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Conserved domains on  [gi|1511001160|gb|AYU65434|]
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amylase-related protein [Drosophila lacteicornis]

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, ...
 30-399 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: 529.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  30 RNTIVHLFEWKWADIAEECEEFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 110 RIYVDVLLNHMSGDfdgvavgtggteaepskksfpgvpysaqdfhpsceitdwndRFQVQECELVGLKDLNQHSDYVRSK 189
Cdd:cd11317    81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 190 LIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYGSLSNLNiehGFPHNARAFIFQEVIDHGHETVSREEYNGLGAVTEFR 269
Cdd:cd11317   120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 270 FSEEIGNAFRGNNALKWLQSWGAGWGFLSSDQALTFVDNHDNQRDHGA---VLNYKSPKQYKMATAFHLAYPYGISRVMS 346
Cdd:cd11317   197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGggdMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1511001160 347 SFAFDDHDTPPPQDAQENIISPEFGEDGGCLNGWICEHRWRQIYAMVGFKNAV 399
Cdd:cd11317   277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
406-493 2.50e-31

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 115.41  E-value: 2.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  406 EWWDNGDSQISFCRGNKGFLAVNNNLYDLSQELNTCLPAGEYCDVISGSlvdgaCTGKSVKVNERGYGYIHIGSddfDGV 485
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISGL-----CTGKSVTVGSNGIATFTLPA---GGA 73


                   ....*...
gi 1511001160  486 LALHVDAK 493
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, ...
 30-399 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: 529.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  30 RNTIVHLFEWKWADIAEECEEFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 110 RIYVDVLLNHMSGDfdgvavgtggteaepskksfpgvpysaqdfhpsceitdwndRFQVQECELVGLKDLNQHSDYVRSK 189
Cdd:cd11317    81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 190 LIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYGSLSNLNiehGFPHNARAFIFQEVIDHGHETVSREEYNGLGAVTEFR 269
Cdd:cd11317   120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 270 FSEEIGNAFRGNNALKWLQSWGAGWGFLSSDQALTFVDNHDNQRDHGA---VLNYKSPKQYKMATAFHLAYPYGISRVMS 346
Cdd:cd11317   197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGggdMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1511001160 347 SFAFDDHDTPPPQDAQENIISPEFGEDGGCLNGWICEHRWRQIYAMVGFKNAV 399
Cdd:cd11317   277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
406-493 2.50e-31

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 115.41  E-value: 2.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  406 EWWDNGDSQISFCRGNKGFLAVNNNLYDLSQELNTCLPAGEYCDVISGSlvdgaCTGKSVKVNERGYGYIHIGSddfDGV 485
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISGL-----CTGKSVTVGSNGIATFTLPA---GGA 73


                   ....*...
gi 1511001160  486 LALHVDAK 493
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
32-123 7.72e-28

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 108.96  E-value: 7.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160   32 TIVHLFEWK-------WADIAEECEeFLAPRGFAGVQVSPVNENIIsaGRPWWERYQPISYK-LTTRSGNEEEFADMVRR 103
Cdd:smart00642   2 IYPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKqIDPRFGTMEDFKELVDA 78

                           90       100
                   ....*....|....*....|
gi 1511001160  104 CNDVGIRIYVDVLLNHMSGD 123
Cdd:smart00642  79 AHARGIKVILDVVINHTSDG 98
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
92-338 1.58e-15

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 78.37  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  92 GNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFdgvavgtggteaeP----SKKSfPGVPYSA----QDFHPSCEITDWN 163
Cdd:COG0366    76 GTLADFDELVAEAHARGIKVILDLVLNHTSDEH-------------PwfqeARAG-PDSPYRDwyvwRDGKPDLPPNNWF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 164 DRFQV----------QECE---LVGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHM-----ASEDLEYIYGSL 225
Cdd:COG0366   142 SIFGGsawtwdpedgQYYLhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLdkdegLPENLPEVHEFL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 226 SNLNiEHGFPHNARAFIFQEVIDHGHETVSReeY---NGLGAVTEFRFSEEIGNAFRGNNALKW---LQSWGAGWGflSS 299
Cdd:COG0366   222 RELR-AAVDEYYPDFFLVGEAWVDPPEDVAR--YfggDELDMAFNFPLMPALWDALAPEDAAELrdaLAQTPALYP--EG 296

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1511001160 300 DQALTFVDNHDNQRDHGAVLNYKSPKQYKMATAFHLAYP 338
Cdd:COG0366   297 GWWANFLRNHDQPRLASRLGGDYDRRRAKLAAALLLTLP 335
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 409-491 8.89e-15

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: 69.68  E-value: 8.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 409 DNGDSQISFCRGN---KGFLAVNNNLYDLSQELNTCLP-AGEYCDVISGSLV--DGACTGKSVKVNERGYGYIHIGSDDF 482
Cdd:pfam02806   6 DAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLTLTLPP 85


                  ....*....
gi 1511001160 483 DGVLALHVD 491
Cdd:pfam02806  86 LSALVLKVE 94
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 85-333 1.69e-11

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: 65.46  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTggTEAEPSKKSF----PGVPYSaqdfHPSCEI- 159
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESR--SSKDNPYRDYyfwrPGGGPI----PPNNWRs 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 160 ----TDWNDRFQVQECEL----VGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYgslSNLNIE 231
Cdd:pfam00128 116 yfggSAWTYDEKGQEYYLhlfvAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFE---NNGPFW 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 232 HGFPH--NARAFIFQEVI------------------DHGHETVSREEYNGLGAVTEFRFSEEIGNAfrgnNALKW---LQ 288
Cdd:pfam00128 193 HEFTQamNETVFGYKDVMtvgevfhgdgewarvyttEARMELEMGFNFPHNDVALKPFIKWDLAPI----SARKLkemIT 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1511001160 289 SW------GAGWGFlssdqalTFVDNHDNQRdhgaVLNYKS--PKQYKMATAF 333
Cdd:pfam00128 269 DWldalpdTNGWNF-------TFLGNHDQPR----FLSRFGddRASAKLLAVF 310
PLN02784 PLN02784
alpha-amylase
 37-310 1.80e-05

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 47.31  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  37 FEW------KWADIAEECEEFLAPRGFAGVQVSPVNENIISAGrpwwerYQPIS-YKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:PLN02784  509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVSPEG------YMPKDlYNLNSRYGTIDELKDLVKSFHEVGI 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 110 RIYVDVLLNHMSGDF---DGVAVGTGG--------TEAEPSKKSFPGVPYSAQDFHPSCEItdwndrfqvqecelvglkD 178
Cdd:PLN02784  583 KVLGDAVLNHRCAHFqnqNGVWNIFGGrlnwddraVVADDPHFQGRGNKSSGDNFHAAPNI------------------D 644

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 179 LNQhsDYVRSKLIEFLDHLI-ELGVAGFRVDAAK---------HM-ASE----------DLEYIYGSLSN---------- 227
Cdd:PLN02784  645 HSQ--DFVRKDLKEWLCWMRkEVGYDGWRLDFVRgfwggyvkdYMeASEpyfavgeywdSLSYTYGEMDYnqdahrqriv 722

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 228 --LNIEHGfphNARAFifqEVIDHG--HETVSREEYnglgavteFRFSEEIGNAfrgNNALKWLQSwgagwgflssdQAL 303
Cdd:PLN02784  723 dwINATNG---TAGAF---DVTTKGilHSALERCEY--------WRLSDQKGKP---PGVVGWWPS-----------RAV 774


                  ....*..
gi 1511001160 304 TFVDNHD 310
Cdd:PLN02784  775 TFIENHD 781
 
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, ...
 30-399 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: 529.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  30 RNTIVHLFEWKWADIAEECEEFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 110 RIYVDVLLNHMSGDfdgvavgtggteaepskksfpgvpysaqdfhpsceitdwndRFQVQECELVGLKDLNQHSDYVRSK 189
Cdd:cd11317    81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 190 LIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYGSLSNLNiehGFPHNARAFIFQEVIDHGHETVSREEYNGLGAVTEFR 269
Cdd:cd11317   120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 270 FSEEIGNAFRGNNALKWLQSWGAGWGFLSSDQALTFVDNHDNQRDHGA---VLNYKSPKQYKMATAFHLAYPYGISRVMS 346
Cdd:cd11317   197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGggdMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1511001160 347 SFAFDDHDTPPPQDAQENIISPEFGEDGGCLNGWICEHRWRQIYAMVGFKNAV 399
Cdd:cd11317   277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 32-399 1.31e-57

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: 194.80  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  32 TIVHLFEWKWADIAEECEEfLAPRGFAGVQVSPVNENI--ISAGRPWWERYQPISYKLTTRS-GNEEEFADMVRRCNDVG 108
Cdd:cd11315     3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKegGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 109 IRIYVDVLLNHMSGDFDGVAVgtggteaePSKKSFPGVPYSAQDFHPSCEITDWNDRFQVQECELVGLKDLNQHSDYVRS 188
Cdd:cd11315    82 IKIIVDVVFNHMANEGSAIED--------LWYPSADIELFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 189 KLIEFLDHLIELGVAGFRVDAAKHMASEDlEYIYGSLSNLNIEHGFPHNARaFIFQEVIDHGHETVSREE-YNGLGAVTE 267
Cdd:cd11315   154 QQKAYLKALVALGVDGFRFDAAKHIELPD-EPSKASDFWTNILNNLDKDGL-FIYGEVLQDGGSRDSDYAsYLSLGGVTA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 268 FRFSEEIGNAFRGNNAL---KWLQSWGAGwgfLSSDQALTFVDNHDNQRDHGAVLNYKSPKQYKMATAFHLAYPYGISRV 344
Cdd:cd11315   232 SAYGFPLRGALKNAFLFggsLDPASYGQA---LPSDRAVTWVESHDTYNNDGFESTGLDDEDERLAWAYLAARDGGTPLF 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511001160 345 mssfaFDDHDTpppqdaqeniispefgedGGCLNGWICEhRWRQIY------AMVGFKNAV 399
Cdd:cd11315   309 -----FSRPNG------------------SGGTNPQIGD-RGDDAWkspdvvAVNKFHNAM 345
Aamy_C smart00632
Aamy_C domain;
406-493 2.50e-31

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 115.41  E-value: 2.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  406 EWWDNGDSQISFCRGNKGFLAVNNNLYDLSQELNTCLPAGEYCDVISGSlvdgaCTGKSVKVNERGYGYIHIGSddfDGV 485
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISGL-----CTGKSVTVGSNGIATFTLPA---GGA 73


                   ....*...
gi 1511001160  486 LALHVDAK 493
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
32-123 7.72e-28

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 108.96  E-value: 7.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160   32 TIVHLFEWK-------WADIAEECEeFLAPRGFAGVQVSPVNENIIsaGRPWWERYQPISYK-LTTRSGNEEEFADMVRR 103
Cdd:smart00642   2 IYPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKqIDPRFGTMEDFKELVDA 78

                           90       100
                   ....*....|....*....|
gi 1511001160  104 CNDVGIRIYVDVLLNHMSGD 123
Cdd:smart00642  79 AHARGIKVILDVVINHTSDG 98
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 56-333 5.80e-21

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: 94.55  E-value: 5.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  56 GFAGVQVSPVNENIiSAGRPWWERY-----QPIsYKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVg 130
Cdd:cd11319    56 GFDAIWISPIVKNI-EGNTAYGEAYhgywaQDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDV- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 131 tggteaepSKKSFpgVPYSAQ-DFHPSCEITDWNDRFQVQECEL----VGLKDLNQHSDYVRSKLIEFLDHLI-ELGVAG 204
Cdd:cd11319   133 --------DYSSF--VPFNDSsYYHPYCWITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 205 FRVDAAKHMASEDLeyiygslsnlnieHGFPHNARAFIFQEVIDHGHETVSreEY-NGLGAVTEF--------RFSEEIG 275
Cdd:cd11319   203 LRIDTAKHVRKDFW-------------PGFVEAAGVFAIGEVFDGDPNYVC--PYqNYLDGVLNYplyyplvdAFQSTKG 267

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511001160 276 NAFRGNNALKWLQSwgagwgfLSSDQAL--TFVDNHDNQRdhgaVLNYKS-PKQYKMATAF 333
Cdd:cd11319   268 SMSALVDTINSVQS-------SCKDPTLlgTFLENHDNPR----FLSYTSdQALAKNALAF 317
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 56-355 7.38e-21

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: 94.28  E-value: 7.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  56 GFAGVQVSPVNENI-------ISAGrpwWERYQPISYKLTTRS-GNEEEFADMVRRCNDVGIRIYVDVLLNHmSGDFDgv 127
Cdd:cd11320    60 GVTAIWISPPVENInspieggGNTG---YHGYWARDFKRTNEHfGTWEDFDELVDAAHANGIKVIIDFVPNH-SSPAD-- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 128 AVGTGGTEAEPSKKsfPGVPYSAQD-FHPSCEITDWNDRFQVQECELVGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFR 206
Cdd:cd11320   134 YAEDGALYDNGTLV--GDYPNDDNGwFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 207 VDAAKHMASEDLE----YIYGSLSnlniehgfphnarAFIFQEVIDHGHETV---SREEYNGLG-AVTEFRFSEEIGNAF 278
Cdd:cd11320   212 VDAVKHMPPGWQKsfadAIYSKKP-------------VFTFGEWFLGSPDPGyedYVKFANNSGmSLLDFPLNQAIRDVF 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 279 RGNNALKW-----LQSWGAgwGFLSSDQALTFVDNHDNQRDHGAVLNYkspKQYKMATAFHLAYP------YGISRVMSS 347
Cdd:cd11320   279 AGFTATMYdldamLQQTSS--DYNYENDLVTFIDNHDMPRFLTLNNND---KRLHQALAFLLTSRgipviyYGTEQYLHG 353


                  ....*...
gi 1511001160 348 FAFDDHDT 355
Cdd:cd11320   354 GTQVGGDP 361
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 27-338 5.57e-17

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


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 80.68  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  27 WGNRNTIVHLFEWKWADIAEECEeFLAPRGFAGVQVSPVNENIiSAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCND 106
Cdd:cd00551    10 FTDGDSSGGDGGGDLKGIIDKLD-YLKDLGVTAIWLTPIFESP-EYDGYDKDDGYLDYYEIDPRLGTEEDFKELVKAAHK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 107 VGIRIYVDVLLNHmsgdfdgvavgtggteaepskksfpgvpysaqdfhpsceitdwndrfqvqecelvglkdlnqhsdyv 186
Cdd:cd00551    88 RGIKVILDLVFNH------------------------------------------------------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 187 rskliEFLDHLIELGVAGFRVDAAKHMASEDLEYIYGSLSNLNIEHGfphnARAFIFQEVIDHGHETVSREEY-NGLGAV 265
Cdd:cd00551   101 -----DILRFWLDEGVDGFRLDAAKHVPKPEPVEFLREIRKDAKLAK----PDTLLLGEAWGGPDELLAKAGFdDGLDSV 171

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511001160 266 TEFRFSEEIGNAFRGNNaLKWLQSWGAGWGFLSSDQALTFVDNHDNQRDHGAVLNYKSP---KQYKMATAFHLAYP 338
Cdd:cd00551   172 FDFPLLEALRDALKGGE-GALAILAALLLLNPEGALLVNFLGNHDTFRLADLVSYKIVElrkARLKLALALLLTLP 246
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
92-338 1.58e-15

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 78.37  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  92 GNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFdgvavgtggteaeP----SKKSfPGVPYSA----QDFHPSCEITDWN 163
Cdd:COG0366    76 GTLADFDELVAEAHARGIKVILDLVLNHTSDEH-------------PwfqeARAG-PDSPYRDwyvwRDGKPDLPPNNWF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 164 DRFQV----------QECE---LVGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHM-----ASEDLEYIYGSL 225
Cdd:COG0366   142 SIFGGsawtwdpedgQYYLhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLdkdegLPENLPEVHEFL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 226 SNLNiEHGFPHNARAFIFQEVIDHGHETVSReeY---NGLGAVTEFRFSEEIGNAFRGNNALKW---LQSWGAGWGflSS 299
Cdd:COG0366   222 RELR-AAVDEYYPDFFLVGEAWVDPPEDVAR--YfggDELDMAFNFPLMPALWDALAPEDAAELrdaLAQTPALYP--EG 296

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1511001160 300 DQALTFVDNHDNQRDHGAVLNYKSPKQYKMATAFHLAYP 338
Cdd:COG0366   297 GWWANFLRNHDQPRLASRLGGDYDRRRAKLAAALLLTLP 335
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 409-491 8.89e-15

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: 69.68  E-value: 8.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 409 DNGDSQISFCRGN---KGFLAVNNNLYDLSQELNTCLP-AGEYCDVISGSLV--DGACTGKSVKVNERGYGYIHIGSDDF 482
Cdd:pfam02806   6 DAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLTLTLPP 85


                  ....*....
gi 1511001160 483 DGVLALHVD 491
Cdd:pfam02806  86 LSALVLKVE 94
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 178-329 2.64e-12

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: 68.05  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 178 DLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYGSLSNLNIEHGFphnaraFIFQEVIDHGHETVSR- 256
Cdd:cd11339   126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPDF------FMFGEVYDGDPSYIAPy 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511001160 257 EEYNGLGAVTEFRFSEEIGNAFRGNNALKWLQSW-GAGWGFLSSDQALTFVDNHDNQRDhGAVLNYKSPKQYKM 329
Cdd:cd11339   200 TTTAGGDSVLDFPLYGAIRDAFAGGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGRF-LSSLKDGSADGTAR 272
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 85-333 1.69e-11

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: 65.46  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTggTEAEPSKKSF----PGVPYSaqdfHPSCEI- 159
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESR--SSKDNPYRDYyfwrPGGGPI----PPNNWRs 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 160 ----TDWNDRFQVQECEL----VGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYgslSNLNIE 231
Cdd:pfam00128 116 yfggSAWTYDEKGQEYYLhlfvAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFE---NNGPFW 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 232 HGFPH--NARAFIFQEVI------------------DHGHETVSREEYNGLGAVTEFRFSEEIGNAfrgnNALKW---LQ 288
Cdd:pfam00128 193 HEFTQamNETVFGYKDVMtvgevfhgdgewarvyttEARMELEMGFNFPHNDVALKPFIKWDLAPI----SARKLkemIT 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1511001160 289 SW------GAGWGFlssdqalTFVDNHDNQRdhgaVLNYKS--PKQYKMATAF 333
Cdd:pfam00128 269 DWldalpdTNGWNF-------TFLGNHDQPR----FLSRFGddRASAKLLAVF 310
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 85-319 7.25e-09

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: 57.34  E-value: 7.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHmsgdfdgvaVGTGGTEAEPSKKSFPGVPySAQDFHPSCEITDwnD 164
Cdd:cd11354    67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNH---------VGRSHPAVAQALEDGPGSE-EDRWHGHAGGGTP--A 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 165 RFQVQEcELVglkDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYGSLSnlniEHgFPHnarAFIFQ 244
Cdd:cd11354   135 VFEGHE-DLV---ELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPPEFWARVLPRVR----ER-HPD---AWILG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 245 EVIdHGHE-TVSREeyNGLGAVTEFRFSEEIGNAFRGNNAlkWLQSWGAGW--GFLSSDQALTFVDNHDNQR------DH 315
Cdd:cd11354   203 EVI-HGDYaGIVAA--SGMDSVTQYELWKAIWSSIKDRNF--FELDWALGRhnEFLDSFVPQTFVGNHDVTRiasqvgDD 277


                  ....
gi 1511001160 316 GAVL 319
Cdd:cd11354   278 GAAL 281
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 92-332 1.44e-07

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


Pssm-ID: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 53.74  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  92 GNEEEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDGVAVGTGG--------TEAEPSKKSFPGVP---YSAQDFHpsC 157
Cdd:cd11316    67 GTMEDFERLIAEAHKRGIKVIIDLVINHTSSEhpwFQEAASSPDSpyrdyyiwADDDPGGWSSWGGNvwhKAGDGGY--Y 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 158 EITDWNdrfqvqecelvGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAsEDLEYIYGSLSNLNIEHGF--- 234
Cdd:cd11316   145 YGAFWS-----------GMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIY-ENGEGQADQEENIEFWKEFrdy 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 235 --PHNARAFIFQEVIDHGhETVSREEYNGLGAVTEFRFSEEIG----NAFRGNNALKWLQSW-GAGWGFLSSDQALTFVD 307
Cdd:cd11316   213 vkSVKPDAYLVGEVWDDP-STIAPYYASGLDSAFNFDLAEAIIdsvkNGGSGAGLAKALLRVyELYAKYNPDYIDAPFLS 291

                         250       260
                  ....*....|....*....|....*
gi 1511001160 308 NHDNQRDHGAVLNykSPKQYKMATA 332
Cdd:cd11316   292 NHDQDRVASQLGG--DEAKAKLAAA 314
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 85-338 2.02e-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: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVavgtggteaepskkSFPGVPysaqdfhpsceitdwnd 164
Cdd:cd11314    57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGPDTGE--------------DFGGAP----------------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 165 rfqvqecelvglkDLNQHSDYVRSKLIEFLDHLI-ELGVAGFRVDAAK----HMASEDLEYIYGSLS------NLNIEHG 233
Cdd:cd11314   106 -------------DLDHTNPEVQNDLKAWLNWLKnDIGFDGWRFDFVKgyapSYVKEYNEATSPSFSvgeywdGLSYENQ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 234 FPHnarafiFQEVIDHGHETvsreeyNGLGAVTEFRFSEEIGNAFRGNNALKWLQSWGAGWGFLS--SDQALTFVDNHDN 311
Cdd:cd11314   173 DAH------RQRLVDWIDAT------GGGSAAFDFTTKYILQEAVNNNEYWRLRDGQGKPPGLIGwwPQKAVTFVDNHDT 240

                         250       260
                  ....*....|....*....|....*...
gi 1511001160 312 QRDHGavlNYKSPKQYKM-ATAFHLAYP 338
Cdd:cd11314   241 GSTQG---HWPFPTDNVLqGYAYILTHP 265
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 90-341 7.07e-07

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: 51.55  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  90 RSGNEEEFADMVRRCNDVGIRIYVDVLLNHmSGD-FDGVAVGTGGTEAEPSKKSFPGVPYSA-----QDFHPSC------ 157
Cdd:cd11352    96 RFGTREDLRDLVDAAHARGIYVILDIILNH-SGDvFSYDDDRPYSSSPGYYRGFPNYPPGGWfiggdQDALPEWrpddai 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 158 ---------------EITDWNDRFQVQECELVGLKDLNQHSDYVRSKLiefLDHLIEL--------GVAGFRVDAAKHMA 214
Cdd:cd11352   175 wpaelqnleyytrkgRIRNWDGYPEYKEGDFFSLKDFRTGSGSIPSAA---LDILARVyqywiayaDIDGFRIDTVKHME 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 215 SEDLEYIYGSLsnlnieHGFP---HNARAFIFQEVIDhGHE--TVSREEYNGLGA---VTEFRFS--------EEIGNAF 278
Cdd:cd11352   252 PGAARYFCNAI------KEFAqsiGKDNFFLFGEITG-GREaaAYEDLDVTGLDAaldIPEIPFKlenvakglAPPAEYF 324

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511001160 279 RGNNALKWLQSWGAGWgflSSDQALTFVDNHD-----NQRDHGAVLNYksPKQYKMATAFHLAYPyGI 341
Cdd:cd11352   325 QLFENSKLVGMGSHRW---YGKFHVTFLDDHDqvgrfYKKRRAADAAG--DAQLAAALALNLFTL-GI 386
PLN02784 PLN02784
alpha-amylase
 37-310 1.80e-05

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 47.31  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  37 FEW------KWADIAEECEEFLAPRGFAGVQVSPVNENIISAGrpwwerYQPIS-YKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:PLN02784  509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVSPEG------YMPKDlYNLNSRYGTIDELKDLVKSFHEVGI 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 110 RIYVDVLLNHMSGDF---DGVAVGTGG--------TEAEPSKKSFPGVPYSAQDFHPSCEItdwndrfqvqecelvglkD 178
Cdd:PLN02784  583 KVLGDAVLNHRCAHFqnqNGVWNIFGGrlnwddraVVADDPHFQGRGNKSSGDNFHAAPNI------------------D 644

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 179 LNQhsDYVRSKLIEFLDHLI-ELGVAGFRVDAAK---------HM-ASE----------DLEYIYGSLSN---------- 227
Cdd:PLN02784  645 HSQ--DFVRKDLKEWLCWMRkEVGYDGWRLDFVRgfwggyvkdYMeASEpyfavgeywdSLSYTYGEMDYnqdahrqriv 722

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 228 --LNIEHGfphNARAFifqEVIDHG--HETVSREEYnglgavteFRFSEEIGNAfrgNNALKWLQSwgagwgflssdQAL 303
Cdd:PLN02784  723 dwINATNG---TAGAF---DVTTKGilHSALERCEY--------WRLSDQKGKP---PGVVGWWPS-----------RAV 774


                  ....*..
gi 1511001160 304 TFVDNHD 310
Cdd:PLN02784  775 TFIENHD 781
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 85-213 1.56e-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: 44.09  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDGVAVGTGGTEA-------EPSKKS-----FPGVPYS 149
Cdd:cd11334    65 YGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTSDQhpwFQAARRDPDSPYRdyyvwsdTPPKYKdariiFPDVEKS 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511001160 150 AQDFHPSCEITDWNdRFQVQEcelvglKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHM 213
Cdd:cd11334   145 NWTWDEVAGAYYWH-RFYSHQ------PDLNFDNPAVREEILRIMDFWLDLGVDGFRLDAVPYL 201
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 89-314 2.05e-04

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 43.72  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  89 TRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSG-----DFDGVAVGTGGTEAEPSKK---------SFPGVP--YSA-- 150
Cdd:PRK09441   75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadekeTFRVVEVDPDDRTQIISEPyeiegwtrfTFPGRGgkYSDfk 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 151 ---QDFHPsceiTDWNDR------FQVQECElvglKDLNQHSD-------------------YVRSKLIEFLDHLIE-LG 201
Cdd:PRK09441  155 whwYHFSG----TDYDENpdesgiFKIVGDG----KGWDDQVDdengnfdylmgadidfrhpEVREELKYWAKWYMEtTG 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 202 VAGFRVDAAKHMasedleyiygslsnlniehgfphnaRAFIFQEVIDHGHETVSREEYnglgAVTEFrFSEEIG------ 275
Cdd:PRK09441  227 FDGFRLDAVKHI-------------------------DAWFIKEWIEHVREVAGKDLF----IVGEY-WSHDVDklqdyl 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511001160 276 NAFRGNNAL-------KWLQSWGAGWGF-LSS-----------DQALTFVDNHDNQRD 314
Cdd:PRK09441  277 EQVEGKTDLfdvplhyNFHEASKQGRDYdMRNifdgtlveadpFHAVTFVDNHDTQPG 334
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 85-310 2.30e-04

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


Pssm-ID: 200476 [Multi-domain]  Cd Length: 328  Bit Score: 43.28  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHmsgdfdgvaVGTGgteaepskksFPgvpysaqdfhpsceitdWND 164
Cdd:cd11337    64 YRIDRRLGTNEDFKALVAALHERGIRVVLDGVFNH---------VGRD----------FF-----------------WEG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 165 RFqvqecELVglkDLNQHSDYVRSKLIEFLDHLIELG-VAGFRVDAAKHMASEDLEYIYGSLSNLniehgFPHnarAFIF 243
Cdd:cd11337   108 HY-----DLV---KLNLDNPAVVDYLFDVVRFWIEEFdIDGLRLDAAYCLDPDFWRELRPFCREL-----KPD---FWLM 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511001160 244 QEVIdHGhetvsreEYN------GLGAVTEFRFSEEIGNAFRGNN--ALKWLQSWGAG-WGFLSSDQALTFVDNHD 310
Cdd:cd11337   172 GEVI-HG-------DYNrwvndsMLDSVTNYELYKGLWSSHNDHNffEIAHSLNRLFRhNGLYRGFHLYTFVDNHD 239
PLN02361 PLN02361
alpha-amylase
 22-224 2.33e-04

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 43.27  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160  22 HNPQWWGNrntivhlFEWKWADIAEEceeflaprGFAGVQVSPVNENIISAGrpwwerYQPIS-YKLTTRSGNEEEFADM 100
Cdd:PLN02361   23 HKHDWWRN-------LEGKVPDLAKS--------GFTSAWLPPPSQSLAPEG------YLPQNlYSLNSAYGSEHLLKSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511001160 101 VRRCNDVGIRIYVDVLLNH----------MSGDFDGVAVG---------TGGTEAEPSKKSFPGVPysaqdfhpsceitd 161
Cdd:PLN02361   82 LRKMKQYNVRAMADIVINHrvgttqghggMYNRYDGIPLPwdehavtscTGGLGNRSTGDNFNGVP-------------- 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511001160 162 wndrfqvqecelvglkDLNQHSDYVRSKLIEFLDHLIE-LGVAGFRVDAAKHMASEDL-EYIYGS 224
Cdd:PLN02361  148 ----------------NIDHTQHFVRKDIIGWLIWLRNdVGFQDFRFDFAKGYSAKFVkEYIEAA 196
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 178-212 8.99e-04

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: 41.60  E-value: 8.99e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1511001160 178 DLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKH 212
Cdd:cd11329   203 DLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY 237
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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