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Conserved domains on  [gi|19850140|gb|AAL99578|]
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putative amylase-related protein AMYREL [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, ...
 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: 530.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  30 RNTIVHLFEWKWSDIAEECETFLVPRGFAGVQVSPVNENIIAAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 110 RIYVDVLLNHMSGDfdgvavgtagteaepskksfpgvpytaqdfhpsceitdwndRFQVQECELVGLKDLNQHSDYVRSK 189
Cdd:cd11317  81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 190 LIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSNLNiehGFPHNARPFIFQEVIDHGHETVSREEYNQLGAVTEFR 269
Cdd:cd11317 120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 270 FSEEIGRAFRGNNALKWLQSWGTDWGFLNSEQALTFVDNHDNQRDHGS---VLNYKSPRQYKMATAFHLAYPYGISRVMS 346
Cdd:cd11317 197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGggdMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 19850140 347 SFAFDDHDTPPPQDAQENIISPEFDEDGACVNGWICEHRWRQIYAMVGFKNAV 399
Cdd:cd11317 277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
407-493 2.74e-32

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 118.11  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140    407 WWDNGDNQISFCRGNKGFLAVNNNLYDLSQELNTCLPAGEYCDVISGSlidgaCTGKSVTVNEYGYGYIHIGSddfDGVL 486
Cdd:smart00632   3 WWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISGL-----CTGKSVTVGSNGIATFTLPA---GGAV 74


                   ....*..
gi 19850140    487 ALHVNAK 493
Cdd:smart00632  75 AIHVDAK 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: 530.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  30 RNTIVHLFEWKWSDIAEECETFLVPRGFAGVQVSPVNENIIAAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 110 RIYVDVLLNHMSGDfdgvavgtagteaepskksfpgvpytaqdfhpsceitdwndRFQVQECELVGLKDLNQHSDYVRSK 189
Cdd:cd11317  81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 190 LIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSNLNiehGFPHNARPFIFQEVIDHGHETVSREEYNQLGAVTEFR 269
Cdd:cd11317 120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 270 FSEEIGRAFRGNNALKWLQSWGTDWGFLNSEQALTFVDNHDNQRDHGS---VLNYKSPRQYKMATAFHLAYPYGISRVMS 346
Cdd:cd11317 197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGggdMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 19850140 347 SFAFDDHDTPPPQDAQENIISPEFDEDGACVNGWICEHRWRQIYAMVGFKNAV 399
Cdd:cd11317 277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
407-493 2.74e-32

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 118.11  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140    407 WWDNGDNQISFCRGNKGFLAVNNNLYDLSQELNTCLPAGEYCDVISGSlidgaCTGKSVTVNEYGYGYIHIGSddfDGVL 486
Cdd:smart00632   3 WWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISGL-----CTGKSVTVGSNGIATFTLPA---GGAV 74


                   ....*..
gi 19850140    487 ALHVNAK 493
Cdd:smart00632  75 AIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
32-123 5.78e-27

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 106.64  E-value: 5.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140     32 TIVHLFEWK-------WSDIAEECEtFLVPRGFAGVQVSPVNENIIaaGRPWWERYQPISYK-LTTRSGNEEEFADMVRR 103
Cdd:smart00642   2 IYPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKqIDPRFGTMEDFKELVDA 78

                           90       100
                   ....*....|....*....|
gi 19850140    104 CNDVGIRIYVDVLLNHMSGD 123
Cdd:smart00642  79 AHARGIKVILDVVINHTSDG 98
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
92-338 1.65e-15

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 78.37  E-value: 1.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  92 GNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFdgvavgtagteaeP----SKKSfPGVPYTA----QDFHPSCEITDWN 163
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDEH-------------PwfqeARAG-PDSPYRDwyvwRDGKPDLPPNNWF 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 164 DRFQV----------QECE---LVGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDleyiyGSLSNLNI 230
Cdd:COG0366 142 SIFGGsawtwdpedgQYYLhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDKDE-----GLPENLPE 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 231 EHGFPHNARPFIFQ---------EVIDHGHETVSReeY---NQLGAVTEFRFSEEIGRAFRGNNALKWLQSWgTDWGFLN 298
Cdd:COG0366 217 VHEFLRELRAAVDEyypdfflvgEAWVDPPEDVAR--YfggDELDMAFNFPLMPALWDALAPEDAAELRDAL-AQTPALY 293

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 19850140 299 SEQA--LTFVDNHDNQRdHGSVL-NYKSPRQYKMATAFHLAYP 338
Cdd:COG0366 294 PEGGwwANFLRNHDQPR-LASRLgGDYDRRRAKLAAALLLTLP 335
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 409-491 4.04e-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: 70.83  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   409 DNGDNQISFCRGN---KGFLAVNNNLYDLSQELNTCLP-AGEYCDVISG--SLIDGACTGKSVTVNEYGYGYIHIGSDDF 482
Cdd:pfam02806   6 DAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTddEEYGGSNTGEVVTVDGPGHPNSLTLTLPP 85


                  ....*....
gi 19850140   483 DGVLALHVN 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 5.73e-12

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 67.00  E-value: 5.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140    85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGTEaEPSKKSF---PGVPYTaqdfHPSCEI-- 159
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSSKD-NPYRDYYfwrPGGGPI----PPNNWRsy 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   160 ---TDWNDRFQVQECEL----VGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYgslSNLNIEH 232
Cdd:pfam00128 117 fggSAWTYDEKGQEYYLhlfvAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFE---NNGPFWH 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   233 GFPH--NARPFIFQEVI---DHGHETV---------SREEYNQLGAVTEFRFSEEIGRAFRGNN----ALK-WLQSWGTD 293
Cdd:pfam00128 194 EFTQamNETVFGYKDVMtvgEVFHGDGewarvytteARMELEMGFNFPHNDVALKPFIKWDLAPisarKLKeMITDWLDA 273

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 19850140   294 WGFLNSEQAlTFVDNHDNQRdHGSVLNYKSpRQYKMATAF 333
Cdd:pfam00128 274 LPDTNGWNF-TFLGNHDQPR-FLSRFGDDR-ASAKLLAVF 310
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 89-314 9.14e-05

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 44.88  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   89 TRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSG-----DFDGVAVGTAGTEAEPSKK---------SFPGV-------P 147
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadekeTFRVVEVDPDDRTQIISEPyeiegwtrfTFPGRggkysdfK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  148 YTAQDFHPsceiTDWNDR------FQVQECElvglKDLNQHSD-------------------YVRSKLIEFLDHLIE-LG 201
Cdd:PRK09441 155 WHWYHFSG----TDYDENpdesgiFKIVGDG----KGWDDQVDdengnfdylmgadidfrhpEVREELKYWAKWYMEtTG 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  202 VAGFRVDAAKHMAAedleYIYGSLSNLNIEHGfphNARPFIFQEVIDHGHETVSREEYNQLGAVTEFRFS--------EE 273
Cdd:PRK09441 227 FDGFRLDAVKHIDA----WFIKEWIEHVREVA---GKDLFIVGEYWSHDVDKLQDYLEQVEGKTDLFDVPlhynfheaSK 299

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 19850140  274 IGRAFRGNNALKwlqswGTDWGfLNSEQALTFVDNHDNQRD 314
Cdd:PRK09441 300 QGRDYDMRNIFD-----GTLVE-ADPFHAVTFVDNHDTQPG 334
 
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: 530.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  30 RNTIVHLFEWKWSDIAEECETFLVPRGFAGVQVSPVNENIIAAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 110 RIYVDVLLNHMSGDfdgvavgtagteaepskksfpgvpytaqdfhpsceitdwndRFQVQECELVGLKDLNQHSDYVRSK 189
Cdd:cd11317  81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 190 LIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSNLNiehGFPHNARPFIFQEVIDHGHETVSREEYNQLGAVTEFR 269
Cdd:cd11317 120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 270 FSEEIGRAFRGNNALKWLQSWGTDWGFLNSEQALTFVDNHDNQRDHGS---VLNYKSPRQYKMATAFHLAYPYGISRVMS 346
Cdd:cd11317 197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGggdMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 19850140 347 SFAFDDHDTPPPQDAQENIISPEFDEDGACVNGWICEHRWRQIYAMVGFKNAV 399
Cdd:cd11317 277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 32-355 6.91e-52

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: 179.40  E-value: 6.91e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  32 TIVHLFEWKWSDIAEECETfLVPRGFAGVQVSPVNENI--IAAGRPWWERYQPISYKLTTRS-GNEEEFADMVRRCNDVG 108
Cdd:cd11315   3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKegGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 109 IRIYVDVLLNHMSGDFDGVAVgtagteaePSKKSFPGVPYTAQDFHPSCEITDWNDRFQVQECELVGLKDLNQHSDYVRS 188
Cdd:cd11315  82 IKIIVDVVFNHMANEGSAIED--------LWYPSADIELFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 189 KLIEFLDHLIELGVAGFRVDAAKHMAAEDlEYIYGSLSNLNIeHGFPHNARPFIFQEVIDHGheTVSREEYNQLGAVTEF 268
Cdd:cd11315 154 QQKAYLKALVALGVDGFRFDAAKHIELPD-EPSKASDFWTNI-LNNLDKDGLFIYGEVLQDG--GSRDSDYASYLSLGGV 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 269 RFSeEIGRAFRgnNALKWLQSWGTDWGFLNSEQAL------TFVDNHDNQRDHGSVLNYKSPRQYKMATAFHLAYPYGIS 342
Cdd:cd11315 230 TAS-AYGFPLR--GALKNAFLFGGSLDPASYGQALpsdravTWVESHDTYNNDGFESTGLDDEDERLAWAYLAARDGGTP 306

                       330
                ....*....|...
gi 19850140 343 RVmssfaFDDHDT 355
Cdd:cd11315 307 LF-----FSRPNG 314
Aamy_C smart00632
Aamy_C domain;
407-493 2.74e-32

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 118.11  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140    407 WWDNGDNQISFCRGNKGFLAVNNNLYDLSQELNTCLPAGEYCDVISGSlidgaCTGKSVTVNEYGYGYIHIGSddfDGVL 486
Cdd:smart00632   3 WWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISGL-----CTGKSVTVGSNGIATFTLPA---GGAV 74


                   ....*..
gi 19850140    487 ALHVNAK 493
Cdd:smart00632  75 AIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
32-123 5.78e-27

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 106.64  E-value: 5.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140     32 TIVHLFEWK-------WSDIAEECEtFLVPRGFAGVQVSPVNENIIaaGRPWWERYQPISYK-LTTRSGNEEEFADMVRR 103
Cdd:smart00642   2 IYPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKqIDPRFGTMEDFKELVDA 78

                           90       100
                   ....*....|....*....|
gi 19850140    104 CNDVGIRIYVDVLLNHMSGD 123
Cdd:smart00642  79 AHARGIKVILDVVINHTSDG 98
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 56-355 4.54e-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: 95.05  E-value: 4.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  56 GFAGVQVSPVNENI----IAAGRPWWERYQPISYKLTTRS-GNEEEFADMVRRCNDVGIRIYVDVLLNHmSGDFDgvavg 130
Cdd:cd11320  60 GVTAIWISPPVENInspiEGGGNTGYHGYWARDFKRTNEHfGTWEDFDELVDAAHANGIKVIIDFVPNH-SSPAD----- 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 131 tagtEAEPSKKSFPGVPYTAQD------FHPSCEITDWNDRFQVQECELVGLKDLNQHSDYVRSKLIEFLDHLIELGVAG 204
Cdd:cd11320 134 ----YAEDGALYDNGTLVGDYPnddngwFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDG 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 205 FRVDAAKHMAAEDLE----YIYgslsnlniehgfphNARP-FIFQEVIDHGHETV---SREEYNQLG-AVTEFRFSEEIG 275
Cdd:cd11320 210 IRVDAVKHMPPGWQKsfadAIY--------------SKKPvFTFGEWFLGSPDPGyedYVKFANNSGmSLLDFPLNQAIR 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 276 RAFRGNNALKW-----LQSWGTDwgFLNSEQALTFVDNHDNQRdHGSVLNykSPRQYKMATAFHLAYP------YGISRV 344
Cdd:cd11320 276 DVFAGFTATMYdldamLQQTSSD--YNYENDLVTFIDNHDMPR-FLTLNN--NDKRLHQALAFLLTSRgipviyYGTEQY 350

                       330
                ....*....|.
gi 19850140 345 MSSFAFDDHDT 355
Cdd:cd11320 351 LHGGTQVGGDP 361
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 56-333 1.33e-20

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: 93.40  E-value: 1.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  56 GFAGVQVSPVNENI---IAAGRP----WWERYqpisYKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMsgdfdgva 128
Cdd:cd11319  56 GFDAIWISPIVKNIegnTAYGEAyhgyWAQDL----YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM-------- 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 129 vGTAGTEAEPSKKSFpgVPY-TAQDFHPSCEITDWNDRFQVQECEL----VGLKDLNQHSDYVRSKLIEFLDHLI-ELGV 202
Cdd:cd11319 124 -ASAGPGSDVDYSSF--VPFnDSSYYHPYCWITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSI 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 203 AGFRVDAAKHMAAEDLeyiygslsnlnieHGFPHNARPFIFQEVIDHGHETVSreEY-NQLGAVTEFRFSEEIGRAFrgn 281
Cdd:cd11319 201 DGLRIDTAKHVRKDFW-------------PGFVEAAGVFAIGEVFDGDPNYVC--PYqNYLDGVLNYPLYYPLVDAF--- 262

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19850140 282 nalkwLQSWGTDWGF---LNSEQAL--------TFVDNHDNQRdhgsVLNYKS-PRQYKMATAF 333
Cdd:cd11319 263 -----QSTKGSMSALvdtINSVQSSckdptllgTFLENHDNPR----FLSYTSdQALAKNALAF 317
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 27-338 2.17e-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: 2.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  27 WGNRNTIVHLFEWKWSDIAEECETfLVPRGFAGVQVSPVNENIiAAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCND 106
Cdd:cd00551  10 FTDGDSSGGDGGGDLKGIIDKLDY-LKDLGVTAIWLTPIFESP-EYDGYDKDDGYLDYYEIDPRLGTEEDFKELVKAAHK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 107 VGIRIYVDVLLNHmsgdfdgvavgtagteaepskksfpgvpytaqdfhpsceitdwndrfqvqecelvglkdlnqhsdyv 186
Cdd:cd00551  88 RGIKVILDLVFNH------------------------------------------------------------------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 187 rskliEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSNLNIEHGfphnARPFIFQEVIDHGHETVSREEYNQ-LGAV 265
Cdd:cd00551 101 -----DILRFWLDEGVDGFRLDAAKHVPKPEPVEFLREIRKDAKLAK----PDTLLLGEAWGGPDELLAKAGFDDgLDSV 171

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19850140 266 TEFRFSEEIgRAFRGNNALKWLQSWGTDWGFLNSEQALTFVDNHDNQRDHGSVLNYKSP---RQYKMATAFHLAYP 338
Cdd:cd00551 172 FDFPLLEAL-RDALKGGEGALAILAALLLLNPEGALLVNFLGNHDTFRLADLVSYKIVElrkARLKLALALLLTLP 246
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
92-338 1.65e-15

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 78.37  E-value: 1.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  92 GNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFdgvavgtagteaeP----SKKSfPGVPYTA----QDFHPSCEITDWN 163
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDEH-------------PwfqeARAG-PDSPYRDwyvwRDGKPDLPPNNWF 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 164 DRFQV----------QECE---LVGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDleyiyGSLSNLNI 230
Cdd:COG0366 142 SIFGGsawtwdpedgQYYLhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDKDE-----GLPENLPE 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 231 EHGFPHNARPFIFQ---------EVIDHGHETVSReeY---NQLGAVTEFRFSEEIGRAFRGNNALKWLQSWgTDWGFLN 298
Cdd:COG0366 217 VHEFLRELRAAVDEyypdfflvgEAWVDPPEDVAR--YfggDELDMAFNFPLMPALWDALAPEDAAELRDAL-AQTPALY 293

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 19850140 299 SEQA--LTFVDNHDNQRdHGSVL-NYKSPRQYKMATAFHLAYP 338
Cdd:COG0366 294 PEGGwwANFLRNHDQPR-LASRLgGDYDRRRAKLAAALLLTLP 335
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 409-491 4.04e-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: 70.83  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   409 DNGDNQISFCRGN---KGFLAVNNNLYDLSQELNTCLP-AGEYCDVISG--SLIDGACTGKSVTVNEYGYGYIHIGSDDF 482
Cdd:pfam02806   6 DAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTddEEYGGSNTGEVVTVDGPGHPNSLTLTLPP 85


                  ....*....
gi 19850140   483 DGVLALHVN 491
Cdd:pfam02806  86 LSALVLKVE 94
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 178-333 6.83e-13

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: 69.59  E-value: 6.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 178 DLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSNLNIEHGFphnarpFIFQEVIDHGHETVSR- 256
Cdd:cd11339 126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPDF------FMFGEVYDGDPSYIAPy 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 257 EEYNQLGAVTEFRFSEEIGRAFRGNNALKWLQSW-GTDWGFLNSEQALTFVDNHDNQRDhGSVLNYKSP---RQYKMATA 332
Cdd:cd11339 200 TTTAGGDSVLDFPLYGAIRDAFAGGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGRF-LSSLKDGSAdgtARLALALA 278


                .
gi 19850140 333 F 333
Cdd:cd11339 279 L 279
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 85-333 5.73e-12

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 67.00  E-value: 5.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140    85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGTEaEPSKKSF---PGVPYTaqdfHPSCEI-- 159
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSSKD-NPYRDYYfwrPGGGPI----PPNNWRsy 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   160 ---TDWNDRFQVQECEL----VGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYgslSNLNIEH 232
Cdd:pfam00128 117 fggSAWTYDEKGQEYYLhlfvAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFE---NNGPFWH 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   233 GFPH--NARPFIFQEVI---DHGHETV---------SREEYNQLGAVTEFRFSEEIGRAFRGNN----ALK-WLQSWGTD 293
Cdd:pfam00128 194 EFTQamNETVFGYKDVMtvgEVFHGDGewarvytteARMELEMGFNFPHNDVALKPFIKWDLAPisarKLKeMITDWLDA 273

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 19850140   294 WGFLNSEQAlTFVDNHDNQRdHGSVLNYKSpRQYKMATAF 333
Cdd:pfam00128 274 LPDTNGWNF-TFLGNHDQPR-FLSRFGDDR-ASAKLLAVF 310
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 85-313 2.57e-08

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: 55.80  E-value: 2.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGTEAEPSkksfpgvpytAQDFHPSCEITDwnD 164
Cdd:cd11354  67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALEDGPGSEE----------DRWHGHAGGGTP--A 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 165 RFQVQEcELVglkDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSnlniEHgFPHnarPFIFQ 244
Cdd:cd11354 135 VFEGHE-DLV---ELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPPEFWARVLPRVR----ER-HPD---AWILG 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 245 EVIdHGhetvsreEYNQLGA------VTEFrfseEIGRAFRgnNALKWLQSWGTDW------GFLNSEQALTFVDNHDNQ 312
Cdd:cd11354 203 EVI-HG-------DYAGIVAasgmdsVTQY----ELWKAIW--SSIKDRNFFELDWalgrhnEFLDSFVPQTFVGNHDVT 268


                .
gi 19850140 313 R 313
Cdd:cd11354 269 R 269
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 85-338 1.16e-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: 53.38  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVavgtagteaepskkSFPGVPytaqdfhpsceitdwnd 164
Cdd:cd11314  57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGPDTGE--------------DFGGAP----------------- 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 165 rfqvqecelvglkDLNQHSDYVRSKLIEFLDHLI-ELGVAGFRVDAAK----HMAAEDLEYIYGSLS------NLNIEHG 233
Cdd:cd11314 106 -------------DLDHTNPEVQNDLKAWLNWLKnDIGFDGWRFDFVKgyapSYVKEYNEATSPSFSvgeywdGLSYENQ 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 234 FPHnarpfiFQEVIDHGHETVSReeynqlGAVTEFRFSEEIGRAFrGNNALKWLQSW----GTDWGFlNSEQALTFVDNH 309
Cdd:cd11314 173 DAH------RQRLVDWIDATGGG------SAAFDFTTKYILQEAV-NNNEYWRLRDGqgkpPGLIGW-WPQKAVTFVDNH 238

                       250       260       270
                ....*....|....*....|....*....|
gi 19850140 310 DNQRDHGsvlNYKSPRQYKM-ATAFHLAYP 338
Cdd:cd11314 239 DTGSTQG---HWPFPTDNVLqGYAYILTHP 265
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 92-332 5.68e-06

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: 48.73  E-value: 5.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  92 GNEEEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDGVAVGTAG--------TEAEPSKKSFPGVP---YTAQDFHpsC 157
Cdd:cd11316  67 GTMEDFERLIAEAHKRGIKVIIDLVINHTSSEhpwFQEAASSPDSpyrdyyiwADDDPGGWSSWGGNvwhKAGDGGY--Y 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 158 EITDWNdrfqvqecelvGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHmAAEDLEYIYGSLSNLNIEHGF--- 234
Cdd:cd11316 145 YGAFWS-----------GMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKH-IYENGEGQADQEENIEFWKEFrdy 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 235 -----PHNarpFIFQEVIDHGhETVSREEYNQLGAVTEFRFSEEIGRA----FRGNNALKWLQSWGTDWGFLNSEQAL-T 304
Cdd:cd11316 213 vksvkPDA---YLVGEVWDDP-STIAPYYASGLDSAFNFDLAEAIIDSvkngGSGAGLAKALLRVYELYAKYNPDYIDaP 288

                       250       260
                ....*....|....*....|....*...
gi 19850140 305 FVDNHDNQRdHGSVLNYkSPRQYKMATA 332
Cdd:cd11316 289 FLSNHDQDR-VASQLGG-DEAKAKLAAA 314
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 89-314 9.14e-05

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 44.88  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   89 TRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSG-----DFDGVAVGTAGTEAEPSKK---------SFPGV-------P 147
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadekeTFRVVEVDPDDRTQIISEPyeiegwtrfTFPGRggkysdfK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  148 YTAQDFHPsceiTDWNDR------FQVQECElvglKDLNQHSD-------------------YVRSKLIEFLDHLIE-LG 201
Cdd:PRK09441 155 WHWYHFSG----TDYDENpdesgiFKIVGDG----KGWDDQVDdengnfdylmgadidfrhpEVREELKYWAKWYMEtTG 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  202 VAGFRVDAAKHMAAedleYIYGSLSNLNIEHGfphNARPFIFQEVIDHGHETVSREEYNQLGAVTEFRFS--------EE 273
Cdd:PRK09441 227 FDGFRLDAVKHIDA----WFIKEWIEHVREVA---GKDLFIVGEYWSHDVDKLQDYLEQVEGKTDLFDVPlhynfheaSK 299

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 19850140  274 IGRAFRGNNALKwlqswGTDWGfLNSEQALTFVDNHDNQRD 314
Cdd:PRK09441 300 QGRDYDMRNIFD-----GTLVE-ADPFHAVTFVDNHDTQPG 334
PLN02361 PLN02361
alpha-amylase
 22-224 1.64e-04

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 44.04  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   22 HNPQWWGNrntivhlFEWKWSDIAEEcetflvprGFAGVQVSPVNENIIAAGrpwwerYQPIS-YKLTTRSGNEEEFADM 100
Cdd:PLN02361  23 HKHDWWRN-------LEGKVPDLAKS--------GFTSAWLPPPSQSLAPEG------YLPQNlYSLNSAYGSEHLLKSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  101 VRRCNDVGIRIYVDVLLNH----------MSGDFDGVAVgTAGTEAEPSKKSFPGVPYTAQDFHpsceitdwndrfqvqe 170
Cdd:PLN02361  82 LRKMKQYNVRAMADIVINHrvgttqghggMYNRYDGIPL-PWDEHAVTSCTGGLGNRSTGDNFN---------------- 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19850140  171 celvGLKDLNQHSDYVRSKLIEFLDHLIE-LGVAGFRVDAAKHMAAEDL-EYIYGS 224
Cdd:PLN02361 145 ----GVPNIDHTQHFVRKDIIGWLIWLRNdVGFQDFRFDFAKGYSAKFVkEYIEAA 196
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 90-220 3.64e-04

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: 43.07  E-value: 3.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  90 RSGNEEEFADMVRRCNDVGIRIYVDVLLNHmSGD-FDGVAVGTAGTEAEPSKKSFPGVPYTA-----QDFHPSC------ 157
Cdd:cd11352  96 RFGTREDLRDLVDAAHARGIYVILDIILNH-SGDvFSYDDDRPYSSSPGYYRGFPNYPPGGWfiggdQDALPEWrpddai 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 158 ---------------EITDWNDRFQVQECELVGLKDLNQHSDYVRSKLiefLDHLIEL--------GVAGFRVDAAKHMA 214
Cdd:cd11352 175 wpaelqnleyytrkgRIRNWDGYPEYKEGDFFSLKDFRTGSGSIPSAA---LDILARVyqywiayaDIDGFRIDTVKHME 251


                ....*.
gi 19850140 215 AEDLEY 220
Cdd:cd11352 252 PGAARY 257
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 178-212 9.15e-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: 9.15e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19850140 178 DLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKH 212
Cdd:cd11329 203 DLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY 237
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 85-310 1.38e-03

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: 40.97  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFdgvavgtagteaepskksfpgvpytaqdfhpsceitDWND 164
Cdd:cd11337  64 YRIDRRLGTNEDFKALVAALHERGIRVVLDGVFNHVGRDF------------------------------------FWEG 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 165 RFqvqecELVglkDLNQHSDYVRSKLIEFLDHLIELG-VAGFRVDAAkhmaaedleYIygslsnlnIEHGFPHNARPF-- 241
Cdd:cd11337 108 HY-----DLV---KLNLDNPAVVDYLFDVVRFWIEEFdIDGLRLDAA---------YC--------LDPDFWRELRPFcr 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140 242 -------IFQEVIdHGhetvsreEYNQ------LGAVTEFRFSEEIGRAFRGNN--ALKW-LQSWGTDWGFLNSEQALTF 305
Cdd:cd11337 163 elkpdfwLMGEVI-HG-------DYNRwvndsmLDSVTNYELYKGLWSSHNDHNffEIAHsLNRLFRHNGLYRGFHLYTF 234


                ....*
gi 19850140 306 VDNHD 310
Cdd:cd11337 235 VDNHD 239
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
45-221 1.67e-03

bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 41.02  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140    45 AEECETFLVPRGFAGVQVSPV-----NENIIAAGRPWWERYQPISY-KLTTR--SGNEEEFADMVRRCNDVGIRIYVDVL 116
Cdd:PRK14510  189 APEAISYLKKLGVSIVELNPIfasvdEHHLPQLGLSNYWGYNTVAFlAPDPRlaPGGEEEFAQAIKEAQSAGIAVILDVV 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   117 LNHM-SGDFDGVAVGTAGTEAEPSKKSFPGvpytaqdfHPSCEITDWNdrfqvqeCELVglkdLNQHSDYVRSKLIEFLD 195
Cdd:PRK14510  269 FNHTgESNHYGPTLSAYGSDNSPYYRLEPG--------NPKEYENWWG-------CGNL----PNLERPFILRLPMDVLR 329

                         170       180
                  ....*....|....*....|....*.
gi 19850140   196 HLIELGVAGFRVDAAKHMAAEDLEYI 221
Cdd:PRK14510  330 SWAKRGVDGFRLDLADELAREPDGFI 355
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 85-213 1.72e-03

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: 40.63  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140  85 YKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDgvavgtagtEAEPSKKSfpgvPY--------TAQDF 153
Cdd:cd11334  65 YGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTSDQhpwFQ---------AARRDPDS----PYrdyyvwsdTPPKY 131

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19850140 154 H------PSCEITDWN-D---------RFQVQEcelvglKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHM 213
Cdd:cd11334 132 KdariifPDVEKSNWTwDevagayywhRFYSHQ------PDLNFDNPAVREEILRIMDFWLDLGVDGFRLDAVPYL 201
PLN02784 PLN02784
alpha-amylase
 37-126 3.06e-03

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 40.38  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19850140   37 FEW------KWSDIAEECETFLVPRGFAGVQVSPVNENIIAAGrpwwerYQPIS-YKLTTRSGNEEEFADMVRRCNDVGI 109
Cdd:PLN02784 509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVSPEG------YMPKDlYNLNSRYGTIDELKDLVKSFHEVGI 582

                         90
                 ....*....|....*..
gi 19850140  110 RIYVDVLLNHMSGDFDG 126
Cdd:PLN02784 583 KVLGDAVLNHRCAHFQN 599
 
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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