSAYGSDNSPYYRLEPGNPKEYENWWGCGNLPNLERPFI 320

                         170       180
                  ....*....|....*....|....*..
gi 39625      230 NNNAMDayfksAIDLWLGMGVDGIRFD 256
Cdd:PRK14510  321 LRLPMD-----VLRSWAKRGVDGFRLD 342
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 139-359 6.64e-09

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: 57.96  E-value: 6.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    139 FGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpADRDNpgfAENGgmydngsllgaysndtaglfhhnggtdfstiedgiy 218
Cdd:cd11317  62 SGTEAEFRDMVNRCNAAGVRVYVDAVINHMA-GDANE---VRNC------------------------------------ 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    219 kNLYDLADINHNN----NAMDAYFKSAIDlwlgMGVDGIRFDAVKHMPfgwqKSFVSSIYGG--DHPVFTFGE---WYL- 288
Cdd:cd11317 102 -ELVGLADLNTESdyvrDKIADYLNDLIS----LGVAGFRIDAAKHMW----PEDLAAILARlkDLNGGPLGSrpyIYQe 172

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39625    289 -----GADQTDGDNIKFAnesgmNLLDFEYAQEVREVFRDKTetmKDLYEVLASTESQYDYINNMVTFIDNHDMDR 359
Cdd:cd11317 173 vidggGEAIQPSEYTGNG-----DVTEFRYARGLSNAFRGKI---KLLLLKNFGEGWGLLPSERAVVFVDNHDNQR 240
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 43-391 7.32e-09

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: 58.45  E-value: 7.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     43 VIYQIVTDRFADGDRTNNPAGD-AFSGdrsnlklyfggdwQGIIDKIND---GYLTGMGVTALWIsqpveniTSVIKYSG 118
Cdd:cd11349   2 IIYQLLPRLFGNKNTTNIPNGTiEENG-------------VGKFNDFDDtalKEIKSLGFTHVWY-------TGVIRHAT 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    119 VNNTSYHG----------------YWARDFKQTN-----DAFGDFADFQNLIDTAHAHNIKVVIDFAPNH--------TS 169
Cdd:cd11349  62 QTDYSAYGippddpdivkgragspYAIKDYYDVDpdlatDPTNRMEEFEALVERTHAAGLKVIIDFVPNHvarqyhsdAK 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    170 PAD------RDNPGFA---ENGGMYDNGSLLGA-----YSNDTAGLFHH-------NGGTDFS-TIEDgiyknLYDLADI 227
Cdd:cd11349 142 PEGvkdfgaNDDTSKAfdpSNNFYYLPGEPFVLpfslnGSPATDGPYHEspakatgNDCFSAApSIND-----WYETVKL 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    228 N-----------HNNNAMDAYFK--SAIDLWLGMGVDGIRFDAVkHM---PFgWqkSFVSSIYGGDHPVFTF-GEWYLGA 290
Cdd:cd11349 217 NygvdydgggsfHFDPIPDTWIKmlDILLFWAAKGVDGFRCDMA-EMvpvEF-W--HWAIPEIKARYPELIFiAEIYNPG 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    291 DQTDgdnikFANESGMNLLdfeYaqevrevfrDKtetmKDLYEVLASTESQY--------------DYINNMVTFIDNHD 356
Cdd:cd11349 293 LYRD-----YLDEGGFDYL---Y---------DK----VGLYDTLRAVICGGgsaseitvwwqesdDIADHMLYFLENHD 351

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 39625    357 MDRFQ---VAGSGTRATeQALALTLT-SRGVPAIYYGTE 391
Cdd:cd11349 352 EQRIAspfFAGNAEKAL-PAMVVSATlSTGPFMLYFGQE 389
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
 54-267 1.68e-08

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: 57.58  E-value: 1.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     54 DGDRTNNPagDAF-SGDRSNLKLY---FGGDWQGIIDKINdgYLTGMGVTALWI-----SQPVENitsvikySGvnntsy 124
Cdd:cd11324  56 DLAREADP--DWFqSPDMVGYALYvdlFAGDLKGLAEKIP--YLKELGVTYLHLmpllkPPEGDN-------DG------ 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    125 hGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTS-------PADRDNPGFAENGGMYDNGSLLGAYSN- 196
Cdd:cd11324 119 -GYAVSDYREVDPRLGTMEDLRALAAELRERGISLVLDFVLNHTAdehewaqKARAGDPEYQDYYYMFPDRTLPDAYERt 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    197 ------DTA-GLFHHNGG------TDFSTIEdgiyknlYDLadiNHNN----NAMdayfkSAIDLWLG-MGVDGIRFDAV 258
Cdd:cd11324 198 lpevfpDTApGNFTWDEEmgkwvwTTFNPFQ-------WDL---NYANpavfNEM-----LDEMLFLAnQGVDVLRLDAV 262


                ....*....
gi 39625    259 khmPFGWQK 267
Cdd:cd11324 263 ---AFIWKR 268
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 614-712 2.90e-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: 51.74  E-value: 2.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    614 QVTVRFLVNQaNTNYGTNVYLVGNAAELGSWDPNKAIGPMYNqviakypSWYYDVSVPAGTKLDFKF-IKKGGGTVTWEG 692
Cdd:cd05818   1 KVKLQVRLDH-QVKFGEHVAILGSTKELGSWKKKVPMNWTEN-------GWVCDLELDGGELVEYKFvIVKRDGSVIWEG 72

                        90       100
                ....*....|....*....|
gi 39625    693 GGNHTYTTPASGVGTVTVDW 712
Cdd:cd05818  73 GNNRVLELPKEGNFEIVCHW 92
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 441-521 1.09e-07

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: 50.03  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      441 WVN-----NDVLIIERKFGSSAALVAINRNSSAAYPisGLLSSLP-AGTYSDVLN-------GLLNGNSITVGSGG--AV 505
Cdd:pfam02806   1 WIDgddaeNNVIAFERGDDGGKLLVVFNFTPSVSYT--DYRTGLPeAGTYCEVLNtddeeygGSNTGEVVTVDGPGhpNS 78

                          90
                  ....*....|....*.
gi 39625      506 TNFTLAAGGTAVWQYT 521
Cdd:pfam02806  79 LTLTLPPLSALVLKVE 94
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
 92-176 3.71e-07

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


Pssm-ID: 200475 [Multi-domain]  Cd Length: 660  Bit Score: 53.65  E-value: 3.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     92 YLTGMGVTALWISqPVenITSVikySGvnntSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPA 171
Cdd:cd11336  22 YLADLGISHLYAS-PI--LTAR---PG----STHGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVS 91


                ....*
gi 39625    172 DRDNP 176
Cdd:cd11336  92 GAENP 96
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 136-260 6.21e-07

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: 52.38  E-value: 6.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    136 NDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSpadRDNPGFAENGGmyDNGSLLGAYS-NDTAGLFHHN------GGT 208
Cdd:cd11329 108 NNSYGVESDLKELVKTAKQKDIKVILDLTPNHSS---KQHPLFKDSVL--KEPPYRSAFVwADGKGHTPPNnwlsvtGGS 182

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 39625    209 DFSTIEDGIYKnLY----DLADINHNNNAMDAYFKSAIDLWLGMGVDGIRFDAVKH 260
Cdd:cd11329 183 AWKWVEDRQYY-LHqfgpDQPDLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY 237
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
 139-261 9.20e-07

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: 51.76  E-value: 9.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    139 FGDFADFQNLIDTAHAHNIKVVIDFAPNHtspadrdnpgFAenggmydngsllgaysNDTAGLFHHNGGTDF-STIEDGI 217
Cdd:cd11322 104 YGTPDDFKYFVDACHQAGIGVILDWVPGH----------FP----------------KDDHGLARFDGTPLYeYPDPRKG 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 39625    218 YKNLYDLADINHNNNAMDAYFKSAIDLWLG-MGVDGIRFDAVKHM 261
Cdd:cd11322 158 EHPDWGTLNFDYGRNEVRSFLISNALYWLEeYHIDGLRVDAVSSM 202
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 527-603 1.64e-06

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: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 46.29  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      527 PAIGNVGPTMGQP--GNIVTIDGRGFGGTAG--TVYFGTTAVTgsgIVSWEDTQIKAVIPKVAAGKTGVSVKTSSGTASN 602
Cdd:pfam01833   1 PVITSISPSSGPAsgGTTITITGSNFGTDSSdlKVTIGGTPCT---VISVSSTTIVCTTPPGTSGLVNVSVTVGGGGISS 77


                  .
gi 39625      603 T 603
Cdd:pfam01833  78 S 78
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
 64-333 8.37e-06

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: 48.59  E-value: 8.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     64 DAFSGDrSNLKlyfggdwqGIIDKINdgYLTGMGVTALWISqPVeNITSVIKYSGVNntsyhgywardFKQTNDAFGDFA 143
Cdd:cd11345  25 QAFSEA-GGLK--------GVEGKLD--YLSQLKVKGLVLG-PI-HVVQADQPGELN-----------LTEIDPDLGTLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    144 DFQNLIDTAHAHNIKVVIDFAPNHtspadRDNPGFAEnggmydngsllgaysndtaglfhhnggtdfstiedgiyknlyd 223
Cdd:cd11345  81 DFTSLLTAAHKKGISVVLDLTPNY-----RGESSWAF------------------------------------------- 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    224 ladiNHNNNAMDAyFKSAIDLWLGMGVDGIRF----DAVKHMPFGWQK--SFVSSIYGGDHPVFtfgewYLGADQTDGDN 297
Cdd:cd11345 113 ----SDAENVAEK-VKEALEFWLNQGVDGIQVsdleNVASSASSEWSNltAIVQKNTDGKKRVL-----IGVTSSSSLSE 182

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 39625    298 IKFA-NESGMNLLDFEY--AQEVREVFRdktETMKDLYE 333
Cdd:cd11345 183 ISLLlNTSGVDLLLSGAllSASNRPSFG---TLVTQLLS 218
AmyAc_1 cd11347
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 134-389 1.23e-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: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    134 QTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPadrDNPGFAENGGMYDNGSllGAYSNDTAGLFHHNGGTDFSTI 213
Cdd:cd11347  93 TVNPDLGGEDDLAALRERLAARGLKLMLDFVPNHVAL---DHPWVEEHPEYFIRGT--DEDLARDPANYTYYGGNILAHG 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    214 EDGIYKNLYDLADINHNNNAMDAYfksAIDLWLGMG--VDGIRFD-----------------AVKHMP--FgWQKSF--V 270
Cdd:cd11347 168 RDPYFPPWTDTAQLNYANPATRAA---MIETLLKIAsqCDGVRCDmamlllndvfertwgsrLYGPPSeeF-WPEAIsaV 243

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    271 SSiyggDHPVFTF-------GEWYLgadQTDGdnikFanesgmnllDFEYaqevrevfrDktetmKDLYEVLAS------ 337
Cdd:cd11347 244 KA----RHPDFIFiaevywdLEWEL---QQLG----F---------DYTY---------D-----KRLYDRLRHgdaevv 289

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 39625    338 ---TESQYDYINNMVTFIDNHDMDRFQVAGSGTRAtEQALALTLTSRGVPAIYYG 389
Cdd:cd11347 290 ryhLSADLDYQSHLVRFIENHDEPRAAAKFGPERH-RAAALITLTLPGMRLFHQG 343
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 527-611 3.39e-05

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 [Multi-domain]  Cd Length: 89  Bit Score: 42.83  E-value: 3.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    527 PAIGNVGPTMG--QPGNIVTIDGRGFG-GTAGTVYFGTTAVTgsGIVSWEDTQIKAVIPKVAAGKTG---VSVKTSSGTA 600
Cdd:cd00102   1 PVITSISPSSGpvSGGTEVTITGSNFGsGSNLRVTFGGGVPC--SVLSVSSTAIVCTTPPYANPGPGpveVTVDRGNGGI 78

                        90
                ....*....|.
gi 39625    601 SNTFKSFNVLT 611
Cdd:cd00102  79 TSSPLTFTYVP 89
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
 144-436 5.12e-05

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: 46.54  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      144 DFQNLIDTAHAHNIKVVIDFAPNHT-----SPADRDNPG--FAENG-GMYDNGSLLGaysNDTAglfhhnggtdfSTIEd 215
Cdd:TIGR02104 230 ELKQMIQALHENGIRVIMDVVYNHTysreeSPFEKTVPGyyYRYNEdGTLSNGTGVG---NDTA-----------SERE- 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      216 giyknlydladinhnnnAMDAYFKSAIDLWLG-MGVDGIRFDA-----VKHMpfGWQKSFVSSIyggDHPVFTFGE-WYL 288
Cdd:TIGR02104 295 -----------------MMRKFIVDSVLYWVKeYNIDGFRFDLmgihdIETM--NEIRKALNKI---DPNILLYGEgWDL 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      289 GADQTDGDNIKFANESGMNLLDFeYAQEVR-----EVFRDK----------TEtMKDLYEVLASTE-----SQYDYINNM 348
Cdd:TIGR02104 353 GTPLPPEQKATKANAYQMPGIAF-FNDEFRdalkgSVFHLKkkgfvsgnpgTE-EIVKKGILGSIEldavkPSALDPSQS 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      349 VTFI---DNHDM-DRFQVAGSG------TRATEQALALTLTSRGVPAIYYGTEQYMTGDGDPNnrammtSFNTG------ 412
Cdd:TIGR02104 431 INYVechDNHTLwDKLSLANPDeteeqlKKRQKLATAILLLSQGIPFLHAGQEFMRTKQGDEN------SYNSPdsinql 504

                         330       340       350
                  ....*....|....*....|....*....|....
gi 39625      413 ----------TTAYkvIQALAPLRKSNPAIAYGT 436
Cdd:TIGR02104 505 dwdrkatfkdDVNY--IKGLIALRKAHPAFRLSS 536
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 623-700 6.31e-05

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: 42.46  E-value: 6.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    623 QANTNYGTNVYLVGNAAELGSWDPNKAIGPMYNQviakYPSWYYDVSVPAGTKLDFKFI---KKGGGTVTWEGGGNHTYT 699
Cdd:cd05817   7 HYPTQFGEAVYISGNCNQLGNWNPSKAKRMQWNE----GDLWTVDVGIPESVYIEYKYFvsnYDDPNTVLWESGPNRVLR 82


                .
gi 39625    700 T 700
Cdd:cd05817  83 T 83
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
91-176 7.12e-05

malto-oligosyltrehalose synthase;


Pssm-ID: 237740 [Multi-domain]  Cd Length: 879  Bit Score: 46.12  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      91 GYLTGMGVTALWISqPVenITSVikySGvnntSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSP 170
Cdd:PRK14511  27 PYFADLGVSHLYLS-PI--LAAR---PG----STHGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAV 96


                 ....*.
gi 39625     171 ADRDNP 176
Cdd:PRK14511  97 GGPDNP 102
PLN02361 PLN02361
alpha-amylase
 81-388 8.16e-05

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 45.58  E-value: 8.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625      81 WQGIIDKINDgyLTGMGVTALWISQPVENItsvikysgvnntSYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVV 160
Cdd:PLN02361  28 WRNLEGKVPD--LAKSGFTSAWLPPPSQSL------------APEGYLPQNLYSLNSAYGSEHLLKSLLRKMKQYNVRAM 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     161 IDFAPNHTSPADRDnpgfaeNGGMYD--NGSLLG----AYSNDTAGLFHHNGGTDFstieDGIyknlydlADINHNNNam 234
Cdd:PLN02361  94 ADIVINHRVGTTQG------HGGMYNryDGIPLPwdehAVTSCTGGLGNRSTGDNF----NGV-------PNIDHTQH-- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     235 daYFKSAIDLWL-----GMGVDGIRFDAVKhmpfGWQKSFVSSIYGGDHPVFTFGEW-----YLGADQTDGDNIKFANES 304
Cdd:PLN02361 155 --FVRKDIIGWLiwlrnDVGFQDFRFDFAK----GYSAKFVKEYIEAAKPLFSVGEYwdscnYSGPDYRLDYNQDSHRQR 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     305 GMNLLDFEYAQEVREVFRDK---TETMKDLYEVLASTESQYDYINNM-----VTFIDNHDmdrfqvAGSgTRA------- 369
Cdd:PLN02361 229 IVNWIDGTGGLSAAFDFTTKgilQEAVKGQWWRLRDAQGKPPGVMGWwpsraVTFIDNHD------TGS-TQAhwpfpsd 301

                        330       340
                 ....*....|....*....|
gi 39625     370 -TEQALALTLTSRGVPAIYY 388
Cdd:PLN02361 302 hIMEGYAYILTHPGIPTVFY 321
PRK12313 PRK12313
1,4-alpha-glucan branching protein GlgB;
126-276 1.28e-04

1,4-alpha-glucan branching protein GlgB;


Pssm-ID: 237052 [Multi-domain]  Cd Length: 633  Bit Score: 45.28  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     126 GYWARDFKqtndaFGDFADFQNLIDTAHAHNIKVVIDFAPNHtspadrdnpgFAENG---GMYDnGSLLGAYSNDTAGlF 202
Cdd:PRK12313 208 GYFAPTSR-----YGTPEDFMYLVDALHQNGIGVILDWVPGH----------FPKDDdglAYFD-GTPLYEYQDPRRA-E 270

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39625     203 HHNGGTdfstiedgiyknlydlADINHNNNAMDAYFKSAIDLWLG-MGVDGIRFDAVKHM---PFGWQKSFVSSIYGG 276
Cdd:PRK12313 271 NPDWGA----------------LNFDLGKNEVRSFLISSALFWLDeYHLDGLRVDAVSNMlylDYDEEGEWTPNKYGG 332
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
123-176 1.63e-04

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 45.09  E-value: 1.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 39625      123 SYHGYWARDFKQTNDAFGDFADFQNLIDTAHAHNIKVVIDFAPNHTSPADRDNP 176
Cdd:PRK14507  787 STHGYDIVDHSQINPEIGGEEGFERFCAALKAHGLGQLLDIVPNHMGVGGADNP 840
PLN02950 PLN02950
4-alpha-glucanotransferase
 571-710 3.71e-04

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 43.94  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     571 SWEDTQIKAVIPKVAAGKTGVSVKTSSGTASNTFKSFNVLTGDQVTVRFLVNQANTNYGTNVYLVGNAAELGSWDPNKAI 650
Cdd:PLN02950 109 LWQKSGPEALFFRSAFKDVIFRHSWGVNTERPLGALNKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDDGL 188

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39625     651 GPMYnqviAKYPSWYYDVSVPagtKLDFKF-----IKKGGGTVTWEGGGNHTYTTPASGVGTVTV 710
Cdd:PLN02950 189 KLNY----TGDSIWEADCLVP---KSDFPIkykyaLQTAEGLVSLELGVNRELSLDSSSGKPPSY 246
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
78-167 5.15e-04

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


Pssm-ID: 440065 [Multi-domain]  Cd Length: 625  Bit Score: 43.20  E-value: 5.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     78 GGDWQGIIDKINDgYLTGMGVTAL-------------WISQPVenitsvikysgvnntsyhGYWA---RdfkqtndaFGD 141
Cdd:COG0296 162 FLTYRELAERLVP-YLKELGFTHIelmpvaehpfdgsWGYQPT------------------GYFAptsR--------YGT 214

                        90       100
                ....*....|....*....|....*.
gi 39625    142 FADFQNLIDTAHAHNIKVVIDFAPNH 167
Cdd:COG0296 215 PDDFKYFVDACHQAGIGVILDWVPNH 240
AmyAc_Glg_debranch cd11326
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ...
 92-256 4.54e-03

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: 40.14  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625     92 YLTGMGVTAL-------WISQPVENITSVIKYSGVNNTSY----HGYWARDfkqtnDAFGDFADFQNLIDTAHAHNIKVV 160
Cdd:cd11326  52 YLKELGVTAVellpvhaFDDEEHLVERGLTNYWGYNTLNFfapdPRYASDD-----APGGPVDEFKAMVKALHKAGIEVI 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39625    161 IDFAPNHTSPADRDNP-----GFaenggmyDNGSllgAYSNDTAGLFHHN----GGTdfstiedgiyknlydladINHNN 231
Cdd:cd11326 127 LDVVYNHTAEGGELGPtlsfrGL-------DNAS---YYRLDPDGPYYLNytgcGNT------------------LNTNH 178

                       170       180       190
                ....*....|....*....|....*....|..
gi 39625    232 NA-----MDA--YFKSAidlwlgMGVDGIRFD 256
Cdd:cd11326 179 PVvlrliLDSlrYWVTE------MHVDGFRFD 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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