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Conserved domains on  [gi|1040667097|ref|XP_017207095|]
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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

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 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 1040667097  25 RTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLtkPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNV 104
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 105 GVNIYADAVINHMCGasggegthsscgtyfnaknedfpsvpysswdfndnkcktanedienysDIFQVRDCRLVSLLDLA 184
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 185 LEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfSPGTKPFIYQEVIDLGGEPIKASEYVS 264
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 265 LGRVTEFKYSAKLGTVIRKWEKEKlcYLKNWGEGWGFMPSHKALVFVDNHDNQRGHGAGGaSVLTFWDSRLYKIATGLML 344
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040667097 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 1040667097  424 NWWDNNNNQIAFSRGSKGFIVINNDDWDLNVTLKTGLPSGTYCDIISGdksgnSCTGKQVTVDSDGQATFSICHTEEdpf 503
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 1040667097  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 1040667097  25 RTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLtkPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNV 104
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 105 GVNIYADAVINHMCGasggegthsscgtyfnaknedfpsvpysswdfndnkcktanedienysDIFQVRDCRLVSLLDLA 184
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 185 LEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfSPGTKPFIYQEVIDLGGEPIKASEYVS 264
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 265 LGRVTEFKYSAKLGTVIRKWEKEKlcYLKNWGEGWGFMPSHKALVFVDNHDNQRGHGAGGaSVLTFWDSRLYKIATGLML 344
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040667097 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 1040667097  424 NWWDNNNNQIAFSRGSKGFIVINNDDWDLNVTLKTGLPSGTYCDIISGdksgnSCTGKQVTVDSDGQATFSICHTEEdpf 503
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 1040667097  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 1040667097   28 IVHLFEWR-------WADIAKECErYLAPNGYGGVQISPPSESIVLtkpwHPWWQRYQPISYNLC-SRSGTEEELKDMIA 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|
gi 1040667097  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 1040667097 424 NWWDNNNNQIAFSRGS---KGFIVINNDDWDLNVTLKTGLP-SGTYCDIISGDKS--GNSCTGKQVTVDSDGQATFSICH 497
Cdd:pfam02806   3 DGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLTLT 82

                          90
                  ....*....|..
gi 1040667097 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 1040667097  89 GTEEELKDMIARCNNVGVNIYADAVINHmcgaSGGE---------GTHSSCGTYFNAKNEDFPSVP--------YSSWDF 151
Cdd:COG0366    76 GTLADFDELVAEAHARGIKVILDLVLNH----TSDEhpwfqearaGPDSPYRDWYVWRDGKPDLPPnnwfsifgGSAWTW 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 152 NDnkcktanEDIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMW-----PGDLSNVY 226
Cdd:COG0366   152 DP-------EDGQYYLHLF------FSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVH 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 227 SRLKTLNTTWFSPGTKPFIYQEVIdlGGEPIKASEYVSLGR---VTEFKYSAKLGTVIRKWEKEKLCY-LKNWGEGwgfM 302
Cdd:COG0366   219 EFLRELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELRDaLAQTPAL---Y 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040667097 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 1040667097  32 FEW------RWADIAKECERYLAPNGYGGVQISPPSESIvltKPwhpwwQRYQPIS-YNLCSRSGTEEELKDMIARCNNV 104
Cdd:PLN02784  509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDELKDLVKSFHEV 580

                          90
                  ....*....|....
gi 1040667097 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 1040667097  89 GTEEELKDMIARCNNVGVNIYADAVINHMC--------GASGGEGTHSSCGTYFNAKNEDFPS-----VPYSSWDFNDNK 155
Cdd:pfam00128  49 GTMEDFKELISKAHERGIKVILDLVVNHTSdehawfqeSRSSKDNPYRDYYFWRPGGGPIPPNnwrsyFGGSAWTYDEKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 156 cktanedIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSR------- 228
Cdd:pfam00128 129 -------QEYYLHLF------VAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgpfwhef 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 229 LKTLNTTWFSpGTKPFIYQEVIDLGGEPIKAS---EYVSLGRVTEFK-YSAKLGTVIR-KWEKEKLCYLKNWGEGW-GFM 302
Cdd:pfam00128 196 TQAMNETVFG-YKDVMTVGEVFHGDGEWARVYtteARMELEMGFNFPhNDVALKPFIKwDLAPISARKLKEMITDWlDAL 274

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1040667097 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 1040667097  25 RTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLtkPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNV 104
Cdd:cd11317     1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 105 GVNIYADAVINHMCGasggegthsscgtyfnaknedfpsvpysswdfndnkcktanedienysDIFQVRDCRLVSLLDLA 184
Cdd:cd11317    79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 185 LEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfSPGTKPFIYQEVIDLGGEPIKASEYVS 264
Cdd:cd11317   111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 265 LGRVTEFKYSAKLGTVIRKWEKEKlcYLKNWGEGWGFMPSHKALVFVDNHDNQRGHGAGGaSVLTFWDSRLYKIATGLML 344
Cdd:cd11317   189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040667097 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 1040667097  28 IVHLFEWRWADIAKECERyLAPNGYGGVQISPPSESIVLTKPWHPWWQRYQPISYNLC-SRSGTEEELKDMIARCNNVGV 106
Cdd:cd11315     4 ILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGnNQLGTEDDFKALCAAAHKYGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 107 NIYADAVINHMcgasggegthsscGTYFNAKNEDFPSVPY----SSWDFNDNKCktanedIENYSDIFQVRDCRLVSLLD 182
Cdd:cd11315    83 KIIVDVVFNHM-------------ANEGSAIEDLWYPSADielfSPEDFHGNGG------ISNWNDRWQVTQGRLGGLPD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 183 LALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMwpgDLSNVYSRLKTLNTTWFSPGTKP--FIYQEVIDLGGEPIKA- 259
Cdd:cd11315   144 LNTENPAVQQQQKAYLKALVALGVDGFRFDAAKHI---ELPDEPSKASDFWTNILNNLDKDglFIYGEVLQDGGSRDSDy 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 260 SEYVSLGRVTEFKY-SAKLGTVIRKWEKEKLCYLKNWGEGwgfMPSHKALVFVDNHDNQrgHGAGGASV-LTFWDSRLyk 337
Cdd:cd11315   221 ASYLSLGGVTASAYgFPLRGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY--NNDGFESTgLDDEDERL-- 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 338 iATGLMLAHPYGVTAVmssyrWDRHfVNGKDQNDWMGPPSNADGStksvpiNPDstcgdnwicehrwrqIRNMVIFRNVV 417
Cdd:cd11315   294 -AWAYLAARDGGTPLF-----FSRP-NGSGGTNPQIGDRGDDAWK------SPD---------------VVAVNKFHNAM 345


                  ....
gi 1040667097 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 1040667097  424 NWWDNNNNQIAFSRGSKGFIVINNDDWDLNVTLKTGLPSGTYCDIISGdksgnSCTGKQVTVDSDGQATFSICHTEEdpf 503
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISG-----LCTGKSVTVGSNGIATFTLPAGGA--- 73


                   ....*...
gi 1040667097  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 1040667097   28 IVHLFEWR-------WADIAKECErYLAPNGYGGVQISPPSESIVLtkpwHPWWQRYQPISYNLC-SRSGTEEELKDMIA 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|
gi 1040667097  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 1040667097 424 NWWDNNNNQIAFSRGS---KGFIVINNDDWDLNVTLKTGLP-SGTYCDIISGDKS--GNSCTGKQVTVDSDGQATFSICH 497
Cdd:pfam02806   3 DGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLTLT 82

                          90
                  ....*....|..
gi 1040667097 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 1040667097  55 VQISPPSESIVLTKPW----HPWWQryQPIsYNLCSRSGTEEELKDMIARCNNVGVNIYADAVINHMcgASGGEGThssc 130
Cdd:cd11319    60 IWISPIVKNIEGNTAYgeayHGYWA--QDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM--ASAGPGS---- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 131 gtyfnaknedfpSVPYSSWD-FNDNK-----CktaneDIENYSDIFQVRDCRL----VSLLDLALEKDYVRGKVAEYMNK 200
Cdd:cd11319   131 ------------DVDYSSFVpFNDSSyyhpyC-----WITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKN 193

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1040667097 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 1040667097  46 YLAPNGYGGVQISPPSESI------VLTKPWHPWWQR--YQPISYnlcsrSGTEEELKDMIARCNNVGVNIYADAVINHM 117
Cdd:cd11320    55 YLKDLGVTAIWISPPVENInspiegGGNTGYHGYWARdfKRTNEH-----FGTWEDFDELVDAAHANGIKVIIDFVPNHS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 118 CGASGGE-GTHSSCGTYFNAknedfpsvpyssWDFNDNKCKTANEDIENYSDIFQVRDCRLVSLLDLALEKDYVRGKVAE 196
Cdd:cd11320   130 SPADYAEdGALYDNGTLVGD------------YPNDDNGWFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 197 YMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTwfspgtkpFIYQEVIDLGGEPiKASEYVS------------ 264
Cdd:cd11320   198 AIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKPV--------FTFGEWFLGSPDP-GYEDYVKfannsgmslldf 268

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040667097 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 1040667097  45 RYLAPNGYGGVQISPPSESIvltkPWHPWWQRYQPISY-NLCSRSGTEEELKDMIARCNNVGVNIYADAVINHmcgasgg 123
Cdd:cd00551    32 DYLKDLGVTAIWLTPIFESP----EYDGYDKDDGYLDYyEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 124 egthsscgtyfnaknedfpsvpysswdfndnkcktanedienysdifqvrdcrlvslldlalekdyvrgkvaEYMNKLID 203
Cdd:cd00551   101 ------------------------------------------------------------------------DILRFWLD 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 204 IGVAGFRVDACKHMWPGDLSNVYSRLKTLNTTWfspGTKPFIYQEVIDlGGEPIKASEYVSLGRVTEFKYSakLGTVIRK 283
Cdd:cd00551   109 EGVDGFRLDAAKHVPKPEPVEFLREIRKDAKLA---KPDTLLLGEAWG-GPDELLAKAGFDDGLDSVFDFP--LLEALRD 182

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040667097 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 1040667097  89 GTEEELKDMIARCNNVGVNIYADAVINHmcgaSGGE---------GTHSSCGTYFNAKNEDFPSVP--------YSSWDF 151
Cdd:COG0366    76 GTLADFDELVAEAHARGIKVILDLVLNH----TSDEhpwfqearaGPDSPYRDWYVWRDGKPDLPPnnwfsifgGSAWTW 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 152 NDnkcktanEDIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMW-----PGDLSNVY 226
Cdd:COG0366   152 DP-------EDGQYYLHLF------FSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVH 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 227 SRLKTLNTTWFSPGTKPFIYQEVIdlGGEPIKASEYVSLGR---VTEFKYSAKLGTVIRKWEKEKLCY-LKNWGEGwgfM 302
Cdd:COG0366   219 EFLRELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELRDaLAQTPAL---Y 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040667097 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 1040667097  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 1040667097  32 FEW------RWADIAKECERYLAPNGYGGVQISPPSESIvltKPwhpwwQRYQPIS-YNLCSRSGTEEELKDMIARCNNV 104
Cdd:PLN02784  509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDELKDLVKSFHEV 580

                          90
                  ....*....|....
gi 1040667097 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 1040667097  89 GTEEELKDMIARCNNVGVNIYADAVINHMCGA----------------------------------SGGEGTHSScgtyF 134
Cdd:PRK09441   78 GTKEELLNAIDALHENGIKVYADVVLNHKAGAdeketfrvvevdpddrtqiisepyeiegwtrftfPGRGGKYSD----F 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 135 NAKNEDFPSVPYSSWD------FNDNKCKTANEDIENYSDIFQVRDCrlvslLDLALEKDYVRGKVAEYMNKLID-IGVA 207
Cdd:PRK09441  154 KWHWYHFSGTDYDENPdesgifKIVGDGKGWDDQVDDENGNFDYLMG-----ADIDFRHPEVREELKYWAKWYMEtTGFD 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 208 GFRVDACKHMwpgdlsnvysrlktlnTTWFspgTKPFIyQEVIDLGGEPIKAseyvslgrVTEFkYSAKLGTvirkweke 287
Cdd:PRK09441  229 GFRLDAVKHI----------------DAWF---IKEWI-EHVREVAGKDLFI--------VGEY-WSHDVDK-------- 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 288 klcyLKNWGE--GWGFM----PSH-----------------------------KALVFVDNHDNQRghgagGASVLTFWD 332
Cdd:PRK09441  272 ----LQDYLEqvEGKTDlfdvPLHynfheaskqgrdydmrnifdgtlveadpfHAVTFVDNHDTQP-----GQALESPVE 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 333 SRLYKIATGLMLAHPYGVTAVMssYRwdrhfvngkdqnDWMGPPsnadgstksvpinpdstcGDNWICEHRWrQIRNMVI 412
Cdd:PRK09441  343 PWFKPLAYALILLREEGYPCVF--YG------------DYYGAS------------------GYYIDMPFKE-KLDKLLL 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 413 FRNVVNGQPLSNWWDnNNNQIAFSR----GSKGFIVI--NNDDWDLNVTLKTGLPSGTYCDIisgdkSGNSctGKQVTVD 486
Cdd:PRK09441  390 ARKNFAYGEQTDYFD-HPNCIGWTRsgdeENPGLAVVisNGDAGEKTMEVGENYAGKTWRDY-----TGNR--QETVTID 461


                  ....*....
gi 1040667097 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 1040667097  89 GTEEELKDMIARCNNVGVNIYADAVINHMC--------GASGGEGTHSSCGTYFNAKNEDFPS-----VPYSSWDFNDNK 155
Cdd:pfam00128  49 GTMEDFKELISKAHERGIKVILDLVVNHTSdehawfqeSRSSKDNPYRDYYFWRPGGGPIPPNnwrsyFGGSAWTYDEKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 156 cktanedIENYSDIFqvrdcrLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSR------- 228
Cdd:pfam00128 129 -------QEYYLHLF------VAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgpfwhef 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040667097 229 LKTLNTTWFSpGTKPFIYQEVIDLGGEPIKAS---EYVSLGRVTEFK-YSAKLGTVIR-KWEKEKLCYLKNWGEGW-GFM 302
Cdd:pfam00128 196 TQAMNETVFG-YKDVMTVGEVFHGDGEWARVYtteARMELEMGFNFPhNDVALKPFIKwDLAPISARKLKEMITDWlDAL 274

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1040667097 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 1040667097  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 1040667097  82 YNLCSRSGTEEELKDMIARCNNVGVNIYADAVINHMcgasggeGTHSScgtYFNAKNEDFPSVPYSSWDFNDnkCKTANE 161
Cdd:cd11354    67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV-------GRSHP---AVAQALEDGPGSEEDRWHGHA--GGGTPA 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1040667097 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 1040667097  22 KHNRTSIVHLFEWR-----WADIAKECERYLAPNGYGGVQISPPSESIvltKPwhpwwQRYQPIS-YNLCSRSGTEEELK 95
Cdd:PLN02361    8 RNGREILLQAFNWEshkhdWWRNLEGKVPDLAKSGFTSAWLPPPSQSL---AP-----EGYLPQNlYSLNSAYGSEHLLK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1040667097  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 1040667097 194 VAEYM----NKLIDIGVAGFRVDACKHMWPGDLSNVYSRlktlnttWFSPGTKP--FIYQEVIDlgGEPIKASEYV---S 264
Cdd:cd11339   134 VVDYLidayKWWIDTGVDGFRIDTVKHVPREFWQEFAPA-------IRQAAGKPdfFMFGEVYD--GDPSYIAPYTttaG 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1040667097 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 1040667097  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.
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