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Conserved domains on  [gi|21954500|dbj|BAC06332|]
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alpha-amylase [Drosophila nagarholensis]

Protein Classification

alpha-amylase family protein( domain architecture ID 10183021)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 28-399 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: 573.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  28 RSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGV 107
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 108 RIYVDVIFNHMAADggtygtggstaspssksypgvpyssldfnptcainnyndANQVRNCELVGLRDLNQGNSYVQEKVA 187
Cdd:cd11317  81 RVYVDAVINHMAGD---------------------------------------ANEVRNCELVGLADLNTESDYVRDKIA 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 188 EFLNHLIDLGVAGFRVDAAKHMWPADLGNIYGRLKNLNTDhgfASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHS 267
Cdd:cd11317 122 DYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG---PLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYA 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 268 DSIGKAFRGKDQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGaDVLTYKVPKQYKMASAFMLAHPFGTPRVMSS 347
Cdd:cd11317 199 RGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWPYGTPRVMSS 277

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 21954500 348 FSFSNTDQGPPTTDGHNIASPVFNSDNSCSGGWVCEHRWRQIYSMVAFRNAV 399
Cdd:cd11317 278 YYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
405-493 3.39e-35

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 126.20  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500    405 QNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGtkngsSCTGKTVTVGSDGRASIYIGNsedDG 484
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPA---GG 72


                   ....*....
gi 21954500    485 VLAIHVNAK 493
Cdd:smart00632  73 AVAIHVDAK 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, ...
 28-399 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: 573.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  28 RSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGV 107
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 108 RIYVDVIFNHMAADggtygtggstaspssksypgvpyssldfnptcainnyndANQVRNCELVGLRDLNQGNSYVQEKVA 187
Cdd:cd11317  81 RVYVDAVINHMAGD---------------------------------------ANEVRNCELVGLADLNTESDYVRDKIA 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 188 EFLNHLIDLGVAGFRVDAAKHMWPADLGNIYGRLKNLNTDhgfASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHS 267
Cdd:cd11317 122 DYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG---PLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYA 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 268 DSIGKAFRGKDQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGaDVLTYKVPKQYKMASAFMLAHPFGTPRVMSS 347
Cdd:cd11317 199 RGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWPYGTPRVMSS 277

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 21954500 348 FSFSNTDQGPPTTDGHNIASPVFNSDNSCSGGWVCEHRWRQIYSMVAFRNAV 399
Cdd:cd11317 278 YYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
405-493 3.39e-35

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 126.20  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500    405 QNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGtkngsSCTGKTVTVGSDGRASIYIGNsedDG 484
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPA---GG 72


                   ....*....
gi 21954500    485 VLAIHVNAK 493
Cdd:smart00632  73 AVAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
31-121 2.14e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.10  E-value: 2.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500     31 MVHLFEWK-------WDDIAAECEnFLGPNGFAGVQVSPVNENAVkdSRPWWERYQPISYKLV-TRSGNEEQFASMTRRC 102
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKQIdPRFGTMEDFKELVDAA 79

                           90
                   ....*....|....*....
gi 21954500    103 NAVGVRIYVDVIFNHMAAD 121
Cdd:smart00642  80 HARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 406-491 1.13e-19

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: 83.54  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   406 NWWDNGSNQIAFSRGS---RGFVAFNNDNYDLNSSLQTGLP-AGTYCDVISG--TKNGSSCTGKTVTVGSDGRASIYIGN 479
Cdd:pfam02806   3 DGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTddEEYGGSNTGEVVTVDGPGHPNSLTLT 82

                          90
                  ....*....|..
gi 21954500   480 SEDDGVLAIHVN 491
Cdd:pfam02806  83 LPPLSALVLKVE 94
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
90-342 1.29e-16

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 81.83  E-value: 1.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  90 GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggstaSP---SSKSYPGVPYSS----LDFNPTCAINNYNDAN 162
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDE-----------HPwfqEARAGPDSPYRDwyvwRDGKPDLPPNNWFSIF 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 163 QVRNCELVGLR-------------DLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMW-----PADLGNIYGRLKNL 224
Cdd:COG0366 145 GGSAWTWDPEDgqyylhlffssqpDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLREL 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 225 NtDHGFASGSKAYIVQEVIDMGGEAISKseYTG---LGAITEFRHSDSIGKAFRGKDQLRY---LSNWGTAwgFAASDRS 298
Cdd:COG0366 225 R-AAVDEYYPDFFLVGEAWVDPPEDVAR--YFGgdeLDMAFNFPLMPALWDALAPEDAAELrdaLAQTPAL--YPEGGWW 299

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 21954500 299 LVFVDNHDNQR-GHGAGGADVLtykvpKQYKMASAFMLAHPfGTP 342
Cdd:COG0366 300 ANFLRNHDQPRlASRLGGDYDR-----RRAKLAAALLLTLP-GTP 338
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 54-342 1.73e-13

Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 71.62  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500    54 GFAGVQVSPVNENAVKDSRPWWERYqpisYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTAS 133
Cdd:pfam00128  17 GVTAIWLSPIFDSPQADHGYDIADY----YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSSKD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   134 PSSKSY----PGVPYSSldfnPTCAINnYNDANQVRNCE----------LVGLRDLNQGNSYVQEKVAEFLNHLIDLGVA 199
Cdd:pfam00128  93 NPYRDYyfwrPGGGPIP----PNNWRS-YFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGID 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   200 GFRVDAAKHM--WPADLGNIYG-RLKNLNTDHG--FASGSKAYIVQEV-IDMGGEAISKSE--YTGLGAITEFRHSDSIG 271
Cdd:pfam00128 168 GFRIDVVKHIskVPGLPFENNGpFWHEFTQAMNetVFGYKDVMTVGEVfHGDGEWARVYTTeaRMELEMGFNFPHNDVAL 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21954500   272 KAFR----GKDQLRYLSNWGTAWGFAASD---RSLVFVDNHDNQRGHGAGGADVltykvpKQYKMASAFMLAHPfGTP 342
Cdd:pfam00128 248 KPFIkwdlAPISARKLKEMITDWLDALPDtngWNFTFLGNHDQPRFLSRFGDDR------ASAKLLAVFLLTLR-GTP 318
PLN00196 PLN00196
alpha-amylase; Provisional
 87-218 3.43e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 39.90  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   87 TRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASpssksyPGVPYSSLDFNPTCAINN---YND--A 161
Cdd:PLN00196  86 SKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFE------GGTPDSRLDWGPHMICRDdtqYSDgtG 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21954500  162 NQVRNCELVGLRDLNQGNSYVQEKVAEFLNHL-IDLGVAGFRVDAAKHmWPADLGNIY 218
Cdd:PLN00196 160 NLDTGADFAAAPDIDHLNKRVQRELIGWLLWLkSDIGFDAWRLDFAKG-YSAEVAKVY 216
 
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, ...
 28-399 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: 573.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  28 RSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGV 107
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 108 RIYVDVIFNHMAADggtygtggstaspssksypgvpyssldfnptcainnyndANQVRNCELVGLRDLNQGNSYVQEKVA 187
Cdd:cd11317  81 RVYVDAVINHMAGD---------------------------------------ANEVRNCELVGLADLNTESDYVRDKIA 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 188 EFLNHLIDLGVAGFRVDAAKHMWPADLGNIYGRLKNLNTDhgfASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHS 267
Cdd:cd11317 122 DYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG---PLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYA 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 268 DSIGKAFRGKDQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGaDVLTYKVPKQYKMASAFMLAHPFGTPRVMSS 347
Cdd:cd11317 199 RGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWPYGTPRVMSS 277

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 21954500 348 FSFSNTDQGPPTTDGHNIASPVFNSDNSCSGGWVCEHRWRQIYSMVAFRNAV 399
Cdd:cd11317 278 YYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 31-346 9.47e-49

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: 171.31  E-value: 9.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  31 MVHLFEWKWDDIAAECENfLGPNGFAGVQVSPVNENA--VKDSRPWWERYQPISYKLVTRS-GNEEQFASMTRRCNAVGV 107
Cdd:cd11315   4 ILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKegGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYGI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 108 RIYVDVIFNHMAADGgtygtggstASPSSKSYPGV---PYSSLDFNPTCAINNYNDANQVRNCELVGLRDLNQGNSYVQE 184
Cdd:cd11315  83 KIIVDVVFNHMANEG---------SAIEDLWYPSAdieLFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 185 KVAEFLNHLIDLGVAGFRVDAAKHM-WPADLGNIYGRLKN-LNTDHGFASgskaYIVQEVIDMGGEAISK-SEYTGLGAI 261
Cdd:cd11315 154 QQKAYLKALVALGVDGFRFDAAKHIeLPDEPSKASDFWTNiLNNLDKDGL----FIYGEVLQDGGSRDSDyASYLSLGGV 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 262 TefrhSDSIGKAFRGKDQLRYL---SNWGTAWGFAASDRSLV-FVDNHDNQrghgAGGADVLTYKVPKQYKMASAFMLAH 337
Cdd:cd11315 230 T----ASAYGFPLRGALKNAFLfggSLDPASYGQALPSDRAVtWVESHDTY----NNDGFESTGLDDEDERLAWAYLAAR 301


                ....*....
gi 21954500 338 PFGTPRVMS 346
Cdd:cd11315 302 DGGTPLFFS 310
Aamy_C smart00632
Aamy_C domain;
405-493 3.39e-35

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 126.20  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500    405 QNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGtkngsSCTGKTVTVGSDGRASIYIGNsedDG 484
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPA---GG 72


                   ....*....
gi 21954500    485 VLAIHVNAK 493
Cdd:smart00632  73 AVAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
31-121 2.14e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.10  E-value: 2.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500     31 MVHLFEWK-------WDDIAAECEnFLGPNGFAGVQVSPVNENAVkdSRPWWERYQPISYKLV-TRSGNEEQFASMTRRC 102
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKQIdPRFGTMEDFKELVDAA 79

                           90
                   ....*....|....*....
gi 21954500    103 NAVGVRIYVDVIFNHMAAD 121
Cdd:smart00642  80 HARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 406-491 1.13e-19

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: 83.54  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   406 NWWDNGSNQIAFSRGS---RGFVAFNNDNYDLNSSLQTGLP-AGTYCDVISG--TKNGSSCTGKTVTVGSDGRASIYIGN 479
Cdd:pfam02806   3 DGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTddEEYGGSNTGEVVTVDGPGHPNSLTLT 82

                          90
                  ....*....|..
gi 21954500   480 SEDDGVLAIHVN 491
Cdd:pfam02806  83 LPPLSALVLKVE 94
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 54-309 8.58e-19

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: 88.01  E-value: 8.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  54 GFAGVQVSPVNENaVKDSRPWWERY-----QPIsYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTG 128
Cdd:cd11319  56 GFDAIWISPIVKN-IEGNTAYGEAYhgywaQDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVD 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 129 GSTASP-SSKSYpgvpyssldFNPTCAINNYNDANQVRNCEL----VGLRDLNQGNSYVQEKVAEFLNHLI-DLGVAGFR 202
Cdd:cd11319 134 YSSFVPfNDSSY---------YHPYCWITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLR 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 203 VDAAKHM----WPadlgniygrlknlntdhGFASGSKAYIVQEVIDmgGEAISKSEYTG-LGAITEFRHSDSIGKAF-RG 276
Cdd:cd11319 205 IDTAKHVrkdfWP-----------------GFVEAAGVFAIGEVFD--GDPNYVCPYQNyLDGVLNYPLYYPLVDAFqST 265

                       250       260       270
                ....*....|....*....|....*....|....*
gi 21954500 277 KDQLRYLSNWGTAWGFAASDRSLV--FVDNHDNQR 309
Cdd:cd11319 266 KGSMSALVDTINSVQSSCKDPTLLgtFLENHDNPR 300
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
90-342 1.29e-16

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 81.83  E-value: 1.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  90 GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggstaSP---SSKSYPGVPYSS----LDFNPTCAINNYNDAN 162
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDE-----------HPwfqEARAGPDSPYRDwyvwRDGKPDLPPNNWFSIF 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 163 QVRNCELVGLR-------------DLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMW-----PADLGNIYGRLKNL 224
Cdd:COG0366 145 GGSAWTWDPEDgqyylhlffssqpDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLREL 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 225 NtDHGFASGSKAYIVQEVIDMGGEAISKseYTG---LGAITEFRHSDSIGKAFRGKDQLRY---LSNWGTAwgFAASDRS 298
Cdd:COG0366 225 R-AAVDEYYPDFFLVGEAWVDPPEDVAR--YFGgdeLDMAFNFPLMPALWDALAPEDAAELrdaLAQTPAL--YPEGGWW 299

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 21954500 299 LVFVDNHDNQR-GHGAGGADVLtykvpKQYKMASAFMLAHPfGTP 342
Cdd:COG0366 300 ANFLRNHDQPRlASRLGGDYDR-----RRAKLAAALLLTLP-GTP 338
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 54-342 2.19e-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: 2.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  54 GFAGVQVSPVNENaVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHmaadggtygtggstas 133
Cdd:cd00551  38 GVTAIWLTPIFES-PEYDGYDKDDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH---------------- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 134 pssksypgvpyssldfnptcainnyndanqvrncelvglrdlnqgnsyvqekvaEFLNHLIDLGVAGFRVDAAKHMWPAD 213
Cdd:cd00551 101 ------------------------------------------------------DILRFWLDEGVDGFRLDAAKHVPKPE 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 214 LGNIYGRLKNLNTDHgfasGSKAYIVQEVIDMGGEAISKSEYT-GLGAITEFRHSDSIGKAFRGKDQLRYLSNWGTaWGF 292
Cdd:cd00551 127 PVEFLREIRKDAKLA----KPDTLLLGEAWGGPDELLAKAGFDdGLDSVFDFPLLEALRDALKGGEGALAILAALL-LLN 201

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 21954500 293 AASDRSLVFVDNHDNQRghgagGADVLTYKVP----KQYKMASAFMLAHPfGTP 342
Cdd:cd00551 202 PEGALLVNFLGNHDTFR-----LADLVSYKIVelrkARLKLALALLLTLP-GTP 249
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 154-342 6.04e-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: 73.47  E-value: 6.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 154 AINNYNDANQVRNCELVGLRDLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMWPADLGNIYGRL---KNLNTDHGF 230
Cdd:cd11320 163 GIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIyskKPVFTFGEW 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 231 ASGSKAyivqeviDMGGEAISKSEYTGLGAItEFRHSDSIGKAFRGkdqlrylsNWGTAWGFAA-----------SDRSL 299
Cdd:cd11320 243 FLGSPD-------PGYEDYVKFANNSGMSLL-DFPLNQAIRDVFAG--------FTATMYDLDAmlqqtssdynyENDLV 306

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21954500 300 VFVDNHDNQRGHGAGGADvltykvpKQYKMASAFMLAHPfGTP 342
Cdd:cd11320 307 TFIDNHDMPRFLTLNNND-------KRLHQALAFLLTSR-GIP 341
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 54-342 1.73e-13

Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 71.62  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500    54 GFAGVQVSPVNENAVKDSRPWWERYqpisYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTAS 133
Cdd:pfam00128  17 GVTAIWLSPIFDSPQADHGYDIADY----YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSSKD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   134 PSSKSY----PGVPYSSldfnPTCAINnYNDANQVRNCE----------LVGLRDLNQGNSYVQEKVAEFLNHLIDLGVA 199
Cdd:pfam00128  93 NPYRDYyfwrPGGGPIP----PNNWRS-YFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGID 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   200 GFRVDAAKHM--WPADLGNIYG-RLKNLNTDHG--FASGSKAYIVQEV-IDMGGEAISKSE--YTGLGAITEFRHSDSIG 271
Cdd:pfam00128 168 GFRIDVVKHIskVPGLPFENNGpFWHEFTQAMNetVFGYKDVMTVGEVfHGDGEWARVYTTeaRMELEMGFNFPHNDVAL 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21954500   272 KAFR----GKDQLRYLSNWGTAWGFAASD---RSLVFVDNHDNQRGHGAGGADVltykvpKQYKMASAFMLAHPfGTP 342
Cdd:pfam00128 248 KPFIkwdlAPISARKLKEMITDWLDALPDtngWNFTFLGNHDQPRFLSRFGDDR------ASAKLLAVFLLTLR-GTP 318
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 174-309 2.67e-10

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: 61.89  E-value: 2.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 174 DLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMWPADLGNIYGRLKNLNTDHGFasgskaYIVQEVIDMGGEAISK- 252
Cdd:cd11339 126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPDF------FMFGEVYDGDPSYIAPy 199

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21954500 253 SEYTGLGAITEFRHSDSIGKAFRGKDQLRYLSNW-GTAWGFAASDRSLVFVDNHDNQR 309
Cdd:cd11339 200 TTTAGGDSVLDFPLYGAIRDAFAGGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGR 257
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 90-342 1.90e-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: 59.52  E-value: 1.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  90 GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGgtygtggstasP---SSKSYPGVPYSSL----DFNPTCA----INNY 158
Cdd:cd11316  67 GTMEDFERLIAEAHKRGIKVIIDLVINHTSSEH-----------PwfqEAASSPDSPYRDYyiwaDDDPGGWsswgGNVW 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 159 NDANQVRNCELV---GLRDLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMWPaDLGNIYGRLKNLN-----TDHGF 230
Cdd:cd11316 136 HKAGDGGYYYGAfwsGMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYE-NGEGQADQEENIEfwkefRDYVK 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 231 ASGSKAYIVQEVIDmGGEAISKSEYTGLGAITEFRHSDSIG----KAFRGKDQLRYLSNW-GTAWGFAASDRSLVFVDNH 305
Cdd:cd11316 215 SVKPDAYLVGEVWD-DPSTIAPYYASGLDSAFNFDLAEAIIdsvkNGGSGAGLAKALLRVyELYAKYNPDYIDAPFLSNH 293

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21954500 306 DNQRGHGAGGADvltykvPKQYKMASAFMLAHPfGTP 342
Cdd:cd11316 294 DQDRVASQLGGD------EAKAKLAAALLLTLP-GNP 323
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 83-342 2.19e-07

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: 52.61  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  83 YKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAAdggtygtggstaspssksypgvPYSSLDFNptcainnyndan 162
Cdd:cd11314  57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSG----------------------PDTGEDFG------------ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 163 qvrncelvGLRDLNQGNSYVQEKVAEFLNHLI-DLGVAGFRVDAAKHMWPAdlgniYGRLKNLNTDHGFASG----SKAY 237
Cdd:cd11314 103 --------GAPDLDHTNPEVQNDLKAWLNWLKnDIGFDGWRFDFVKGYAPS-----YVKEYNEATSPSFSVGeywdGLSY 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 238 IVQE--------VIDMGGEAISKSEYTGLGAITEfrhsdsigkAFRGKDQLRYLSNWGTAWGFAA--SDRSLVFVDNHDN 307
Cdd:cd11314 170 ENQDahrqrlvdWIDATGGGSAAFDFTTKYILQE---------AVNNNEYWRLRDGQGKPPGLIGwwPQKAVTFVDNHDT 240

                       250       260       270
                ....*....|....*....|....*....|....*
gi 21954500 308 qrGHGAGGADVLTYKVPkqykMASAFMLAHPfGTP 342
Cdd:cd11314 241 --GSTQGHWPFPTDNVL----QGYAYILTHP-GTP 268
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 83-309 3.97e-06

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: 48.86  E-value: 3.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  83 YKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMaadggtygtggstaspsSKSYPGVPYSSLDFNPTCAINNYNDAN 162
Cdd:cd11354  67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV-----------------GRSHPAVAQALEDGPGSEEDRWHGHAG 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 163 QVRNCELVG---LRDLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMWPADLGNIYGRLKNLNTDhgfasgskAYIV 239
Cdd:cd11354 130 GGTPAVFEGhedLVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPPEFWARVLPRVRERHPD--------AWIL 201

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21954500 240 QEVIDmgGEAISKSEYTGLGAITEFRHSDSIGKAFrgKDQlrylsN-WGTAW------GFAASDRSLVFVDNHDNQR 309
Cdd:cd11354 202 GEVIH--GDYAGIVAASGMDSVTQYELWKAIWSSI--KDR-----NfFELDWalgrhnEFLDSFVPQTFVGNHDVTR 269
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 82-235 5.52e-05

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: 45.45  E-value: 5.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  82 SYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASPSSKSY----PGVPYssldfnptcAINN 157
Cdd:cd11329 104 ETYLNNSYGVESDLKELVKTAKQKDIKVILDLTPNHSSKQHPLFKDSVLKEPPYRSAFvwadGKGHT---------PPNN 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 158 YNDANQVRNCELVGLR------------DLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMW-PADLGN--IYGRLK 222
Cdd:cd11329 175 WLSVTGGSAWKWVEDRqyylhqfgpdqpDLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKYLLeDPNLKDeeISSNTK 254

                       170
                ....*....|....
gi 21954500 223 NLN-TDHGFASGSK 235
Cdd:cd11329 255 GVTpNDYGFYTHIK 268
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 174-209 1.24e-04

Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200473 [Multi-domain]  Cd Length: 447  Bit Score: 44.48  E-value: 1.24e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21954500 174 DLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHM 209
Cdd:cd11334 166 DLNFDNPAVREEILRIMDFWLDLGVDGFRLDAVPYL 201
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
 174-213 1.25e-03

Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200494 [Multi-domain]  Cd Length: 456  Bit Score: 41.19  E-value: 1.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21954500 174 DLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHMWPAD 213
Cdd:cd11359 168 DLNFRNPDVQQEMDDVLRFWLDKGVDGFRVDAVKHLLEAT 207
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 54-248 1.51e-03

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


Pssm-ID: 200488 [Multi-domain]  Cd Length: 390  Bit Score: 40.72  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500  54 GFAGVQVSPVNENAVKDSrpwWErYQPISYKLVTRS-GNEEQFASMTRRCNAVGVRIYVDVIFNHmaadggtygtggstA 132
Cdd:cd11350  46 GVNAIELMPVQEFPGNDS---WG-YNPRHYFALDKAyGTPEDLKRLVDECHQRGIAVILDVVYNH--------------A 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 133 SPSSksypgvPYSSLDFNPTC--AINNYNDANQVRNCELVGLRDLNQGNSYVQEKVAEFLNHLID-LGVAGFRVDAAKHM 209
Cdd:cd11350 108 EGQS------PLARLYWDYWYnpPPADPPWFNVWGPHFYYVGYDFNHESPPTRDFVDDVNRYWLEeYHIDGFRFDLTKGF 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21954500 210 W--PADLGNIYG----RLKNLN--TDHGFASGSKAYIVQEVIDMGGE 248
Cdd:cd11350 182 TqkPTGGGAWGGydaaRIDFLKryADEAKAVDKDFYVIAEHLPDNPE 228
PLN00196 PLN00196
alpha-amylase; Provisional
 87-218 3.43e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 39.90  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500   87 TRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASpssksyPGVPYSSLDFNPTCAINN---YND--A 161
Cdd:PLN00196  86 SKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFE------GGTPDSRLDWGPHMICRDdtqYSDgtG 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21954500  162 NQVRNCELVGLRDLNQGNSYVQEKVAEFLNHL-IDLGVAGFRVDAAKHmWPADLGNIY 218
Cdd:PLN00196 160 NLDTGADFAAAPDIDHLNKRVQRELIGWLLWLkSDIGFDAWRLDFAKG-YSAEVAKVY 216
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
 170-209 4.99e-03

Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200467 [Multi-domain]  Cd Length: 470  Bit Score: 39.14  E-value: 4.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21954500 170 VGLRDLNQGNSYVQEKVAEFLNHLIDLGVAGFRVDAAKHM 209
Cdd:cd11328 168 VKQPDLNYRNPKVVEEMKNVLRFWLDKGVDGFRIDAVPHL 207
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 172-342 9.51e-03

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


Pssm-ID: 200489 [Multi-domain]  Cd Length: 443  Bit Score: 38.45  E-value: 9.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 172 LRDLNQGNSYVQEKVaefLNHLIDL--------GVAGFRVDAAKHMWPADLgNIYGrlknlNTDHGFA-SGSKA--YIVQ 240
Cdd:cd11352 208 LKDFRTGSGSIPSAA---LDILARVyqywiayaDIDGFRIDTVKHMEPGAA-RYFC-----NAIKEFAqSIGKDnfFLFG 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21954500 241 EVIDmGGEAISK--SEYTGLGA---ITEFRHS--------DSIGKAFRGKDQlRYLSNWGT-AWgfaASDRSLVFVDNHD 306
Cdd:cd11352 279 EITG-GREAAAYedLDVTGLDAaldIPEIPFKlenvakglAPPAEYFQLFEN-SKLVGMGShRW---YGKFHVTFLDDHD 353

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21954500 307 --NQRGHGAGGADVLTYkvpKQYKMASAFMLAHPfGTP 342
Cdd:cd11352 354 qvGRFYKKRRAADAAGD---AQLAAALALNLFTL-GIP 387
 
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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