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Conserved domains on  [gi|157921591|gb|ABW02889|]
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pancreatic amylase B [Pan paniscus]

Protein Classification

alpha-amylase( domain architecture ID 10183021)

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

CATH:  3.20.20.80|2.60.40.1180
CAZY:  GH13
EC:  3.2.1.1
Gene Ontology:  GO:0004556|GO:0005975
PubMed:  21544166|17085431|11257505
SCOP:  4003138|4002636

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: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 105 GVRIYVDAVINHMCGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLVGLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 185 LEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNwfPAGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157921591 345 AHPYGFTRVMSSYRWPrqfqngndvNDWVGPPNN-NGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 2.06e-30

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.10  E-value: 2.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591   422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSVSNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 157921591   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: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 105 GVRIYVDAVINHMCGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLVGLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 185 LEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNwfPAGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157921591 345 AHPYGFTRVMSSYRWPrqfqngndvNDWVGPPNN-NGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 2.06e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.10  E-value: 2.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591   422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSVSNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 157921591   502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-120 1.08e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.87  E-value: 1.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591    28 IVHLFEWR-------WVDIALECErYLAPKGFGGVQVSPPNENVaihnPFRPWWERYQPVSYKLC-TRSGNEDEFRNMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
gi 157921591   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 1.37e-16

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: 75.07  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  421 FTNWYDNGSNQVAFGRGN---RGFIVFNNDDWTFSLTLQTGLP-AGTYCDVISGDKIN--GNCTGIKIYVSDDGKAHFSV 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 157921591  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 1.33e-14

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: 75.09  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591   82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsSTCGSYFNPgSRDFPAVPYS-GWDFNDGKCKTGS 160
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQE-SRSSKDNPYRdYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  161 GDIENYNDATQVRDCR----------LVGLLDLALEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLH 230
Cdd:pfam00128 111 NNWRSYFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  231 NLNSNWFPAGSKPFIYQEVIDLG------GEPIKSSDYFGNGRVTE----FKYGAKLGTVIrKWNGEK--MSYLKNWGEG 298
Cdd:pfam00128 191 FWHEFTQAMNETVFGYKDVMTVGevfhgdGEWARVYTTEARMELEMgfnfPHNDVALKPFI-KWDLAPisARKLKEMITD 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157921591  299 W-GFMP--SDRALVFVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 270 WlDALPdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 3.13e-12

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 68.35  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsstcgSYFNP---GSRDFPAVPYSGW----DFNDGKCKTGSG 161
Cdd:COG0366   76 GTLADFDELVAEAHARGIKVILDLVLNHT--------------SDEHPwfqEARAGPDSPYRDWyvwrDGKPDLPPNNWF 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 162 DIENYNDATQVRDCR-------LVGLLDLALEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMW-----PGDIKAILDKL 229
Cdd:COG0366  142 SIFGGSAWTWDPEDGqyylhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFL 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 230 HNLNSNWFPAGSKPFIYQEVIdlGGEPIKSSDYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEGwgfMPSD 305
Cdd:COG0366  222 RELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEG 296

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157921591 306 RALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366  297 GWWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
PLN02784 PLN02784
alpha-amylase
 21-332 1.02e-07

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 54.63  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  21 TQQGRTSIVHLFEW------RWVDIALECERYLAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVS------P--EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  94 FRNMVTRCNNVGVRIYVDAVINHMCGNAVSA-GTSSTCGSYFNPGSRdfpAVPYSGWDFNdGKCKTGSGDieNYNDATQV 172
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQnGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGD--NFHAAPNI 643

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 173 RDcrlvglldlalEKDYVRSKIAKYMNHLID-IGVAGFRLDASKHMWPGDIKAILDKlhnlNSNWFPAG----SKPFIY- 246
Cdd:PLN02784 644 DH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYMEA----SEPYFAVGeywdSLSYTYg 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 247 ----------QEVIDLggepIKSSdyfgNGRVTEFKYGAK--LGTVIRKWNGEKMSYLKNWGEG-WGFMPSdRALVFVDN 313
Cdd:PLN02784 709 emdynqdahrQRIVDW----INAT----NGTAGAFDVTTKgiLHSALERCEYWRLSDQKGKPPGvVGWWPS-RAVTFIEN 779

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157921591 314 HD--NQRGHG--------AGGASILT-------FWD 332
Cdd:PLN02784 780 HDtgSTQGHWrfpegkemQGYAYILThpgtpavFYD 815
 
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: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 105 GVRIYVDAVINHMCGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLVGLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 185 LEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNwfPAGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157921591 345 AHPYGFTRVMSSYRWPrqfqngndvNDWVGPPNN-NGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 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 6.06e-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: 174.77  E-value: 6.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  28 IVHLFEWRWVDIALECERyLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRS-GNEDEFRNMVTRCNNVGV 106
Cdd:cd11315    4 ILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 107 RIYVDAVINHMcgnavsagTSSTCGSYFNPGSRDFPAVPYSGWDFNDGkcktgsgDIENYNDATQVRDCRLVGLLDLALE 186
Cdd:cd11315   83 KIIVDVVFNHM--------ANEGSAIEDLWYPSADIELFSPEDFHGNG-------GISNWNDRWQVTQGRLGGLPDLNTE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 187 KDYVRSKIAKYMNHLIDIGVAGFRLDASKHM-------WPGD-IKAILDKLHNLNsnwfpagskPFIYQEVIDLGGEPIK 258
Cdd:cd11315  148 NPAVQQQQKAYLKALVALGVDGFRFDAAKHIelpdepsKASDfWTNILNNLDKDG---------LFIYGEVLQDGGSRDS 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 259 S-SDYFGNGRVTEFKYGAKL-GTVIRKWNGEKMSYLKNWGEGwgfMPSDRALVFVDNHDNQrGHGAGGASILTFWDARly 336
Cdd:cd11315  219 DyASYLSLGGVTASAYGFPLrGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY-NNDGFESTGLDDEDER-- 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 337 kMAVGFMLAHPYGFTRVMSsyrwpRQFQNGNDvNDWVGPpnnngvikevtinpdttCGNDWVCEHrwrQIRNMVNFRNVV 416
Cdd:cd11315  293 -LAWAYLAARDGGTPLFFS-----RPNGSGGT-NPQIGD-----------------RGDDAWKSP---DVVAVNKFHNAM 345


                 ....
gi 157921591 417 DGQP 420
Cdd:cd11315  346 HGQP 349
Aamy_C smart00632
Aamy_C domain;
422-510 2.06e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.10  E-value: 2.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591   422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSVSNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 157921591   502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-120 1.08e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.87  E-value: 1.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591    28 IVHLFEWR-------WVDIALECErYLAPKGFGGVQVSPPNENVaihnPFRPWWERYQPVSYKLC-TRSGNEDEFRNMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
gi 157921591   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 1.37e-16

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: 75.07  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  421 FTNWYDNGSNQVAFGRGN---RGFIVFNNDDWTFSLTLQTGLP-AGTYCDVISGDKIN--GNCTGIKIYVSDDGKAHFSV 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 157921591  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 1.89e-16

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: 79.14  E-value: 1.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  45 RYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYqpvSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHmcgnavsa 124
Cdd:cd00551   32 DYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLD---YYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 125 gtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrlvglldlalekdyvrskiaKYMNHLIDI 204
Cdd:cd00551  101 -----------------------------------------------------------------------DILRFWLDE 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 205 GVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPagsKPFIYQEVIDlGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKW 284
Cdd:cd00551  110 GVDGFRLDAAKHVPKPEPVEFLREIRKDAKLAKP---DTLLLGEAWG-GPDELLAKAGFDDGLDSVFDFPLLEALRDALK 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157921591 285 NGEKMSYLKNWGEgWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLyKMAVGFMLAHP 347
Cdd:cd00551  186 GGEGALAILAALL-LLNPEGALLVNFLGNHDTFRLADLVSYKIVELRKARL-KLALALLLTLP 246
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 1.33e-14

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: 75.09  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591   82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsSTCGSYFNPgSRDFPAVPYS-GWDFNDGKCKTGS 160
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQE-SRSSKDNPYRdYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  161 GDIENYNDATQVRDCR----------LVGLLDLALEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLH 230
Cdd:pfam00128 111 NNWRSYFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  231 NLNSNWFPAGSKPFIYQEVIDLG------GEPIKSSDYFGNGRVTE----FKYGAKLGTVIrKWNGEK--MSYLKNWGEG 298
Cdd:pfam00128 191 FWHEFTQAMNETVFGYKDVMTVGevfhgdGEWARVYTTEARMELEMgfnfPHNDVALKPFI-KWDLAPisARKLKEMITD 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157921591  299 W-GFMP--SDRALVFVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 270 WlDALPdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 46-344 1.15e-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: 72.70  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  46 YLAPKGFGGVQVSPPNENV------AIHNPFRPWWER--YQPVSYklctrSGNEDEFRNMVTRCNNVGVRIYVDAVINHM 117
Cdd:cd11320   55 YLKDLGVTAIWISPPVENInspiegGGNTGYHGYWARdfKRTNEH-----FGTWEDFDELVDAAHANGIKVIIDFVPNHS 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 118 cgNAVSAGTSstcGSYFNPGS--RDFPAVPySGWdFNdgkcktGSGDIENYNDATQVRDCRLVGLLDLALE----KDYVR 191
Cdd:cd11320  130 --SPADYAED---GALYDNGTlvGDYPNDD-NGW-FH------HNGGIDDWSDREQVRYKNLFDLADLNQSnpwvDQYLK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 192 SKIAKYMNHlidiGVAGFRLDASKHMWPGDIKAILDKLHNLNSnwfpagskPFIYQEVIDLGGEPiKSSDY--FGNGR-- 267
Cdd:cd11320  197 DAIKFWLDH----GIDGIRVDAVKHMPPGWQKSFADAIYSKKP--------VFTFGEWFLGSPDP-GYEDYvkFANNSgm 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 268 -VTEFKYGAKLGTVIRKwNGEKMSYLKNWGEGWG--FMPSDRALVFVDNHDNQRGHGAGGasiltfwDARLYKMAVGFML 344
Cdd:cd11320  264 sLLDFPLNQAIRDVFAG-FTATMYDLDAMLQQTSsdYNYENDLVTFIDNHDMPRFLTLNN-------NDKRLHQALAFLL 335
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 82-224 1.22e-13

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: 72.21  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnAVSAGTSSTCGSYFNPgsrdfpavpysgwdFNDGK-----C 156
Cdd:cd11319   88 YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM---ASAGPGSDVDYSSFVP--------------FNDSSyyhpyC 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157921591 157 ktgsgDIENYNDATQVRDCRL----VGLLDLALEKDYVRSKIAKYMNHLI-DIGVAGFRLDASKHM----WPGDIKA 224
Cdd:cd11319  151 -----WITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLRIDTAKHVrkdfWPGFVEA 222
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 3.13e-12

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 68.35  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMcgnavsagtsstcgSYFNP---GSRDFPAVPYSGW----DFNDGKCKTGSG 161
Cdd:COG0366   76 GTLADFDELVAEAHARGIKVILDLVLNHT--------------SDEHPwfqEARAGPDSPYRDWyvwrDGKPDLPPNNWF 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 162 DIENYNDATQVRDCR-------LVGLLDLALEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHMW-----PGDIKAILDKL 229
Cdd:COG0366  142 SIFGGSAWTWDPEDGqyylhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFL 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 230 HNLNSNWFPAGSKPFIYQEVIdlGGEPIKSSDYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEGwgfMPSD 305
Cdd:COG0366  222 RELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEG 296

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157921591 306 RALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366  297 GWWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 89-348 8.58e-08

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: 54.51  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHmcgnavsagTSS------TCGSYFNPGSRD---FPAVPYSGWDFNDGKCKTG 159
Cdd:cd11316   67 GTMEDFERLIAEAHKRGIKVIIDLVINH---------TSSehpwfqEAASSPDSPYRDyyiWADDDPGGWSSWGGNVWHK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 160 SGDIENYNDA-TQvrdcrlvGLLDLALEKDYVRS---KIAKYMnhlIDIGVAGFRLDASKHMWPGDiKAILDKLHNLNS- 234
Cdd:cd11316  138 AGDGGYYYGAfWS-------GMPDLNLDNPAVREeikKIAKFW---LDKGVDGFRLDAAKHIYENG-EGQADQEENIEFw 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 235 NWFPA---GSKP--FIYQEVIDLGGEPiksSDYFGNG--RVTEFKYGAKLGTVIRKWNG--EKMSYLKNW-GEGWGFMPS 304
Cdd:cd11316  207 KEFRDyvkSVKPdaYLVGEVWDDPSTI---APYYASGldSAFNFDLAEAIIDSVKNGGSgaGLAKALLRVyELYAKYNPD 283

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157921591 305 DRALVFVDNHDNQRGHGAGGAsiltfwDARLYKMAVGFML---AHPY 348
Cdd:cd11316  284 YIDAPFLSNHDQDRVASQLGG------DEAKAKLAAALLLtlpGNPF 324
PLN02784 PLN02784
alpha-amylase
 21-332 1.02e-07

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 54.63  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  21 TQQGRTSIVHLFEW------RWVDIALECERYLAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVS------P--EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  94 FRNMVTRCNNVGVRIYVDAVINHMCGNAVSA-GTSSTCGSYFNPGSRdfpAVPYSGWDFNdGKCKTGSGDieNYNDATQV 172
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQnGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGD--NFHAAPNI 643

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 173 RDcrlvglldlalEKDYVRSKIAKYMNHLID-IGVAGFRLDASKHMWPGDIKAILDKlhnlNSNWFPAG----SKPFIY- 246
Cdd:PLN02784 644 DH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYMEA----SEPYFAVGeywdSLSYTYg 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 247 ----------QEVIDLggepIKSSdyfgNGRVTEFKYGAK--LGTVIRKWNGEKMSYLKNWGEG-WGFMPSdRALVFVDN 313
Cdd:PLN02784 709 emdynqdahrQRIVDW----INAT----NGTAGAFDVTTKgiLHSALERCEYWRLSDQKGKPPGvVGWWPS-RAVTFIEN 779

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157921591 314 HD--NQRGHG--------AGGASILT-------FWD 332
Cdd:PLN02784 780 HDtgSTQGHWrfpegkemQGYAYILThpgtpavFYD 815
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 47-227 6.25e-06

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


Pssm-ID: 200453 [Multi-domain]  Cd Length: 302  Bit Score: 47.99  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  47 LAPKGFGGVQVSPPNENVAIHNpfrpwwERYQPVS-YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNavSAG 125
Cdd:cd11314   27 LAAAGFTAIWLPPPSKSVSGSS------MGYDPGDlYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGP--DTG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 126 TsstcgsyfnpgsrDFPAVPysgwdfndgkcktgsgDIENYNdatqvrdcrlvglldlalekDYVRSKIAKYMNHLI-DI 204
Cdd:cd11314   99 E-------------DFGGAP----------------DLDHTN--------------------PEVQNDLKAWLNWLKnDI 129

                        170       180
                 ....*....|....*....|...
gi 157921591 205 GVAGFRLDASKHMWPGDIKAILD 227
Cdd:cd11314  130 GFDGWRFDFVKGYAPSYVKEYNE 152
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 82-213 2.15e-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: 46.55  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN--AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDfndgkcktG 159
Cdd:cd11354   67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRShpAVAQALEDGPGSEEDRWHGHAGGGTPAVFE--------G 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157921591 160 SGDienyndatqvrdcrlvgLLDLALEKDYVRSKIAKYMNHLIDIGVAGFRLDA 213
Cdd:cd11354  139 HED-----------------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDA 175
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 182-351 7.66e-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: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 44.94  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 182 DLALEKDYVRSKIAKYMNHLIDIGVAGFRLDASKHM----WPGDIKAILDKLHnlnsnwfpagsKP--FIYQEVIDlgGE 255
Cdd:cd11339  126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVprefWQEFAPAIRQAAG-----------KPdfFMFGEVYD--GD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 256 PIKSSDYF---GNGRVTEFKYGAKLGTVIRkwNGEKMSYLKNW-GEGWGFMPSDRALVFVDNHDNQRghgaggasILTFW 331
Cdd:cd11339  193 PSYIAPYTttaGGDSVLDFPLYGAIRDAFA--GGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGR--------FLSSL 262

                        170       180
                 ....*....|....*....|
gi 157921591 332 DARLYKMAVGFMLAHPYGFT 351
Cdd:cd11339  263 KDGSADGTARLALALALLFT 282
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 86-217 3.15e-03

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 39.87  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  86 TRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCG------------------NAVSAGTSSTCGSYFN-PG----SRDFP 142
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadeketfrvvevdpddrtQIISEPYEIEGWTRFTfPGrggkYSDFK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 143 AVPY--SGWDFNDGKCKTGSGDIENYND--ATQVRDCR-----LVGlLDLALEKDYVRSKIAKYMNHLID-IGVAGFRLD 212
Cdd:PRK09441 155 WHWYhfSGTDYDENPDESGIFKIVGDGKgwDDQVDDENgnfdyLMG-ADIDFRHPEVREELKYWAKWYMEtTGFDGFRLD 233


                 ....*
gi 157921591 213 ASKHM 217
Cdd:PRK09441 234 AVKHI 238
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 89-216 6.04e-03

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: 39.29  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAV----SAGTSSTCGSYF--NPGSRDFPAVPY------SGWDFNDGKC 156
Cdd:cd11329  112 GVESDLKELVKTAKQKDIKVILDLTPNHSSKQHPlfkdSVLKEPPYRSAFvwADGKGHTPPNNWlsvtggSAWKWVEDRQ 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157921591 157 KTGSgdienYNDATQVrdcrlvgllDLALEKDYVRSKIAKYMNHLIDIGVAGFRLDASKH 216
Cdd:cd11329  192 YYLH-----QFGPDQP---------DLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY 237
 
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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