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Conserved domains on  [gi|1093953596|ref|NP_001333709|]
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alpha-amylase 1C precursor [Homo sapiens]

Protein Classification

alpha-amylase family protein( domain architecture ID 10183021)

alpha-amylase family protein catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-416 0e+00

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: 581.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 105 GVRIYVDAVINHMCGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLSGLLDLA 184
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 185 LGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNwfPEGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953596 345 AHPYGFTRVMSSYRWPryfengkdvNDWVGPPND-NGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317   266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 1.82e-30

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 1.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 1093953596  502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-416 0e+00

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: 581.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 105 GVRIYVDAVINHMCGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLSGLLDLA 184
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 185 LGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNwfPEGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953596 345 AHPYGFTRVMSSYRWPryfengkdvNDWVGPPND-NGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317   266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 1.82e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 1.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 1093953596  502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-120 1.74e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.49  E-value: 1.74e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596   28 IVHLFEWR-------WVDIALECErYLAPKGFGGVQVSPPNENVaihnPFRPWWERYQPVSYKLC-TRSGNEDEFRNMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
gi 1093953596  100 RCNNVGVRIYVDAVINHMCGN 120
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 421-508 9.84e-17

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: 75.45  E-value: 9.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 421 FTNWYDNGSNQVAFGRGN---RGFIVFNNDDWTFSLTLQTGLP-AGTYCDVISGDKIN--GNCTGIKIYVSDDGKAHFSI 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 1093953596 495 SNSAEDPFIAIHAE 508
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 3.65e-13

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: 70.46  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsSTCGSYFNPgSRDFPAVPYS-GWDFNDGKCKTGS 160
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQE-SRSSKDNPYRdYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 161 GDIENYNDATQVRDCRLSG----------LLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLH 230
Cdd:pfam00128 111 NNWRSYFGGSAWTYDEKGQeyylhlfvagQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 231 NLNS-----NWFPEGSKP-FIYQEVIDLGGEPIKSSDYFGNGRVTE----FKYGAKLGTVIrKWNGEK--MSYLKNWGEG 298
Cdd:pfam00128 191 FWHEftqamNETVFGYKDvMTVGEVFHGDGEWARVYTTEARMELEMgfnfPHNDVALKPFI-KWDLAPisARKLKEMITD 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1093953596 299 W-GFMP--SDRALVFVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 270 WlDALPdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 7.85e-12

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 67.20  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsstcgSYFNP---GSRDFPAVPYSGW----DFNDGKCKTGSG 161
Cdd:COG0366    76 GTLADFDELVAEAHARGIKVILDLVLNHT--------------SDEHPwfqEARAGPDSPYRDWyvwrDGKPDLPPNNWF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 162 DIENYNDATQVRDCR-------LSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMW-----PGDIKAILDKL 229
Cdd:COG0366   142 SIFGGSAWTWDPEDGqyylhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 230 HNLNSNWFPEGSKPFIYQEVIdlGGEPIKSSDYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEGwgfMPSD 305
Cdd:COG0366   222 RELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEG 296

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1093953596 306 RALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366   297 GWWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
PLN02784 PLN02784
alpha-amylase
 15-227 3.53e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 56.17  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  15 AQYSSNTQQGRTSIVHLFEW------RWVDIALECERYLAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTR 87
Cdd:PLN02784  492 IKICSGTGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVS------P--EGYMPKDlYNLNSR 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  88 SGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSA-GTSSTCGSYFNPGSRdfpAVPYSGWDFNdGKCKTGSGDieNY 166
Cdd:PLN02784  564 YGTIDELKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQnGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGD--NF 637

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093953596 167 NDATQVRDcrlsglldlalGKDYVRSKIAEYMNHLID-IGVAGFRIDASKHMWPGDIKAILD 227
Cdd:PLN02784  638 HAAPNIDH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYME 688
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-416 0e+00

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: 581.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 105 GVRIYVDAVINHMCGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLSGLLDLA 184
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 185 LGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNwfPEGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953596 345 AHPYGFTRVMSSYRWPryfengkdvNDWVGPPND-NGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317   266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 28-420 4.53e-50

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: 175.16  E-value: 4.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  28 IVHLFEWRWVDIALECERyLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRS-GNEDEFRNMVTRCNNVGV 106
Cdd:cd11315     4 ILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 107 RIYVDAVINHMcgnavsagTSSTCGSYFNPGSRDFPAVPYSGWDFNDGkcktgsgDIENYNDATQVRDCRLSGLLDLALG 186
Cdd:cd11315    83 KIIVDVVFNHM--------ANEGSAIEDLWYPSADIELFSPEDFHGNG-------GISNWNDRWQVTQGRLGGLPDLNTE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 187 KDYVRSKIAEYMNHLIDIGVAGFRIDASKHM-------WPGD-IKAILDKLHNLNsnwfpegskPFIYQEVIDLGGEPIK 258
Cdd:cd11315   148 NPAVQQQQKAYLKALVALGVDGFRFDAAKHIelpdepsKASDfWTNILNNLDKDG---------LFIYGEVLQDGGSRDS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 259 S-SDYFGNGRVTEFKYGAKL-GTVIRKWNGEKMSYLKNWGEGwgfMPSDRALVFVDNHDNQrGHGAGGASILTFWDARly 336
Cdd:cd11315   219 DyASYLSLGGVTASAYGFPLrGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY-NNDGFESTGLDDEDER-- 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 337 kMAVGFMLAHPYGFtrvmssyrwPRYF---ENGKDVNDWVGPpndngvtkevtinpdttCGNDWVCEHrwrQIRNMVNFR 413
Cdd:cd11315   293 -LAWAYLAARDGGT---------PLFFsrpNGSGGTNPQIGD-----------------RGDDAWKSP---DVVAVNKFH 342


                  ....*..
gi 1093953596 414 NVVDGQP 420
Cdd:cd11315   343 NAMHGQP 349
Aamy_C smart00632
Aamy_C domain;
422-510 1.82e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 1.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 1093953596  502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-120 1.74e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.49  E-value: 1.74e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596   28 IVHLFEWR-------WVDIALECErYLAPKGFGGVQVSPPNENVaihnPFRPWWERYQPVSYKLC-TRSGNEDEFRNMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
gi 1093953596  100 RCNNVGVRIYVDAVINHMCGN 120
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 421-508 9.84e-17

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: 75.45  E-value: 9.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 421 FTNWYDNGSNQVAFGRGN---RGFIVFNNDDWTFSLTLQTGLP-AGTYCDVISGDKIN--GNCTGIKIYVSDDGKAHFSI 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 1093953596 495 SNSAEDPFIAIHAE 508
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 45-347 9.95e-17

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: 79.91  E-value: 9.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  45 RYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYqpvSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHmcgnavsa 124
Cdd:cd00551    32 DYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLD---YYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 125 gtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrlsglldlalgkdyvrskiaEYMNHLIDI 204
Cdd:cd00551   101 -----------------------------------------------------------------------DILRFWLDE 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 205 GVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEgskPFIYQEVIDlGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKW 284
Cdd:cd00551   110 GVDGFRLDAAKHVPKPEPVEFLREIRKDAKLAKPD---TLLLGEAWG-GPDELLAKAGFDDGLDSVFDFPLLEALRDALK 185

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093953596 285 NGEKMSYLKNWGEgWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLyKMAVGFMLAHP 347
Cdd:cd00551   186 GGEGALAILAALL-LLNPEGALLVNFLGNHDTFRLADLVSYKIVELRKARL-KLALALLLTLP 246
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 46-344 1.76e-13

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: 71.93  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  46 YLAPKGFGGVQVSPPNENV------AIHNPFRPWWER-YqpvsYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMc 118
Cdd:cd11320    55 YLKDLGVTAIWISPPVENInspiegGGNTGYHGYWARdF----KRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHS- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 119 gNAVSAGTSstcGSYFNPGS--RDFPAVPySGWdFNdgkcktGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAE 196
Cdd:cd11320   130 -SPADYAED---GALYDNGTlvGDYPNDD-NGW-FH------HNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 197 YMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSnwfpegskPFIYQEVIDLGGEPiKSSDY--FGNGR---VTEF 271
Cdd:cd11320   198 AIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKP--------VFTFGEWFLGSPDP-GYEDYvkFANNSgmsLLDF 268

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093953596 272 KYGAKLGTVIRKwNGEKMSYLKNWGEGWG--FMPSDRALVFVDNHDNQRGHGAGGasiltfwDARLYKMAVGFML 344
Cdd:cd11320   269 PLNQAIRDVFAG-FTATMYDLDAMLQQTSsdYNYENDLVTFIDNHDMPRFLTLNN-------NDKRLHQALAFLL 335
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 3.65e-13

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: 70.46  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsSTCGSYFNPgSRDFPAVPYS-GWDFNDGKCKTGS 160
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQE-SRSSKDNPYRdYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 161 GDIENYNDATQVRDCRLSG----------LLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLH 230
Cdd:pfam00128 111 NNWRSYFGGSAWTYDEKGQeyylhlfvagQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 231 NLNS-----NWFPEGSKP-FIYQEVIDLGGEPIKSSDYFGNGRVTE----FKYGAKLGTVIrKWNGEK--MSYLKNWGEG 298
Cdd:pfam00128 191 FWHEftqamNETVFGYKDvMTVGEVFHGDGEWARVYTTEARMELEMgfnfPHNDVALKPFI-KWDLAPisARKLKEMITD 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1093953596 299 W-GFMP--SDRALVFVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 270 WlDALPdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 82-224 2.39e-12

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


Pssm-ID: 200458 [Multi-domain]  Cd Length: 375  Bit Score: 68.36  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnAVSAGTSSTCGSYFNPgsrdfpavpysgwdFNDGK-----C 156
Cdd:cd11319    88 YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM---ASAGPGSDVDYSSFVP--------------FNDSSyyhpyC 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093953596 157 ktgsgDIENYNDATQVRDCRL----SGLLDLALGKDYVRSKIAEYMNHLI-DIGVAGFRIDASKHM----WPGDIKA 224
Cdd:cd11319   151 -----WITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLRIDTAKHVrkdfWPGFVEA 222
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 7.85e-12

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 67.20  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsstcgSYFNP---GSRDFPAVPYSGW----DFNDGKCKTGSG 161
Cdd:COG0366    76 GTLADFDELVAEAHARGIKVILDLVLNHT--------------SDEHPwfqEARAGPDSPYRDWyvwrDGKPDLPPNNWF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 162 DIENYNDATQVRDCR-------LSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMW-----PGDIKAILDKL 229
Cdd:COG0366   142 SIFGGSAWTWDPEDGqyylhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 230 HNLNSNWFPEGSKPFIYQEVIdlGGEPIKSSDYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEGwgfMPSD 305
Cdd:COG0366   222 RELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEG 296

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1093953596 306 RALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366   297 GWWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
PLN02784 PLN02784
alpha-amylase
 15-227 3.53e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 56.17  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  15 AQYSSNTQQGRTSIVHLFEW------RWVDIALECERYLAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTR 87
Cdd:PLN02784  492 IKICSGTGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVS------P--EGYMPKDlYNLNSR 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  88 SGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSA-GTSSTCGSYFNPGSRdfpAVPYSGWDFNdGKCKTGSGDieNY 166
Cdd:PLN02784  564 YGTIDELKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQnGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGD--NF 637

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093953596 167 NDATQVRDcrlsglldlalGKDYVRSKIAEYMNHLID-IGVAGFRIDASKHMWPGDIKAILD 227
Cdd:PLN02784  638 HAAPNIDH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYME 688
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 89-348 2.56e-07

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: 52.97  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHmcgnavsagTSS------TCGSYFNPGSRD---FPAVPYSGWDFNDGKCKTG 159
Cdd:cd11316    67 GTMEDFERLIAEAHKRGIKVIIDLVINH---------TSSehpwfqEAASSPDSPYRDyyiWADDDPGGWSSWGGNVWHK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 160 SGDIENYNDATQvrdcrlSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDiKAILDKLHNLNS-NWFP 238
Cdd:cd11316   138 AGDGGYYYGAFW------SGMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYENG-EGQADQEENIEFwKEFR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 239 ---EGSKP--FIYQEVIDLGGEPiksSDYFGNG--RVTEFKYGAKLGTVIRKWNG--EKMSYLKNW-GEGWGFMPSDRAL 308
Cdd:cd11316   211 dyvKSVKPdaYLVGEVWDDPSTI---APYYASGldSAFNFDLAEAIIDSVKNGGSgaGLAKALLRVyELYAKYNPDYIDA 287

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1093953596 309 VFVDNHDNQRGHGAGGAsiltfwDARLYKMAVGFML---AHPY 348
Cdd:cd11316   288 PFLSNHDQDRVASQLGG------DEAKAKLAAALLLtlpGNPF 324
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 47-227 1.22e-05

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: 47.22  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  47 LAPKGFGGVQVSPPNENVAIHNpfrpwwERYQPVS-YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGnavsag 125
Cdd:cd11314    27 LAAAGFTAIWLPPPSKSVSGSS------MGYDPGDlYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSG------ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 126 tsstcgsyfnpgsrdfpavpysgwdfndgkCKTGsgdiENYNDATqvrdcrlsgllDLALGKDYVRSKIAEYMNHLI-DI 204
Cdd:cd11314    95 ------------------------------PDTG----EDFGGAP-----------DLDHTNPEVQNDLKAWLNWLKnDI 129

                         170       180
                  ....*....|....*....|...
gi 1093953596 205 GVAGFRIDASKHMWPGDIKAILD 227
Cdd:cd11314   130 GFDGWRFDFVKGYAPSYVKEYNE 152
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 82-213 6.48e-05

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: 45.01  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN--AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDfndgkcktG 159
Cdd:cd11354    67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRShpAVAQALEDGPGSEEDRWHGHAGGGTPAVFE--------G 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1093953596 160 SGDienyndatqvrdcrlsgLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDA 213
Cdd:cd11354   139 HED-----------------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDA 175
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 190-351 5.51e-04

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: 42.24  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 190 VRSKIAEYMNHLIDIGVAGFRIDASKHM----WPGDIKAILDKLHnlnsnwfpegsKP--FIYQEVIDlgGEPIKSSDYF 263
Cdd:cd11339   134 VVDYLIDAYKWWIDTGVDGFRIDTVKHVprefWQEFAPAIRQAAG-----------KPdfFMFGEVYD--GDPSYIAPYT 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093953596 264 ---GNGRVTEFKYGAKLGTVIRkwNGEKMSYLKNW-GEGWGFMPSDRALVFVDNHDNQRghgaggasILTFWDARLYKMA 339
Cdd:cd11339   201 ttaGGDSVLDFPLYGAIRDAFA--GGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGR--------FLSSLKDGSADGT 270

                         170
                  ....*....|..
gi 1093953596 340 VGFMLAHPYGFT 351
Cdd:cd11339   271 ARLALALALLFT 282
 
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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