NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27530578|dbj|BAC53974|]
View 

amylase, partial [Drosophila cauverii]

Protein Classification

alpha-amylase family protein; alpha-amylase family glycosyl hydrolase( domain architecture ID 10183008)

alpha-amylase family protein may catalyze the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides; alpha-amylase family glycosyl hydrolase functions as a glycoside hydrolase that may act on starch, glycogen, and related oligo- and polysaccharides

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 1-348 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: 521.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   1 PNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggst 80
Cdd:cd11317  25 PAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMAGD---------- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  81 aspssksypgvpyssldfnptcainnyndANQVRNCELVGLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWP 160
Cdd:cd11317  95 -----------------------------ANEVRNCELVGLADLNTESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWP 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 161 ADLGVIYGRLKNLNTDhgfASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKDQLQYLTNWGTAWG 240
Cdd:cd11317 146 EDLAAILARLKDLNGG---PLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIKLLLLKNFGEGWG 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 241 FAASDRSLVFVDNHDNQRGHGAGGaDVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFN 320
Cdd:cd11317 223 LLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYFSDSDQGPPSDGSGNTLSVTIN 301

                       330       340
                ....*....|....*....|....*...
gi 27530578 321 SDNSCSGGWVCEHRWRQIYNMVAFRNAV 348
Cdd:cd11317 302 DDGTCGGGWVCEHRWPAIANMVGFRNAV 329
 
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, ...
 1-348 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: 521.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   1 PNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggst 80
Cdd:cd11317  25 PAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMAGD---------- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  81 aspssksypgvpyssldfnptcainnyndANQVRNCELVGLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWP 160
Cdd:cd11317  95 -----------------------------ANEVRNCELVGLADLNTESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWP 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 161 ADLGVIYGRLKNLNTDhgfASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKDQLQYLTNWGTAWG 240
Cdd:cd11317 146 EDLAAILARLKDLNGG---PLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIKLLLLKNFGEGWG 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 241 FAASDRSLVFVDNHDNQRGHGAGGaDVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFN 320
Cdd:cd11317 223 LLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYFSDSDQGPPSDGSGNTLSVTIN 301

                       330       340
                ....*....|....*....|....*...
gi 27530578 321 SDNSCSGGWVCEHRWRQIYNMVAFRNAV 348
Cdd:cd11317 302 DDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy smart00642
Alpha-amylase domain;
1-70 3.75e-20

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 86.23  E-value: 3.75e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27530578      1 PNGFAGVQVSPVNENAVkdSRPWWERYQPISYKLV-TRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAAD 70
Cdd:smart00642  30 DLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKQIdPRFGTMEDFKELVDAAHARGIKVILDVVINHTSDG 98
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
39-291 1.25e-16

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 80.29  E-value: 1.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  39 GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggstaSP---SSKSYPGVPYSS----LDFNPTCAINNYNDAN 111
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDE-----------HPwfqEARAGPDSPYRDwyvwRDGKPDLPPNNWFSIF 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 112 QVRNCELVGLR-------------DLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMW-----PADLGVIYGRLKNL 173
Cdd:COG0366 145 GGSAWTWDPEDgqyylhlffssqpDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLREL 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 174 NtDHGFASGSKAYIVQEVIDMGGEAISKseYTG---LGAITEFRHSDSIGKAFRGKD---------QLQYLTNWGTAWgf 241
Cdd:COG0366 225 R-AAVDEYYPDFFLVGEAWVDPPEDVAR--YFGgdeLDMAFNFPLMPALWDALAPEDaaelrdalaQTPALYPEGGWW-- 299

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27530578 242 aasdrsLVFVDNHDNQR-GHGAGGADVLtykvpKQYKMASAFMLAHPfGTP 291
Cdd:COG0366 300 ------ANFLRNHDQPRlASRLGGDYDR-----RRAKLAAALLLTLP-GTP 338
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 3-291 1.27e-12

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 67.77  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578     3 GFAGVQVSPVNENAVKDSRPWWERYqpisYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTAS 82
Cdd:pfam00128  17 GVTAIWLSPIFDSPQADHGYDIADY----YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSSKD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578    83 PSSKSY----PGVPYSSldfnPTCAINnYNDANQVRNCE----------LVGLRDLNQGNSYVQDKIVEFLDHLIDLGVA 148
Cdd:pfam00128  93 NPYRDYyfwrPGGGPIP----PNNWRS-YFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGID 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   149 GFRVDAAKHM--WPADLGVIYG-RLKNLNTDHG--FASGSKAYIVQEV-IDMGGEAISKSE--YTGLGAITEFRHSDsIG 220
Cdd:pfam00128 168 GFRIDVVKHIskVPGLPFENNGpFWHEFTQAMNetVFGYKDVMTVGEVfHGDGEWARVYTTeaRMELEMGFNFPHND-VA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   221 KAFRGKDQLQ---------YLTNWGTAWGFAASdRSLVFVDNHDNQRGHGAGGADVltykvpKQYKMASAFMLAHPfGTP 291
Cdd:pfam00128 247 LKPFIKWDLApisarklkeMITDWLDALPDTNG-WNFTFLGNHDQPRFLSRFGDDR------ASAKLLAVFLLTLR-GTP 318
PLN00196 PLN00196
alpha-amylase; Provisional
 36-167 2.30e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 39.52  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   36 TRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASpssksyPGVPYSSLDFNPTCAINN---YND--A 110
Cdd:PLN00196  86 SKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFE------GGTPDSRLDWGPHMICRDdtqYSDgtG 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 27530578  111 NQVRNCELVGLRDLNQGNSYVQDKIVEFLDHL-IDLGVAGFRVDAAKHmWPADLGVIY 167
Cdd:PLN00196 160 NLDTGADFAAAPDIDHLNKRVQRELIGWLLWLkSDIGFDAWRLDFAKG-YSAEVAKVY 216
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 1-348 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: 521.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   1 PNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggst 80
Cdd:cd11317  25 PAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMAGD---------- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  81 aspssksypgvpyssldfnptcainnyndANQVRNCELVGLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWP 160
Cdd:cd11317  95 -----------------------------ANEVRNCELVGLADLNTESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWP 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 161 ADLGVIYGRLKNLNTDhgfASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKDQLQYLTNWGTAWG 240
Cdd:cd11317 146 EDLAAILARLKDLNGG---PLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIKLLLLKNFGEGWG 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 241 FAASDRSLVFVDNHDNQRGHGAGGaDVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFN 320
Cdd:cd11317 223 LLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYFSDSDQGPPSDGSGNTLSVTIN 301

                       330       340
                ....*....|....*....|....*...
gi 27530578 321 SDNSCSGGWVCEHRWRQIYNMVAFRNAV 348
Cdd:cd11317 302 DDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 3-348 1.05e-44

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: 156.67  E-value: 1.05e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   3 GFAGVQVSPVNENA--VKDSRPWWERYQPISYKLVTRS-GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGgtygtggs 79
Cdd:cd11315  26 GYTAIQTSPPQKSKegGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYGIKIIVDVVFNHMANEG-------- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  80 tASPSSKSYPGV---PYSSLDFNPTCAINNYNDANQVRNCELVGLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAK 156
Cdd:cd11315  98 -SAIEDLWYPSAdieLFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQQQKAYLKALVALGVDGFRFDAAK 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 157 HM-WPADLGVIYGRLKN-LNTDHGFASgskaYIVQEVIDMGGEAISK-SEYTGLGAITefrhSDSIGKAFRGKDQLQYLT 233
Cdd:cd11315 177 HIeLPDEPSKASDFWTNiLNNLDKDGL----FIYGEVLQDGGSRDSDyASYLSLGGVT----ASAYGFPLRGALKNAFLF 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 234 N---WGTAWGFAASDRSLV-FVDNHDNQrghgAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVmssfsFSDtdqgpPTT 309
Cdd:cd11315 249 GgslDPASYGQALPSDRAVtWVESHDTY----NNDGFESTGLDDEDERLAWAYLAARDGGTPLF-----FSR-----PNG 314

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 27530578 310 DGhniaspsfnSDNSCSGGwvcehRWRQIYN------MVAFRNAV 348
Cdd:cd11315 315 SG---------GTNPQIGD-----RGDDAWKspdvvaVNKFHNAM 345
Aamy smart00642
Alpha-amylase domain;
1-70 3.75e-20

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 86.23  E-value: 3.75e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27530578      1 PNGFAGVQVSPVNENAVkdSRPWWERYQPISYKLV-TRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAAD 70
Cdd:smart00642  30 DLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKQIdPRFGTMEDFKELVDAAHARGIKVILDVVINHTSDG 98
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 3-258 4.23e-19

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


Pssm-ID: 200458 [Multi-domain]  Cd Length: 375  Bit Score: 87.24  E-value: 4.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   3 GFAGVQVSPVNENaVKDSRPWWERY-----QPIsYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTG 77
Cdd:cd11319  56 GFDAIWISPIVKN-IEGNTAYGEAYhgywaQDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVD 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  78 GSTASP-SSKSYpgvpyssldFNPTCAINNYNDANQVRNCEL----VGLRDLNQGNSYVQDKIVEFLDHLI-DLGVAGFR 151
Cdd:cd11319 134 YSSFVPfNDSSY---------YHPYCWITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLR 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 152 VDAAKHM----WPadlgviygrlknlntdhGFASGSKAYIVQEVIDmgGEAISKSEYTG-LGAITEFRHSDSIGKAF-RG 225
Cdd:cd11319 205 IDTAKHVrkdfWP-----------------GFVEAAGVFAIGEVFD--GDPNYVCPYQNyLDGVLNYPLYYPLVDAFqST 265

                       250       260       270
                ....*....|....*....|....*....|....*
gi 27530578 226 KDQLQYLTNWGTAWGFAASDRSLV--FVDNHDNQR 258
Cdd:cd11319 266 KGSMSALVDTINSVQSSCKDPTLLgtFLENHDNPR 300
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 3-291 9.16e-17

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


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 79.14  E-value: 9.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   3 GFAGVQVSPVNENaVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHmaadggtygtggstas 82
Cdd:cd00551  38 GVTAIWLTPIFES-PEYDGYDKDDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH---------------- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  83 pssksypgvpyssldfnptcainnyndanqvrncelvglrdlnqgnsyvqdkivEFLDHLIDLGVAGFRVDAAKHMWPAD 162
Cdd:cd00551 101 ------------------------------------------------------DILRFWLDEGVDGFRLDAAKHVPKPE 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 163 LGVIYGRLKNLNTDHgfasGSKAYIVQEVIDMGGEAISKSEYT-GLGAITEFRHSDSIGKAFRGKDQLQYLTNWGTaWGF 241
Cdd:cd00551 127 PVEFLREIRKDAKLA----KPDTLLLGEAWGGPDELLAKAGFDdGLDSVFDFPLLEALRDALKGGEGALAILAALL-LLN 201

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 27530578 242 AASDRSLVFVDNHDNQRghgagGADVLTYKVP----KQYKMASAFMLAHPfGTP 291
Cdd:cd00551 202 PEGALLVNFLGNHDTFR-----LADLVSYKIVelrkARLKLALALLLTLP-GTP 249
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
39-291 1.25e-16

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 80.29  E-value: 1.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  39 GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADggtygtggstaSP---SSKSYPGVPYSS----LDFNPTCAINNYNDAN 111
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDE-----------HPwfqEARAGPDSPYRDwyvwRDGKPDLPPNNWFSIF 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 112 QVRNCELVGLR-------------DLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMW-----PADLGVIYGRLKNL 173
Cdd:COG0366 145 GGSAWTWDPEDgqyylhlffssqpDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLREL 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 174 NtDHGFASGSKAYIVQEVIDMGGEAISKseYTG---LGAITEFRHSDSIGKAFRGKD---------QLQYLTNWGTAWgf 241
Cdd:COG0366 225 R-AAVDEYYPDFFLVGEAWVDPPEDVAR--YFGgdeLDMAFNFPLMPALWDALAPEDaaelrdalaQTPALYPEGGWW-- 299

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27530578 242 aasdrsLVFVDNHDNQR-GHGAGGADVLtykvpKQYKMASAFMLAHPfGTP 291
Cdd:COG0366 300 ------ANFLRNHDQPRlASRLGGDYDR-----RRAKLAAALLLTLP-GTP 338
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 103-320 5.52e-14

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


Pssm-ID: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 72.32  E-value: 5.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 103 AINNYNDANQVRNCELVGLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWPADLGVIYGRL---KNLNTDHGF 179
Cdd:cd11320 163 GIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIyskKPVFTFGEW 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 180 ASGSKAyivqeviDMGGEAISKSEYTGLGAItEFRHSDSIGKAFRG-----KDQLQYLTNwgTAWGFAASDRSLVFVDNH 254
Cdd:cd11320 243 FLGSPD-------PGYEDYVKFANNSGMSLL-DFPLNQAIRDVFAGftatmYDLDAMLQQ--TSSDYNYENDLVTFIDNH 312

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27530578 255 DNQRGHGAGGADvltykvpKQYKMASAFMLAHPfGTPRVmssfsFSDTDQ--GPPTTDGHNIAS----PSFN 320
Cdd:cd11320 313 DMPRFLTLNNND-------KRLHQALAFLLTSR-GIPVI-----YYGTEQylHGGTQVGGDPYNrpmmPSFD 371
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 3-291 1.27e-12

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 67.77  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578     3 GFAGVQVSPVNENAVKDSRPWWERYqpisYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTAS 82
Cdd:pfam00128  17 GVTAIWLSPIFDSPQADHGYDIADY----YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSSKD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578    83 PSSKSY----PGVPYSSldfnPTCAINnYNDANQVRNCE----------LVGLRDLNQGNSYVQDKIVEFLDHLIDLGVA 148
Cdd:pfam00128  93 NPYRDYyfwrPGGGPIP----PNNWRS-YFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGID 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   149 GFRVDAAKHM--WPADLGVIYG-RLKNLNTDHG--FASGSKAYIVQEV-IDMGGEAISKSE--YTGLGAITEFRHSDsIG 220
Cdd:pfam00128 168 GFRIDVVKHIskVPGLPFENNGpFWHEFTQAMNetVFGYKDVMTVGEVfHGDGEWARVYTTeaRMELEMGFNFPHND-VA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   221 KAFRGKDQLQ---------YLTNWGTAWGFAASdRSLVFVDNHDNQRGHGAGGADVltykvpKQYKMASAFMLAHPfGTP 291
Cdd:pfam00128 247 LKPFIKWDLApisarklkeMITDWLDALPDTNG-WNFTFLGNHDQPRFLSRFGDDR------ASAKLLAVFLLTLR-GTP 318
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 123-258 2.46e-10

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


Pssm-ID: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 61.12  E-value: 2.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 123 DLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDHGFasgskaYIVQEVIDMGGEAISK- 201
Cdd:cd11339 126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPDF------FMFGEVYDGDPSYIAPy 199

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27530578 202 SEYTGLGAITEFRHSDSIGKAFRGKDQLQYLTNW-GTAWGFAASDRSLVFVDNHDNQR 258
Cdd:cd11339 200 TTTAGGDSVLDFPLYGAIRDAFAGGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGR 257
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 39-291 2.62e-10

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: 61.06  E-value: 2.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  39 GNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGgtygtggstasP---SSKSYPGVPYSSL----DFNPTCA----INNY 107
Cdd:cd11316  67 GTMEDFERLIAEAHKRGIKVIIDLVINHTSSEH-----------PwfqEAASSPDSPYRDYyiwaDDDPGGWsswgGNVW 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 108 NDANQVRNCELV---GLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWPaDLGVIYGRLKNLN-----TDHGF 179
Cdd:cd11316 136 HKAGDGGYYYGAfwsGMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYE-NGEGQADQEENIEfwkefRDYVK 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 180 ASGSKAYIVQEVIDmGGEAISKSEYTGLGAITEFRHSDSIG----KAFRGKDQLQYLTNW-GTAWGFAASDRSLVFVDNH 254
Cdd:cd11316 215 SVKPDAYLVGEVWD-DPSTIAPYYASGLDSAFNFDLAEAIIdsvkNGGSGAGLAKALLRVyELYAKYNPDYIDAPFLSNH 293

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 27530578 255 DNQRGHGAGGADvltykvPKQYKMASAFMLAHPfGTP 291
Cdd:cd11316 294 DQDRVASQLGGD------EAKAKLAAALLLTLP-GNP 323
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 32-291 2.76e-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: 51.45  E-value: 2.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  32 YKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAAdggtygtggstaspssksypgvPYSSLDFNptcainnyndan 111
Cdd:cd11314  57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSG----------------------PDTGEDFG------------ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 112 qvrncelvGLRDLNQGNSYVQDKIVEFLDHLI-DLGVAGFRVDAAKHMWPAdlgviYGRLKNLNTDHGFASG----SKAY 186
Cdd:cd11314 103 --------GAPDLDHTNPEVQNDLKAWLNWLKnDIGFDGWRFDFVKGYAPS-----YVKEYNEATSPSFSVGeywdGLSY 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 187 IVQE--------VIDMGGEAISKSEYTGLGAItefrHSDSIGKAFRGKDQLQY--LTNWGtAWGFaasdRSLVFVDNHDN 256
Cdd:cd11314 170 ENQDahrqrlvdWIDATGGGSAAFDFTTKYIL----QEAVNNNEYWRLRDGQGkpPGLIG-WWPQ----KAVTFVDNHDT 240

                       250       260       270
                ....*....|....*....|....*....|....*
gi 27530578 257 qrGHGAGGADVLTYKVPkqykMASAFMLAHPfGTP 291
Cdd:cd11314 241 --GSTQGHWPFPTDNVL----QGYAYILTHP-GTP 268
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 32-258 1.69e-05

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: 46.17  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  32 YKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMaadggtygtggstaspsSKSYPGVPYSSLDFNPTCAINNYNDAN 111
Cdd:cd11354  67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV-----------------GRSHPAVAQALEDGPGSEEDRWHGHAG 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578 112 QVRNCELVG---LRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDhgfasgskAYIV 188
Cdd:cd11354 130 GGTPAVFEGhedLVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPPEFWARVLPRVRERHPD--------AWIL 201

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27530578 189 QEVIDmgGEAISKSEYTGLGAITEFRHSDSIGKAFRGKDQlqyltnWGTAW------GFAASDRSLVFVDNHDNQR 258
Cdd:cd11354 202 GEVIH--GDYAGIVAASGMDSVTQYELWKAIWSSIKDRNF------FELDWalgrhnEFLDSFVPQTFVGNHDVTR 269
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 123-158 4.04e-05

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: 45.25  E-value: 4.04e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 27530578 123 DLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHM 158
Cdd:cd11334 166 DLNFDNPAVREEILRIMDFWLDLGVDGFRLDAVPYL 201
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 31-157 5.21e-05

Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200468 [Multi-domain]  Cd Length: 477  Bit Score: 45.06  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  31 SYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASPSSKSY----PGVPYssldfnptcAINN 106
Cdd:cd11329 104 ETYLNNSYGVESDLKELVKTAKQKDIKVILDLTPNHSSKQHPLFKDSVLKEPPYRSAFvwadGKGHT---------PPNN 174

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27530578 107 YNDANQVRNCELVGLR------------DLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKH 157
Cdd:cd11329 175 WLSVTGGSAWKWVEDRqyylhqfgpdqpDLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY 237
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
 123-162 2.21e-04

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


Pssm-ID: 200494 [Multi-domain]  Cd Length: 456  Bit Score: 42.73  E-value: 2.21e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27530578 123 DLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHMWPAD 162
Cdd:cd11359 168 DLNFRNPDVQQEMDDVLRFWLDKGVDGFRVDAVKHLLEAT 207
PLN00196 PLN00196
alpha-amylase; Provisional
 36-167 2.30e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 39.52  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   36 TRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASpssksyPGVPYSSLDFNPTCAINN---YND--A 110
Cdd:PLN00196  86 SKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFE------GGTPDSRLDWGPHMICRDdtqYSDgtG 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 27530578  111 NQVRNCELVGLRDLNQGNSYVQDKIVEFLDHL-IDLGVAGFRVDAAKHmWPADLGVIY 167
Cdd:PLN00196 160 NLDTGADFAAAPDIDHLNKRVQRELIGWLLWLkSDIGFDAWRLDFAKG-YSAEVAKVY 216
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 3-197 2.61e-03

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


Pssm-ID: 200488 [Multi-domain]  Cd Length: 390  Bit Score: 39.56  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578   3 GFAGVQVSPVNENAVKDSrpwWErYQPISYKLVTRS-GNEEQFASMTRRCNAVGVRIYVDVIFNHmaadggtygtggstA 81
Cdd:cd11350  46 GVNAIELMPVQEFPGNDS---WG-YNPRHYFALDKAyGTPEDLKRLVDECHQRGIAVILDVVYNH--------------A 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27530578  82 SPSSksypgvPYSSLDFNPTC--AINNYNDANQVRNCELVGLRDLNQGNSYVQDKIVEFLDHLID-LGVAGFRVDAAKHM 158
Cdd:cd11350 108 EGQS------PLARLYWDYWYnpPPADPPWFNVWGPHFYYVGYDFNHESPPTRDFVDDVNRYWLEeYHIDGFRFDLTKGF 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27530578 159 WPADLGV------IYGRLKNLN--TDHGFASGSKAYIVQEVIDMGGE 197
Cdd:cd11350 182 TQKPTGGgawggyDAARIDFLKryADEAKAVDKDFYVIAEHLPDNPE 228
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
 119-158 3.01e-03

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


Pssm-ID: 200467 [Multi-domain]  Cd Length: 470  Bit Score: 39.52  E-value: 3.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27530578 119 VGLRDLNQGNSYVQDKIVEFLDHLIDLGVAGFRVDAAKHM 158
Cdd:cd11328 168 VKQPDLNYRNPKVVEEMKNVLRFWLDKGVDGFRIDAVPHL 207
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH