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Conserved domains on  [gi|236468117|ref|NP_001153622|]
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amylase 2a4 precursor [Mus musculus]

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, ...
 25-413 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: 583.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  25 RTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVhnPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 105 GVRIYVDAVINHMCGagnpagtsstcgsylnpnnrefpavpysawdfndnkcngeidnynDAYQVRNCRLTGLLDLALEK 184
Cdd:cd11317   79 GVRVYVDAVINHMAG---------------------------------------------DANEVRNCELVGLADLNTES 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 185 DYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFsqGSRPFIFQEVIDLGGEAIKGSEYFGNGR 264
Cdd:cd11317  114 DYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGGPL--GSRPYIYQEVIDGGGEAIQPSEYTGNGD 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 265 VTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGsSILTFWDARMYKMAVGFMLAHP 344
Cdd:cd11317  192 VTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWP 268

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 345 YGFTRVMSSYRWNrnfqngkdqNDWIGPPNN-NGVTKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVV 413
Cdd:cd11317  269 YGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
420-507 1.57e-30

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 1.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117   420 NWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISgdkvdGNCTGLRVNVGSDGKAHFSISNSAEdpf 499
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 236468117   500 IAIHADSK 507
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, ...
 25-413 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: 583.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  25 RTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVhnPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 105 GVRIYVDAVINHMCGagnpagtsstcgsylnpnnrefpavpysawdfndnkcngeidnynDAYQVRNCRLTGLLDLALEK 184
Cdd:cd11317   79 GVRVYVDAVINHMAG---------------------------------------------DANEVRNCELVGLADLNTES 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 185 DYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFsqGSRPFIFQEVIDLGGEAIKGSEYFGNGR 264
Cdd:cd11317  114 DYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGGPL--GSRPYIYQEVIDGGGEAIQPSEYTGNGD 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 265 VTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGsSILTFWDARMYKMAVGFMLAHP 344
Cdd:cd11317  192 VTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWP 268

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 345 YGFTRVMSSYRWNrnfqngkdqNDWIGPPNN-NGVTKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVV 413
Cdd:cd11317  269 YGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
420-507 1.57e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 1.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117   420 NWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISgdkvdGNCTGLRVNVGSDGKAHFSISNSAEdpf 499
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 236468117   500 IAIHADSK 507
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-121 5.45e-28

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 109.34  E-value: 5.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117    28 IVHLFEWR-------WVDIAKECErYLAPKGFGGVQVSPPNENVVVhnpsRPWWERYQPISYK-ICTRSGNEDEFRDMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKqIDPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 236468117   100 RCNNVGVRIYVDAVINHMCGAG 121
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDGG 99
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
82-344 3.69e-17

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 83.37  E-value: 3.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHmCGAGNP------AGTSSTCGSYLNPNNREFPAVPySAWDFNDNK 155
Cdd:COG0366   69 RDVDPRFGTLADFDELVAEAHARGIKVILDLVLNH-TSDEHPwfqearAGPDSPYRDWYVWRDGKPDLPP-NNWFSIFGG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 156 CNGEIDNYNDAYQVRNcRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMW-----PGDIKAVLDKLHNLN 230
Cdd:COG0366  147 SAWTWDPEDGQYYLHL-FFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLRELR 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 231 TKWFSQGSRPFIFQEVIDLGGEAIkgSEYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEgwgLVPSDRALV 306
Cdd:COG0366  226 AAVDEYYPDFFLVGEAWVDPPEDV--ARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPA---LYPEGGWWA 300

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 236468117 307 -FVDNHDNQRghgaggssILTFW----DARMYKMAVGFMLAHP 344
Cdd:COG0366  301 nFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 418-505 3.79e-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: 76.61  E-value: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  418 FSNWWDNNSNQVAFSRGN---RGFIVFNNDDWALSATLQTGLP-AGTYCDVISGDKV--DGNCTGLRVNVGSDGKAHFSI 491
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 236468117  492 SNSAEDPFIAIHAD 505
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-341 3.24e-12

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: 67.77  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117   82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMcgagnpagtsSTCGSYLNPNNREFPAvPYSAWDFNDNKCNGEID 161
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQESRSSKDN-PYRDYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  162 N----YNDAYQVRNCRLTG----------LLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDK-- 225
Cdd:pfam00128 111 NnwrsYFGGSAWTYDEKGQeyylhlfvagQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgp 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  226 -----LHNLNTKWFSQGSRpFIFQEV-IDLGGEAIKGSE--YFGNGRVTEFK-YGAKLGTVIrKWNGEK--MSYLKNWGE 294
Cdd:pfam00128 191 fwhefTQAMNETVFGYKDV-MTVGEVfHGDGEWARVYTTeaRMELEMGFNFPhNDVALKPFI-KWDLAPisARKLKEMIT 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 236468117  295 GWGLVPSD---RALVFVDNHDNQRghgaggssILTFW--DARMYKMAVGFML 341
Cdd:pfam00128 269 DWLDALPDtngWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
PLN02784 PLN02784
alpha-amylase
 21-224 5.24e-10

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 61.95  E-value: 5.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  21 TSDGRTAIVHLFEW------RWVDIAKECERYLAPKGFGGVQVSPPNENVvvhNPsrpwwERYQPIS-YKICTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  94 FRDMVTRCNNVGVRIYVDAVINHMCGA-GNPAGTSSTCGSYLNPNNRefpAVPYSAWDFN--DNKCNGeiDNYNDAYQVR 170
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHfQNQNGVWNIFGGRLNWDDR---AVVADDPHFQgrGNKSSG--DNFHAAPNID 644

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 236468117 171 NcrltglldlalEKDYVRTKVADYMNHLID-IGVAGFRLDAAKHMWPGDIKAVLD 224
Cdd:PLN02784 645 H-----------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, ...
 25-413 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: 583.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  25 RTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVhnPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 105 GVRIYVDAVINHMCGagnpagtsstcgsylnpnnrefpavpysawdfndnkcngeidnynDAYQVRNCRLTGLLDLALEK 184
Cdd:cd11317   79 GVRVYVDAVINHMAG---------------------------------------------DANEVRNCELVGLADLNTES 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 185 DYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFsqGSRPFIFQEVIDLGGEAIKGSEYFGNGR 264
Cdd:cd11317  114 DYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGGPL--GSRPYIYQEVIDGGGEAIQPSEYTGNGD 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 265 VTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGsSILTFWDARMYKMAVGFMLAHP 344
Cdd:cd11317  192 VTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWP 268

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 345 YGFTRVMSSYRWNrnfqngkdqNDWIGPPNN-NGVTKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVV 413
Cdd:cd11317  269 YGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 27-417 1.18e-58

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: 197.89  E-value: 1.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  27 AIVHLFEWRWVDIAKECERyLAPKGFGGVQVSPPNENVVVHNPSRPWWERYQPISYKICTRS-GNEDEFRDMVTRCNNVG 105
Cdd:cd11315    3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 106 VRIYVDAVINHMCGAGNpagtsstcgsylNPNNREFPAVPYSAWDFNDNKCNGEIDNYNDAYQVRNCRLTGLLDLALEKD 185
Cdd:cd11315   82 IKIIVDVVFNHMANEGS------------AIEDLWYPSADIELFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 186 YVRTKVADYMNHLIDIGVAGFRLDAAKHM-------WPGD-IKAVLDKLHNLNtkwfsqgsrPFIFQEVIDLGGEAIKG- 256
Cdd:cd11315  150 AVQQQQKAYLKALVALGVDGFRFDAAKHIelpdepsKASDfWTNILNNLDKDG---------LFIYGEVLQDGGSRDSDy 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 257 SEYFGNGRVTEFKYGAKL-GTVIRKWNGEKMSYLKNWGEGwglVPSDRALVFVDNHDNQrghgAGGSSILTFWDARMYKM 335
Cdd:cd11315  221 ASYLSLGGVTASAYGFPLrGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY----NNDGFESTGLDDEDERL 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 336 AVGFMLAHPYGFTRVmssyrWNRNfQNGKDQNDWIGPpnnngvtkevtinadttCGNDWVCEHrwrQIRNMVAFRNVVNG 415
Cdd:cd11315  294 AWAYLAARDGGTPLF-----FSRP-NGSGGTNPQIGD-----------------RGDDAWKSP---DVVAVNKFHNAMHG 347


                 ..
gi 236468117 416 QP 417
Cdd:cd11315  348 QP 349
Aamy_C smart00632
Aamy_C domain;
420-507 1.57e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 1.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117   420 NWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISgdkvdGNCTGLRVNVGSDGKAHFSISNSAEdpf 499
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 236468117   500 IAIHADSK 507
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-121 5.45e-28

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 109.34  E-value: 5.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117    28 IVHLFEWR-------WVDIAKECErYLAPKGFGGVQVSPPNENVVVhnpsRPWWERYQPISYK-ICTRSGNEDEFRDMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKqIDPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 236468117   100 RCNNVGVRIYVDAVINHMCGAG 121
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDGG 99
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 45-344 3.05e-18

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: 84.53  E-value: 3.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  45 RYLAPKGFGGVQVSPPNENVVVHNPSRPWWERYqpiSYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHmcgagnpa 124
Cdd:cd00551   32 DYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLD---YYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 125 gtsstcgsylnpnnrefpavpysawdfndnkcngeidnyndayqvrncrltglldlalekdyvrtkvaDYMNHLIDIGVA 204
Cdd:cd00551  101 --------------------------------------------------------------------DILRFWLDEGVD 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 205 GFRLDAAKHMWPGDIKAVLDKLHNLNTKWfsqGSRPFIFQEVIDlGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGE 284
Cdd:cd00551  113 GFRLDAAKHVPKPEPVEFLREIRKDAKLA---KPDTLLLGEAWG-GPDELLAKAGFDDGLDSVFDFPLLEALRDALKGGE 188

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 285 KMSYLKNWGEGWGLVPSdRALVFVDNHDNQRGHGAGGSSILTFWDARMyKMAVGFMLAHP 344
Cdd:cd00551  189 GALAILAALLLLNPEGA-LLVNFLGNHDTFRLADLVSYKIVELRKARL-KLALALLLTLP 246
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
82-344 3.69e-17

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 83.37  E-value: 3.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHmCGAGNP------AGTSSTCGSYLNPNNREFPAVPySAWDFNDNK 155
Cdd:COG0366   69 RDVDPRFGTLADFDELVAEAHARGIKVILDLVLNH-TSDEHPwfqearAGPDSPYRDWYVWRDGKPDLPP-NNWFSIFGG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 156 CNGEIDNYNDAYQVRNcRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMW-----PGDIKAVLDKLHNLN 230
Cdd:COG0366  147 SAWTWDPEDGQYYLHL-FFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLRELR 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 231 TKWFSQGSRPFIFQEVIDLGGEAIkgSEYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEgwgLVPSDRALV 306
Cdd:COG0366  226 AAVDEYYPDFFLVGEAWVDPPEDV--ARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPA---LYPEGGWWA 300

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 236468117 307 -FVDNHDNQRghgaggssILTFW----DARMYKMAVGFMLAHP 344
Cdd:COG0366  301 nFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 418-505 3.79e-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: 76.61  E-value: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  418 FSNWWDNNSNQVAFSRGN---RGFIVFNNDDWALSATLQTGLP-AGTYCDVISGDKV--DGNCTGLRVNVGSDGKAHFSI 491
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 236468117  492 SNSAEDPFIAIHAD 505
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 46-341 3.13e-14

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: 74.25  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  46 YLAPKGFGGVQVSPPNENVVVHNPSRPW------WER-YqpisYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMc 118
Cdd:cd11320   55 YLKDLGVTAIWISPPVENINSPIEGGGNtgyhgyWARdF----KRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHS- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 119 GAGNPAGTSSTC--GSYLnpnnrefpavpySAWDFNDNKC---NGEIDNYNDAYQVRNCRLTGLLDLALEKDYVRTKVAD 193
Cdd:cd11320  130 SPADYAEDGALYdnGTLV------------GDYPNDDNGWfhhNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 194 YMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNlntkwfsqgSRP-FIFQEVIDlGGEAIKGSEY--FGNGR---VTE 267
Cdd:cd11320  198 AIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS---------KKPvFTFGEWFL-GSPDPGYEDYvkFANNSgmsLLD 267

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 236468117 268 FKYGAKLGTVIRKwNGEKMSYLKNWGEGWG--LVPSDRALVFVDNHDNQRGHGAGGSsiltfwDARmYKMAVGFML 341
Cdd:cd11320  268 FPLNQAIRDVFAG-FTATMYDLDAMLQQTSsdYNYENDLVTFIDNHDMPRFLTLNNN------DKR-LHQALAFLL 335
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 82-221 3.48e-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: 71.06  E-value: 3.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAGNPAGTSStcgSYLNPnnrefpavpysawdFNDNK-----C 156
Cdd:cd11319   88 YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDY---SSFVP--------------FNDSSyyhpyC 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 236468117 157 ngEIDNYNDAYQVRNCRLT----GLLDLALEKDYVRTKVADYMNHLI-DIGVAGFRLDAAKHM----WPGDIKA 221
Cdd:cd11319  151 --WITDYNNQTSVEDCWLGddvvALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLRIDTAKHVrkdfWPGFVEA 222
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-341 3.24e-12

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: 67.77  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117   82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMcgagnpagtsSTCGSYLNPNNREFPAvPYSAWDFNDNKCNGEID 161
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQESRSSKDN-PYRDYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  162 N----YNDAYQVRNCRLTG----------LLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDK-- 225
Cdd:pfam00128 111 NnwrsYFGGSAWTYDEKGQeyylhlfvagQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgp 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  226 -----LHNLNTKWFSQGSRpFIFQEV-IDLGGEAIKGSE--YFGNGRVTEFK-YGAKLGTVIrKWNGEK--MSYLKNWGE 294
Cdd:pfam00128 191 fwhefTQAMNETVFGYKDV-MTVGEVfHGDGEWARVYTTeaRMELEMGFNFPhNDVALKPFI-KWDLAPisARKLKEMIT 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 236468117  295 GWGLVPSD---RALVFVDNHDNQRghgaggssILTFW--DARMYKMAVGFML 341
Cdd:pfam00128 269 DWLDALPDtngWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
PLN02784 PLN02784
alpha-amylase
 21-224 5.24e-10

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 61.95  E-value: 5.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  21 TSDGRTAIVHLFEW------RWVDIAKECERYLAPKGFGGVQVSPPNENVvvhNPsrpwwERYQPIS-YKICTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  94 FRDMVTRCNNVGVRIYVDAVINHMCGA-GNPAGTSSTCGSYLNPNNRefpAVPYSAWDFN--DNKCNGeiDNYNDAYQVR 170
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHfQNQNGVWNIFGGRLNWDDR---AVVADDPHFQgrGNKSSG--DNFHAAPNID 644

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 236468117 171 NcrltglldlalEKDYVRTKVADYMNHLID-IGVAGFRLDAAKHMWPGDIKAVLD 224
Cdd:PLN02784 645 H-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYME 688
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 89-345 4.49e-09

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: 58.36  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  89 GNEDEFRDMVTRCNNVGVRIYVDAVINHmcgagnpagTSS------TCGSYLNPNNREF----PAVPYSAWDFNDN--KC 156
Cdd:cd11316   67 GTMEDFERLIAEAHKRGIKVIIDLVINH---------TSSehpwfqEAASSPDSPYRDYyiwaDDDPGGWSSWGGNvwHK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 157 NGEIDNYNDAYQvrncrlTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWP-GDIKAVLDKLHNLnTKWFS 235
Cdd:cd11316  138 AGDGGYYYGAFW------SGMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYEnGEGQADQEENIEF-WKEFR 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 236 Q---GSRP--FIFQEVIDLGGEAikgSEYFGNG--RVTEFKYGAKLGTVIRKWNG--EKMSYLKNW-GEGWGLVPSDRAL 305
Cdd:cd11316  211 DyvkSVKPdaYLVGEVWDDPSTI---APYYASGldSAFNFDLAEAIIDSVKNGGSgaGLAKALLRVyELYAKYNPDYIDA 287

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 236468117 306 VFVDNHDNQRGHGAGGSsiltfwDARMYKMAVGFML---AHPY 345
Cdd:cd11316  288 PFLSNHDQDRVASQLGG------DEAKAKLAAALLLtlpGNPF 324
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 82-211 1.07e-07

Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 53.87  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMcGAGNPA---GTSSTCGSYLNPNNREFPAVPYSAWDFNDNkcng 158
Cdd:cd11354   67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV-GRSHPAvaqALEDGPGSEEDRWHGHAGGGTPAVFEGHED---- 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 236468117 159 eidnyndayqvrncrltgLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAA 211
Cdd:cd11354  142 ------------------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAA 176
PRK14705 PRK14705
glycogen branching enzyme; Provisional
 15-116 1.93e-06

glycogen branching enzyme; Provisional


Pssm-ID: 237794 [Multi-domain]  Cd Length: 1224  Bit Score: 50.77  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117   15 AQYDPHTSDGRTAIVHLFEWR----WVDIAKECERYLAPKGFGGVQVSPpnenvVVHNPSRPWWErYQPISYKICT-RSG 89
Cdd:PRK14705  739 AERDPHNSPMSVYEVHLGSWRlglgYRELAKELVDYVKWLGFTHVEFMP-----VAEHPFGGSWG-YQVTSYFAPTsRFG 812

                          90       100
                  ....*....|....*....|....*..
gi 236468117   90 NEDEFRDMVTRCNNVGVRIYVDAVINH 116
Cdd:PRK14705  813 HPDEFRFLVDSLHQAGIGVLLDWVPAH 839
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 82-220 1.73e-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: 46.83  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCgaGNPAGTSstcgsylnpnnreFPAVPysawdfndnkcngEID 161
Cdd:cd11314   57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRS--GPDTGED-------------FGGAP-------------DLD 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 162 NYNdayqvrncrltglldlalekDYVRTKVADYMNHLI-DIGVAGFRLDAAKHMWPGDIK 220
Cdd:cd11314  109 HTN--------------------PEVQNDLKAWLNWLKnDIGFDGWRFDFVKGYAPSYVK 148
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 86-316 4.24e-05

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 46.04  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117  86 TRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAG----NPAgtsstcgSYLNPNNRE----------------FPAVP 145
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGADeketFRV-------VEVDPDDRTqiisepyeiegwtrftFPGRG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 146 --YSA-----WDFN----DNKCNGE----IDNYNDAY--QV----RNCRLTGLLDLALEKDYVRTKVADYMNHLID-IGV 203
Cdd:PRK09441 148 gkYSDfkwhwYHFSgtdyDENPDESgifkIVGDGKGWddQVddenGNFDYLMGADIDFRHPEVREELKYWAKWYMEtTGF 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 204 AGFRLDAAKHMWPGDIKAVLDKLHNlntkwfSQGSRPFIFQEVIDLGGEAIKgsEYfgngrVTEFKYGAKLGTVIRKWNG 283
Cdd:PRK09441 228 DGFRLDAVKHIDAWFIKEWIEHVRE------VAGKDLFIVGEYWSHDVDKLQ--DY-----LEQVEGKTDLFDVPLHYNF 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 236468117 284 EKMSY------LKNWGEGwGLVPSD--RALVFVDNHDNQRG 316
Cdd:PRK09441 295 HEASKqgrdydMRNIFDG-TLVEADpfHAVTFVDNHDTQPG 334
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 179-348 3.08e-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: 43.01  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 179 DLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHM----WPGDIKAVLDKLHNLNTkwfsqgsrpFIFQEVIDLGGEAI 254
Cdd:cd11339  126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVprefWQEFAPAIRQAAGKPDF---------FMFGEVYDGDPSYI 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 236468117 255 kgSEYF---GNGRVTEFKYGAKLGTVIRkwNGEKMSYLKNW-GEGWGLVPSDRALVFVDNHDNQRghgaggssILTFWDA 330
Cdd:cd11339  197 --APYTttaGGDSVLDFPLYGAIRDAFA--GGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGR--------FLSSLKD 264

                        170
                 ....*....|....*...
gi 236468117 331 RMYKMAVGFMLAHPYGFT 348
Cdd:cd11339  265 GSADGTARLALALALLFT 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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