NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528506861|ref|XP_005158947|]
View 

amyAc_bac_euk_AmyA and Aamy_C domain-containing protein isoform X2 [Danio rerio]

Protein Classification

alpha-amylase( domain architecture ID 10183021)

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

CATH:  3.20.20.80|2.60.40.1180
CAZY:  GH13
EC:  3.2.1.1
Gene Ontology:  GO:0004556|GO:0005975
PubMed:  21544166|17085431|11257505
SCOP:  4003138|4002636

Graphical summary

 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, ...
 25-417 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: 564.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  25 RTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLtkPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 105 GVNIYADAVINHMCGasggegthsscgtyfnaknedfpsvpysswdfndnkcktanedienysDIFQVRDCRLVSLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 185 LEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfSPGTKPFIYQEVIDLGGEPIKASEYVS 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 265 LGRVTEFKYSAKLGTVIRKWEKEKlcYLKNWGEGWGFMPSHKALVFVDNHDNQRGHGAGGaSVLTFWDSRLYKIATGLML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528506861 345 AHPYGVTAVMSSYRWDrhfvngkdqNDWMGPPSNADGSTKSVPINPDSTCGDNWICEHRWRQIRNMVIFRNVV 417
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
424-511 6.51e-34

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 122.73  E-value: 6.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861   424 NWWDNNNNQIAFSRGSKGFIVINNDDWDLNVTLKTGLPSGTYCDIISGdksgnSCTGKQVTVDSDGQATFSICHTEEdpf 503
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 528506861   504 MAIHADSK 511
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, ...
 25-417 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: 564.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  25 RTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLtkPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 105 GVNIYADAVINHMCGasggegthsscgtyfnaknedfpsvpysswdfndnkcktanedienysDIFQVRDCRLVSLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 185 LEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfSPGTKPFIYQEVIDLGGEPIKASEYVS 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 265 LGRVTEFKYSAKLGTVIRKWEKEKlcYLKNWGEGWGFMPSHKALVFVDNHDNQRGHGAGGaSVLTFWDSRLYKIATGLML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528506861 345 AHPYGVTAVMSSYRWDrhfvngkdqNDWMGPPSNADGSTKSVPINPDSTCGDNWICEHRWRQIRNMVIFRNVV 417
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
424-511 6.51e-34

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 122.73  E-value: 6.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861   424 NWWDNNNNQIAFSRGSKGFIVINNDDWDLNVTLKTGLPSGTYCDIISGdksgnSCTGKQVTVDSDGQATFSICHTEEdpf 503
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 528506861   504 MAIHADSK 511
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-119 1.58e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.49  E-value: 1.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861    28 IVHLFEWR-------WADIAKECErYLAPNGYGGVQISPPSESIVLtkpwHPWWQRYQPISYNLC-SRSGTEEELKDMIA 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|
gi 528506861   100 RCNNVGVNIYADAVINHMCG 119
Cdd:smart00642  78 AAHARGIKVILDVVINHTSD 97
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 424-509 2.43e-19

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 82.77  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  424 NWWDNNNNQIAFSRGS---KGFIVINNDDWDLNVTLKTGLP-SGTYCDIISGDKS--GNSCTGKQVTVDSDGQATFSICH 497
Cdd:pfam02806   3 DGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLTLT 82

                          90
                  ....*....|..
gi 528506861  498 TEEDPFMAIHAD 509
Cdd:pfam02806  83 LPPLSALVLKVE 94
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 1.46e-10

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 62.96  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  89 GTEEELKDMIARCNNVGVNIYADAVINHmcgaSGGE---------GTHSSCGTYFNAKNEDFPSVP--------YSSWDF 151
Cdd:COG0366   76 GTLADFDELVAEAHARGIKVILDLVLNH----TSDEhpwfqearaGPDSPYRDWYVWRDGKPDLPPnnwfsifgGSAWTW 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 152 NDnkcktanEDIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMW-----PGDLSNVY 226
Cdd:COG0366  152 DP-------EDGQYYLHLF------FSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVH 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 227 SRLKTLNTTWFSPGTKPFIYQEVIdlGGEPIKASEYVSLGR---VTEFKYSAKLGTVIRKWEKEKLCY-LKNWGEGwgfM 302
Cdd:COG0366  219 EFLRELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELRDaLAQTPAL---Y 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 528506861 303 PSHKALV-FVDNHDNQRghgaggasVLTFWDS----RLYKIATGLMLAHP 347
Cdd:COG0366  294 PEGGWWAnFLRNHDQPR--------LASRLGGdydrRRAKLAAALLLTLP 335
PLN02784 PLN02784
alpha-amylase
 32-118 3.20e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 56.56  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  32 FEW------RWADIAKECERYLAPNGYGGVQISPPSESIvltKPwhpwwQRYQPIS-YNLCSRSGTEEELKDMIARCNNV 104
Cdd:PLN02784 509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDELKDLVKSFHEV 580

                         90
                 ....*....|....
gi 528506861 105 GVNIYADAVINHMC 118
Cdd:PLN02784 581 GIKVLGDAVLNHRC 594
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 89-344 5.38e-06

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: 48.51  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861   89 GTEEELKDMIARCNNVGVNIYADAVINHMC--------GASGGEGTHSSCGTYFNAKNEDFPS-----VPYSSWDFNDNK 155
Cdd:pfam00128  49 GTMEDFKELISKAHERGIKVILDLVVNHTSdehawfqeSRSSKDNPYRDYYFWRPGGGPIPPNnwrsyFGGSAWTYDEKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  156 cktanedIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSR------- 228
Cdd:pfam00128 129 -------QEYYLHLF------VAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgpfwhef 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  229 LKTLNTTWFSpGTKPFIYQEVIDLGGEPIKAS---EYVSLGRVTEFK-YSAKLGTVIR-KWEKEKLCYLKNWGEGW-GFM 302
Cdd:pfam00128 196 TQAMNETVFG-YKDVMTVGEVFHGDGEWARVYtteARMELEMGFNFPhNDVALKPFIKwDLAPISARKLKEMITDWlDAL 274

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 528506861  303 P--SHKALVFVDNHDNQRghgaggasVLTFW--DSRLYKIATGLML 344
Cdd:pfam00128 275 PdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
 
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, ...
 25-417 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: 564.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  25 RTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLtkPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 105 GVNIYADAVINHMCGasggegthsscgtyfnaknedfpsvpysswdfndnkcktanedienysDIFQVRDCRLVSLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 185 LEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfSPGTKPFIYQEVIDLGGEPIKASEYVS 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 265 LGRVTEFKYSAKLGTVIRKWEKEKlcYLKNWGEGWGFMPSHKALVFVDNHDNQRGHGAGGaSVLTFWDSRLYKIATGLML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528506861 345 AHPYGVTAVMSSYRWDrhfvngkdqNDWMGPPSNADGSTKSVPINPDSTCGDNWICEHRWRQIRNMVIFRNVV 417
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 28-421 3.18e-50

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: 175.54  E-value: 3.18e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  28 IVHLFEWRWADIAKECERyLAPNGYGGVQISPPSESIVLTKPWHPWWQRYQPISYNLC-SRSGTEEELKDMIARCNNVGV 106
Cdd:cd11315    4 ILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGnNQLGTEDDFKALCAAAHKYGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 107 NIYADAVINHMcgasggegthsscGTYFNAKNEDFPSVPY----SSWDFNDNKCktanedIENYSDIFQVRDCRLVSLLD 182
Cdd:cd11315   83 KIIVDVVFNHM-------------ANEGSAIEDLWYPSADielfSPEDFHGNGG------ISNWNDRWQVTQGRLGGLPD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 183 LALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMwpgDLSNVYSRLKTLNTTWFSPGTKP--FIYQEVIDLGGEPIKA- 259
Cdd:cd11315  144 LNTENPAVQQQQKAYLKALVALGVDGFRFDAAKHI---ELPDEPSKASDFWTNILNNLDKDglFIYGEVLQDGGSRDSDy 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 260 SEYVSLGRVTEFKY-SAKLGTVIRKWEKEKLCYLKNWGEGwgfMPSHKALVFVDNHDNQrgHGAGGASV-LTFWDSRLyk 337
Cdd:cd11315  221 ASYLSLGGVTASAYgFPLRGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY--NNDGFESTgLDDEDERL-- 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 338 iATGLMLAHPYGVTAVmssyrWDRHfVNGKDQNDWMGPPSNADGStksvpiNPDstcgdnwicehrwrqIRNMVIFRNVV 417
Cdd:cd11315  294 -AWAYLAARDGGTPLF-----FSRP-NGSGGTNPQIGDRGDDAWK------SPD---------------VVAVNKFHNAM 345


                 ....
gi 528506861 418 NGQP 421
Cdd:cd11315  346 HGQP 349
Aamy_C smart00632
Aamy_C domain;
424-511 6.51e-34

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 122.73  E-value: 6.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861   424 NWWDNNNNQIAFSRGSKGFIVINNDDWDLNVTLKTGLPSGTYCDIISGdksgnSCTGKQVTVDSDGQATFSICHTEEdpf 503
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 528506861   504 MAIHADSK 511
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-119 1.58e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.49  E-value: 1.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861    28 IVHLFEWR-------WADIAKECErYLAPNGYGGVQISPPSESIVLtkpwHPWWQRYQPISYNLC-SRSGTEEELKDMIA 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|
gi 528506861   100 RCNNVGVNIYADAVINHMCG 119
Cdd:smart00642  78 AAHARGIKVILDVVINHTSD 97
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 424-509 2.43e-19

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 82.77  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  424 NWWDNNNNQIAFSRGS---KGFIVINNDDWDLNVTLKTGLP-SGTYCDIISGDKS--GNSCTGKQVTVDSDGQATFSICH 497
Cdd:pfam02806   3 DGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLTLT 82

                          90
                  ....*....|..
gi 528506861  498 TEEDPFMAIHAD 509
Cdd:pfam02806  83 LPPLSALVLKVE 94
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 55-227 8.63e-14

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: 72.98  E-value: 8.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  55 VQISPPSESIVLTKPW----HPWWQryQPIsYNLCSRSGTEEELKDMIARCNNVGVNIYADAVINHMcgASGGEGThssc 130
Cdd:cd11319   60 IWISPIVKNIEGNTAYgeayHGYWA--QDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM--ASAGPGS---- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 131 gtyfnaknedfpSVPYSSWD-FNDNK-----CktaneDIENYSDIFQVRDCRL----VSLLDLALEKDYVRGKVAEYMNK 200
Cdd:cd11319  131 ------------DVDYSSFVpFNDSSyyhpyC-----WITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKN 193

                        170       180       190
                 ....*....|....*....|....*....|....
gi 528506861 201 LI-DIGVAGFRVDACKHM----WPG--DLSNVYS 227
Cdd:cd11319  194 LVsNYSIDGLRIDTAKHVrkdfWPGfvEAAGVFA 227
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 46-318 3.29e-12

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: 68.08  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  46 YLAPNGYGGVQISPPSESI------VLTKPWHPWWQR--YQPISYnlcsrSGTEEELKDMIARCNNVGVNIYADAVINHM 117
Cdd:cd11320   55 YLKDLGVTAIWISPPVENInspiegGGNTGYHGYWARdfKRTNEH-----FGTWEDFDELVDAAHANGIKVIIDFVPNHS 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 118 CGASGGE-GTHSSCGTYFNAknedfpsvpyssWDFNDNKCKTANEDIENYSDIFQVRDCRLVSLLDLALEKDYVRGKVAE 196
Cdd:cd11320  130 SPADYAEdGALYDNGTLVGD------------YPNDDNGWFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 197 YMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfspgtkpFIYQEVIDLGGEPiKASEYVS------------ 264
Cdd:cd11320  198 AIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKPV--------FTFGEWFLGSPDP-GYEDYVKfannsgmslldf 268

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528506861 265 -LGRVTE--FKYS----AKLGTVIRKWEKEklcylknwgegwgFMPSHKALVFVDNHDNQR 318
Cdd:cd11320  269 pLNQAIRdvFAGFtatmYDLDAMLQQTSSD-------------YNYENDLVTFIDNHDMPR 316
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 45-347 1.21e-10

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: 62.19  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  45 RYLAPNGYGGVQISPPSESIvltkPWHPWWQRYQPISY-NLCSRSGTEEELKDMIARCNNVGVNIYADAVINHmcgasgg 123
Cdd:cd00551   32 DYLKDLGVTAIWLTPIFESP----EYDGYDKDDGYLDYyEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 124 egthsscgtyfnaknedfpsvpysswdfndnkcktanedienysdifqvrdcrlvslldlalekdyvrgkvaEYMNKLID 203
Cdd:cd00551  101 ------------------------------------------------------------------------DILRFWLD 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 204 IGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTWfspGTKPFIYQEVIDlGGEPIKASEYVSLGRVTEFKYSakLGTVIRK 283
Cdd:cd00551  109 EGVDGFRLDAAKHVPKPEPVEFLREIRKDAKLA---KPDTLLLGEAWG-GPDELLAKAGFDDGLDSVFDFP--LLEALRD 182

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528506861 284 WEKEKLCYLKNWGEGWGFMPSHKALV-FVDNHDNQRGHGAGGASVLTFwDSRLYKIATGLMLAHP 347
Cdd:cd00551  183 ALKGGEGALAILAALLLLNPEGALLVnFLGNHDTFRLADLVSYKIVEL-RKARLKLALALLLTLP 246
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 1.46e-10

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 62.96  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  89 GTEEELKDMIARCNNVGVNIYADAVINHmcgaSGGE---------GTHSSCGTYFNAKNEDFPSVP--------YSSWDF 151
Cdd:COG0366   76 GTLADFDELVAEAHARGIKVILDLVLNH----TSDEhpwfqearaGPDSPYRDWYVWRDGKPDLPPnnwfsifgGSAWTW 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 152 NDnkcktanEDIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMW-----PGDLSNVY 226
Cdd:COG0366  152 DP-------EDGQYYLHLF------FSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVH 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 227 SRLKTLNTTWFSPGTKPFIYQEVIdlGGEPIKASEYVSLGR---VTEFKYSAKLGTVIRKWEKEKLCY-LKNWGEGwgfM 302
Cdd:COG0366  219 EFLRELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELRDaLAQTPAL---Y 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 528506861 303 PSHKALV-FVDNHDNQRghgaggasVLTFWDS----RLYKIATGLMLAHP 347
Cdd:COG0366  294 PEGGWWAnFLRNHDQPR--------LASRLGGdydrRRAKLAAALLLTLP 335
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 82-124 1.28e-09

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: 59.54  E-value: 1.28e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528506861  82 YNLCSRSGTEEELKDMIARCNNVGVNIYADAVINHMCGASGGE 124
Cdd:cd11314   57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGPDTGE 99
PLN02784 PLN02784
alpha-amylase
 32-118 3.20e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 56.56  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  32 FEW------RWADIAKECERYLAPNGYGGVQISPPSESIvltKPwhpwwQRYQPIS-YNLCSRSGTEEELKDMIARCNNV 104
Cdd:PLN02784 509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDELKDLVKSFHEV 580

                         90
                 ....*....|....
gi 528506861 105 GVNIYADAVINHMC 118
Cdd:PLN02784 581 GIKVLGDAVLNHRC 594
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 89-495 3.44e-06

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 49.50  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  89 GTEEELKDMIARCNNVGVNIYADAVINHMCGA----------------------------------SGGEGTHSScgtyF 134
Cdd:PRK09441  78 GTKEELLNAIDALHENGIKVYADVVLNHKAGAdeketfrvvevdpddrtqiisepyeiegwtrftfPGRGGKYSD----F 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 135 NAKNEDFPSVPYSSWD------FNDNKCKTANEDIENYSDIFQVRDCrlvslLDLALEKDYVRGKVAEYMNKLID-IGVA 207
Cdd:PRK09441 154 KWHWYHFSGTDYDENPdesgifKIVGDGKGWDDQVDDENGNFDYLMG-----ADIDFRHPEVREELKYWAKWYMEtTGFD 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 208 GFRVDACKHMwpgdlsnvysrlktlnTTWFspgTKPFIyQEVIDLGGEPIKAseyvslgrVTEFkYSAKLGTvirkweke 287
Cdd:PRK09441 229 GFRLDAVKHI----------------DAWF---IKEWI-EHVREVAGKDLFI--------VGEY-WSHDVDK-------- 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 288 klcyLKNWGE--GWGFM----PSH-----------------------------KALVFVDNHDNQRghgagGASVLTFWD 332
Cdd:PRK09441 272 ----LQDYLEqvEGKTDlfdvPLHynfheaskqgrdydmrnifdgtlveadpfHAVTFVDNHDTQP-----GQALESPVE 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 333 SRLYKIATGLMLAHPYGVTAVMssYRwdrhfvngkdqnDWMGPPsnadgstksvpinpdstcGDNWICEHRWrQIRNMVI 412
Cdd:PRK09441 343 PWFKPLAYALILLREEGYPCVF--YG------------DYYGAS------------------GYYIDMPFKE-KLDKLLL 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 413 FRNVVNGQPLSNWWDnNNNQIAFSR----GSKGFIVI--NNDDWDLNVTLKTGLPSGTYCDIisgdkSGNSctGKQVTVD 486
Cdd:PRK09441 390 ARKNFAYGEQTDYFD-HPNCIGWTRsgdeENPGLAVVisNGDAGEKTMEVGENYAGKTWRDY-----TGNR--QETVTID 461


                 ....*....
gi 528506861 487 SDGQATFSI 495
Cdd:PRK09441 462 EDGWGTFPV 470
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 89-344 5.38e-06

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: 48.51  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861   89 GTEEELKDMIARCNNVGVNIYADAVINHMC--------GASGGEGTHSSCGTYFNAKNEDFPS-----VPYSSWDFNDNK 155
Cdd:pfam00128  49 GTMEDFKELISKAHERGIKVILDLVVNHTSdehawfqeSRSSKDNPYRDYYFWRPGGGPIPPNnwrsyFGGSAWTYDEKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  156 cktanedIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSR------- 228
Cdd:pfam00128 129 -------QEYYLHLF------VAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgpfwhef 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  229 LKTLNTTWFSpGTKPFIYQEVIDLGGEPIKAS---EYVSLGRVTEFK-YSAKLGTVIR-KWEKEKLCYLKNWGEGW-GFM 302
Cdd:pfam00128 196 TQAMNETVFG-YKDVMTVGEVFHGDGEWARVYtteARMELEMGFNFPhNDVALKPFIKwDLAPISARKLKEMITDWlDAL 274

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 528506861  303 P--SHKALVFVDNHDNQRghgaggasVLTFW--DSRLYKIATGLML 344
Cdd:pfam00128 275 PdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 89-120 3.22e-05

Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 46.36  E-value: 3.22e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 528506861  89 GTEEELKDMIARCNNVGVNIYADAVINHMCGA 120
Cdd:cd11318   76 GTKEELLEAIKALHENGIQVYADAVLNHKAGA 107
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 82-213 4.00e-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: 45.78  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  82 YNLCSRSGTEEELKDMIARCNNVGVNIYADAVINHMcgasggeGTHSScgtYFNAKNEDFPSVPYSSWDFNDnkCKTANE 161
Cdd:cd11354   67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV-------GRSHP---AVAQALEDGPGSEEDRWHGHA--GGGTPA 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528506861 162 DIENYSDifqvrdcrlvsLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDA 213
Cdd:cd11354  135 VFEGHED-----------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDA 175
PLN02361 PLN02361
alpha-amylase
 22-125 1.94e-04

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 43.65  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861  22 KHNRTSIVHLFEWR-----WADIAKECERYLAPNGYGGVQISPPSESIvltKPwhpwwQRYQPIS-YNLCSRSGTEEELK 95
Cdd:PLN02361   8 RNGREILLQAFNWEshkhdWWRNLEGKVPDLAKSGFTSAWLPPPSQSL---AP-----EGYLPQNlYSLNSAYGSEHLLK 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 528506861  96 DMIARCNNVGVNIYADAVINHMCGASGGEG 125
Cdd:PLN02361  80 SLLRKMKQYNVRAMADIVINHRVGTTQGHG 109
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 194-318 2.88e-04

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: 43.01  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528506861 194 VAEYM----NKLIDIGVAGFRVDACKHMWPGDLSNVYSRlktlnttWFSPGTKP--FIYQEVIDlgGEPIKASEYV---S 264
Cdd:cd11339  134 VVDYLidayKWWIDTGVDGFRIDTVKHVPREFWQEFAPA-------IRQAAGKPdfFMFGEVYD--GDPSYIAPYTttaG 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528506861 265 LGRVTEFKYSAKLGTVIRKWEKEKLcyLKNW-GEGWGFMPSHKALVFVDNHDNQR 318
Cdd:cd11339  205 GDSVLDFPLYGAIRDAFAGGGSGDL--LQDLfLSDDLYNDATELVTFLDNHDMGR 257
PLN00196 PLN00196
alpha-amylase; Provisional
 47-118 3.39e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 39.90  E-value: 3.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528506861  47 LAPNGYGGVQISPPSESIVLtkpwhpwwQRYQPIS-YNL-CSRSGTEEELKDMIARCNNVGVNIYADAVINHMC 118
Cdd:PLN00196  53 IAAAGITHVWLPPPSHSVSE--------QGYMPGRlYDLdASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRT 118
 
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