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Conserved domains on  [gi|1959302532|gb|KAG1969337|]
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alpha-amylase [Pimephales promelas]

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, ...
 71-463 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: 585.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  71 RTAIVHLFEWRWADIAAECERFLGPNGFGGVQISPPSESIVVtnPWHPWWQRYQPIGYNLCSRSGNENELRDMITRCNNV 150
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 151 GVYIYVDAVINHMCGagggsgthsscgsyfnannkdfptvpysnldfndgkcntgsgnienyqDVNQVRNCRLVGLLDLA 230
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 231 LEKDYVRGKTSDYMNKLIDMGVAGFRVDACKHMWPGDLSAVYGRLHNLNTKwfPSGSRPFIFQEVIDLGGEPITSSEYTG 310
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 311 VGRVTEFKYGAKLGNVIRKWNGEKLSflKNWGEGWGFMPSDKALVFTDNHDNQRGHGAGGaSIVTFWDARIYKMAVAFML 390
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLLLL--KNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959302532 391 AHPYGFTRVMSSYRWDrnivngqdqNDWIGPPSNGDGSTKPVTINADGTCGNGWVCEHRWRQITNMVGFRNVV 463
Cdd:cd11317   266 AWPYGTPRVMSSYYFS---------DSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
470-557 1.49e-29

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 111.18  E-value: 1.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  470 NWWDNGSNQISFSRGNRGFLVINNDDWELNATLNTGLPGGTYCDIIsgqkeSGRCTGKQVTVGGDGRASIRISNSEEdpf 549
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVI-----SGLCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 1959302532  550 MAIHADSK 557
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, ...
 71-463 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: 585.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  71 RTAIVHLFEWRWADIAAECERFLGPNGFGGVQISPPSESIVVtnPWHPWWQRYQPIGYNLCSRSGNENELRDMITRCNNV 150
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 151 GVYIYVDAVINHMCGagggsgthsscgsyfnannkdfptvpysnldfndgkcntgsgnienyqDVNQVRNCRLVGLLDLA 230
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 231 LEKDYVRGKTSDYMNKLIDMGVAGFRVDACKHMWPGDLSAVYGRLHNLNTKwfPSGSRPFIFQEVIDLGGEPITSSEYTG 310
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 311 VGRVTEFKYGAKLGNVIRKWNGEKLSflKNWGEGWGFMPSDKALVFTDNHDNQRGHGAGGaSIVTFWDARIYKMAVAFML 390
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLLLL--KNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959302532 391 AHPYGFTRVMSSYRWDrnivngqdqNDWIGPPSNGDGSTKPVTINADGTCGNGWVCEHRWRQITNMVGFRNVV 463
Cdd:cd11317   266 AWPYGTPRVMSSYYFS---------DSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
470-557 1.49e-29

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 111.18  E-value: 1.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  470 NWWDNGSNQISFSRGNRGFLVINNDDWELNATLNTGLPGGTYCDIIsgqkeSGRCTGKQVTVGGDGRASIRISNSEEdpf 549
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVI-----SGLCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 1959302532  550 MAIHADSK 557
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
74-167 2.70e-24

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 99.33  E-value: 2.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532   74 IVHLFEWR-------WADIAAECErFLGPNGFGGVQISPPSESIVVtnpwHPWWQRYQPIGYNLC-SRSGNENELRDMIT 145
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 1959302532  146 RCNNVGVYIYVDAVINHMCGAG 167
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDGG 99
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 468-555 1.42e-16

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 75.07  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 468 FSNWWDNGSNQISFSRGN---RGFLVINNDDWELNATLNTGLP-GGTYCDIISGQKE--SGRCTGKQVTVGGDGRASIRI 541
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 1959302532 542 SNSEEDPFMAIHAD 555
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 135-390 4.13e-09

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: 58.14  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 135 GNENELRDMITRCNNVGVYIYVDAVINHMCGAGGG-----SGTHSSCGSYFNANNKDFPTVPYSNLDFNDG---KCNTGS 206
Cdd:pfam00128  49 GTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWfqesrSSKDNPYRDYYFWRPGGGPIPPNNWRSYFGGsawTYDEKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 207 GNIENYQDVnqvrncrlVGLLDLALEKDYVRGKTSDYMNKLIDMGVAGFRVDACKHM--WPGDLSAVYG-RLHNLNT--K 281
Cdd:pfam00128 129 QEYYLHLFV--------AGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHIskVPGLPFENNGpFWHEFTQamN 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 282 WFPSGSRP-FIFQEVIDLGGEPI---TSSEYTGVGRVTEFK-YGAKLGNVIrKWNGEKLSF--LKNWGEGW-GFMPSDKA 353
Cdd:pfam00128 201 ETVFGYKDvMTVGEVFHGDGEWArvyTTEARMELEMGFNFPhNDVALKPFI-KWDLAPISArkLKEMITDWlDALPDTNG 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1959302532 354 LVFT--DNHDNQRghgaggasIVTFW--DARIYKMAVAFML 390
Cdd:pfam00128 280 WNFTflGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
244-393 5.05e-09

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 58.34  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 244 MNKLIDMGVAGFRVDACKHMW-----PGDLSAVYGRLHNLN--TKWFPSGSrpFIFQEVIdlGGEPITSSEYTGVGR--- 313
Cdd:COG0366   185 LRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLRELRaaVDEYYPDF--FLVGEAW--VDPPEDVARYFGGDEldm 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 314 VTEFKYGAKLGNVIRKWNGEKL-SFLKNWGEGwgfMPSDKALV-FTDNHDNQRghgaggasIVTFW----DARIYKMAVA 387
Cdd:COG0366   261 AFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEGGWWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAA 329


                  ....*.
gi 1959302532 388 FMLAHP 393
Cdd:COG0366   330 LLLTLP 335
PLN02784 PLN02784
alpha-amylase
 67-266 1.11e-06

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 51.55  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  67 TQSGRTAIVHLFEW------RWADIAAECERFLGPNGFGGVQISPPSESIvvtNPwhpwwQRYQPIG-YNLCSRSGNENE 139
Cdd:PLN02784  498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 140 LRDMITRCNNVGVYIYVDAVINHMCGA-GGGSGTHSSCGSYFNANNKdfpTVPYSNLDFNdGKCNTGSG-------NIEN 211
Cdd:PLN02784  570 LKDLVKSFHEVGIKVLGDAVLNHRCAHfQNQNGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGdnfhaapNIDH 645

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1959302532 212 YQdvnqvrncrlvglldlalekDYVRGKTSDYMNKLID-MGVAGFRVDACKHMWPG 266
Cdd:PLN02784  646 SQ--------------------DFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGG 681
 
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, ...
 71-463 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: 585.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  71 RTAIVHLFEWRWADIAAECERFLGPNGFGGVQISPPSESIVVtnPWHPWWQRYQPIGYNLCSRSGNENELRDMITRCNNV 150
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 151 GVYIYVDAVINHMCGagggsgthsscgsyfnannkdfptvpysnldfndgkcntgsgnienyqDVNQVRNCRLVGLLDLA 230
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 231 LEKDYVRGKTSDYMNKLIDMGVAGFRVDACKHMWPGDLSAVYGRLHNLNTKwfPSGSRPFIFQEVIDLGGEPITSSEYTG 310
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 311 VGRVTEFKYGAKLGNVIRKWNGEKLSflKNWGEGWGFMPSDKALVFTDNHDNQRGHGAGGaSIVTFWDARIYKMAVAFML 390
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLLLL--KNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959302532 391 AHPYGFTRVMSSYRWDrnivngqdqNDWIGPPSNGDGSTKPVTINADGTCGNGWVCEHRWRQITNMVGFRNVV 463
Cdd:cd11317   266 AWPYGTPRVMSSYYFS---------DSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 73-421 2.51e-47

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: 168.61  E-value: 2.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  73 AIVHLFEWRWADIAAECERfLGPNGFGGVQISPPSESIVVTNPWHPWWQRYQPIGYNLC-SRSGNENELRDMITRCNNVG 151
Cdd:cd11315     3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGnNQLGTEDDFKALCAAAHKYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 152 VYIYVDAVINHMcgAGGGSGthsscgsyfnANNKDFPTVPYSNLDFNDGKcntGSGNIENYQDVNQVRNCRLVGLLDLAL 231
Cdd:cd11315    82 IKIIVDVVFNHM--ANEGSA----------IEDLWYPSADIELFSPEDFH---GNGGISNWNDRWQVTQGRLGGLPDLNT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 232 EKDYVRGKTSDYMNKLIDMGVAGFRVDACKHM-WPGDLSavYGRLHNLNTKWFPSGSRPFIFQEVIDLGGEPITS-SEYT 309
Cdd:cd11315   147 ENPAVQQQQKAYLKALVALGVDGFRFDAAKHIeLPDEPS--KASDFWTNILNNLDKDGLFIYGEVLQDGGSRDSDyASYL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 310 GVGRVTEFKYGAKLGNVIRKWNGEKLSFLKNWgegWGF-MPSDKALVFTDNHDNQrgHGAGGASivTFWDARIYKMAVAF 388
Cdd:cd11315   225 SLGGVTASAYGFPLRGALKNAFLFGGSLDPAS---YGQaLPSDRAVTWVESHDTY--NNDGFES--TGLDDEDERLAWAY 297

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1959302532 389 MLAHPYGFTRVmssyrWDRNiVNGQDQNDWIGP 421
Cdd:cd11315   298 LAARDGGTPLF-----FSRP-NGSGGTNPQIGD 324
Aamy_C smart00632
Aamy_C domain;
470-557 1.49e-29

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 111.18  E-value: 1.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  470 NWWDNGSNQISFSRGNRGFLVINNDDWELNATLNTGLPGGTYCDIIsgqkeSGRCTGKQVTVGGDGRASIRISNSEEdpf 549
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVI-----SGLCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 1959302532  550 MAIHADSK 557
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
74-167 2.70e-24

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 99.33  E-value: 2.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532   74 IVHLFEWR-------WADIAAECErFLGPNGFGGVQISPPSESIVVtnpwHPWWQRYQPIGYNLC-SRSGNENELRDMIT 145
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 1959302532  146 RCNNVGVYIYVDAVINHMCGAG 167
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDGG 99
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 468-555 1.42e-16

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 75.07  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 468 FSNWWDNGSNQISFSRGN---RGFLVINNDDWELNATLNTGLP-GGTYCDIISGQKE--SGRCTGKQVTVGGDGRASIRI 541
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 1959302532 542 SNSEEDPFMAIHAD 555
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 97-266 2.37e-16

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: 81.07  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  97 GFGGVQISPPSESIVVTNPW----HPWWQryQPIgYNLCSRSGNENELRDMITRCNNVGVYIYVDAVINHMCGAGGGSgt 172
Cdd:cd11319    56 GFDAIWISPIVKNIEGNTAYgeayHGYWA--QDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGS-- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 173 hsscgsyfnannkdfpTVPYSNLD-FNDGK-----CntgsgNIENYQDVNQVRNCRL----VGLLDLALEKDYVRGKTSD 242
Cdd:cd11319   131 ----------------DVDYSSFVpFNDSSyyhpyC-----WITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLND 189

                         170       180
                  ....*....|....*....|....*....
gi 1959302532 243 YMNKLI-DMGVAGFRVDACKHM----WPG 266
Cdd:cd11319   190 WIKNLVsNYSIDGLRIDTAKHVrkdfWPG 218
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 97-390 6.87e-13

Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 70.39  E-value: 6.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  97 GFGGVQISPPSESIVVTNP------WHPWWQR--YQPIGYnlcsrSGNENELRDMITRCNNVGVYIYVDAVINHMCGA-G 167
Cdd:cd11320    60 GVTAIWISPPVENINSPIEgggntgYHGYWARdfKRTNEH-----FGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAdY 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 168 GGSGTHSSCGSYFNANNKDFPTVpysnldFNdgkcntGSGNIENYQDVNQVRNCRLVGLLDLALEKDYVRGKTSDYMNKL 247
Cdd:cd11320   135 AEDGALYDNGTLVGDYPNDDNGW------FH------HNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFW 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 248 IDMGVAGFRVDACKHMWPGDL----SAVYGRlHNLNT--KWFPSGSRPfifqevidLGGEPITSSEYTGVGrVTEFKYGA 321
Cdd:cd11320   203 LDHGIDGIRVDAVKHMPPGWQksfaDAIYSK-KPVFTfgEWFLGSPDP--------GYEDYVKFANNSGMS-LLDFPLNQ 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959302532 322 KLGNVIRKwNGEKLSFLKNWGEGWG--FMPSDKALVFTDNHDNQRGHGAGGAsivtfwDARiYKMAVAFML 390
Cdd:cd11320   273 AIRDVFAG-FTATMYDLDAMLQQTSsdYNYENDLVTFIDNHDMPRFLTLNNN------DKR-LHQALAFLL 335
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 135-390 4.13e-09

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: 58.14  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 135 GNENELRDMITRCNNVGVYIYVDAVINHMCGAGGG-----SGTHSSCGSYFNANNKDFPTVPYSNLDFNDG---KCNTGS 206
Cdd:pfam00128  49 GTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWfqesrSSKDNPYRDYYFWRPGGGPIPPNNWRSYFGGsawTYDEKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 207 GNIENYQDVnqvrncrlVGLLDLALEKDYVRGKTSDYMNKLIDMGVAGFRVDACKHM--WPGDLSAVYG-RLHNLNT--K 281
Cdd:pfam00128 129 QEYYLHLFV--------AGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHIskVPGLPFENNGpFWHEFTQamN 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 282 WFPSGSRP-FIFQEVIDLGGEPI---TSSEYTGVGRVTEFK-YGAKLGNVIrKWNGEKLSF--LKNWGEGW-GFMPSDKA 353
Cdd:pfam00128 201 ETVFGYKDvMTVGEVFHGDGEWArvyTTEARMELEMGFNFPhNDVALKPFI-KWDLAPISArkLKEMITDWlDALPDTNG 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1959302532 354 LVFT--DNHDNQRghgaggasIVTFW--DARIYKMAVAFML 390
Cdd:pfam00128 280 WNFTflGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
244-393 5.05e-09

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 58.34  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 244 MNKLIDMGVAGFRVDACKHMW-----PGDLSAVYGRLHNLN--TKWFPSGSrpFIFQEVIdlGGEPITSSEYTGVGR--- 313
Cdd:COG0366   185 LRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLRELRaaVDEYYPDF--FLVGEAW--VDPPEDVARYFGGDEldm 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 314 VTEFKYGAKLGNVIRKWNGEKL-SFLKNWGEGwgfMPSDKALV-FTDNHDNQRghgaggasIVTFW----DARIYKMAVA 387
Cdd:COG0366   261 AFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEGGWWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAA 329


                  ....*.
gi 1959302532 388 FMLAHP 393
Cdd:COG0366   330 LLLTLP 335
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 97-169 4.78e-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: 51.84  E-value: 4.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1959302532  97 GFGGVQISPPSESiVVTNPwhpwwQRYQPIG-YNLCSRSGNENELRDMITRCNNVGVYIYVDAVINHMCGAGGG 169
Cdd:cd11314    31 GFTAIWLPPPSKS-VSGSS-----MGYDPGDlYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGPDTG 98
PLN02784 PLN02784
alpha-amylase
 67-266 1.11e-06

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 51.55  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  67 TQSGRTAIVHLFEW------RWADIAAECERFLGPNGFGGVQISPPSESIvvtNPwhpwwQRYQPIG-YNLCSRSGNENE 139
Cdd:PLN02784  498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 140 LRDMITRCNNVGVYIYVDAVINHMCGA-GGGSGTHSSCGSYFNANNKdfpTVPYSNLDFNdGKCNTGSG-------NIEN 211
Cdd:PLN02784  570 LKDLVKSFHEVGIKVLGDAVLNHRCAHfQNQNGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGdnfhaapNIDH 645

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1959302532 212 YQdvnqvrncrlvglldlalekDYVRGKTSDYMNKLID-MGVAGFRVDACKHMWPG 266
Cdd:PLN02784  646 SQ--------------------DFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGG 681
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 228-364 8.23e-06

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


Pssm-ID: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 48.02  E-value: 8.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 228 DLALEKDYVRgktsDYM----NKLIDMGVAGFRVDACKHMWPGDLSAVYGRLHNLNTKwfpsgsrP--FIFQEVIDlgGE 301
Cdd:cd11339   126 DLNTENPEVV----DYLidayKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGK-------PdfFMFGEVYD--GD 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1959302532 302 PITSSEYT---GVGRVTEFKYGAKLGNVIRKWN-GEKLSFLKNwgEGWGFMPSDKALVFTDNHDNQR 364
Cdd:cd11339   193 PSYIAPYTttaGGDSVLDFPLYGAIRDAFAGGGsGDLLQDLFL--SDDLYNDATELVTFLDNHDMGR 257
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 135-263 2.15e-05

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 47.19  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 135 GNENELRDMITRCNNVGVYIYVDAVINHMCGAG----------------------------------GGSGTHSScgsyF 180
Cdd:PRK09441   78 GTKEELLNAIDALHENGIKVYADVVLNHKAGADeketfrvvevdpddrtqiisepyeiegwtrftfpGRGGKYSD----F 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532 181 NANNKDFPTVPYSNLDFNDGKC-NTGSGNIENYQDVNQVRNCRLVGLLDLALEKDYVRGKTSDYMNKLID-MGVAGFRVD 258
Cdd:PRK09441  154 KWHWYHFSGTDYDENPDESGIFkIVGDGKGWDDQVDDENGNFDYLMGADIDFRHPEVREELKYWAKWYMEtTGFDGFRLD 233


                  ....*
gi 1959302532 259 ACKHM 263
Cdd:PRK09441  234 AVKHI 238
PLN02361 PLN02361
alpha-amylase
 68-171 3.32e-03

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 40.18  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959302532  68 QSGRTAIVHLFEWR------WADIAAECERfLGPNGFGGVQISPPSESIvvtNPwhpwwQRYQPIG-YNLCSRSGNENEL 140
Cdd:PLN02361    8 RNGREILLQAFNWEshkhdwWRNLEGKVPD-LAKSGFTSAWLPPPSQSL---AP-----EGYLPQNlYSLNSAYGSEHLL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1959302532 141 RDMITRCNNVGVYIYVDAVINHMCGAGGGSG 171
Cdd:PLN02361   79 KSLLRKMKQYNVRAMADIVINHRVGTTQGHG 109
 
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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