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Conserved domains on  [gi|6322241|ref|NP_012314|]
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oligo-1,6-glucosidase IMA4 [Saccharomyces cerevisiae S288C]

Protein Classification

glycoside hydrolase family 13 protein( domain architecture ID 10877748)

glycoside hydrolase family 13 protein similar to alpha-glucosidase that catalyzes the hydrolysis of terminal, non-reducing, alpha-glucosidic linkages of oligosaccharides to produce alpha-glucose, as well as oligo-1,6-glucosidase that catalyzes hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
16-503 0e+00

Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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: 200472 [Multi-domain]  Cd Length: 428  Bit Score: 616.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   16 KEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIE 95
Cdd:cd11333   1 KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFGTMEDFDELIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   96 KTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKgydaegKPIPPNNWRSYFGGSAWTFDEKTQEFYL 175
Cdd:cd11333  81 EAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGK------DGKPPNNWRSFFGGSAWEYDPETGQYYL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  176 RLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwQLSDPFTMNGPRIHEFH 255
Cdd:cd11333 155 HLFAKEQPDLNWENPEVRQEIYD-MMRFWLDKGVDGFRLDVINLISKDPDFPDAPPGDGDG--LSGHKYYANGPGVHEYL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  256 QEMNKfirnRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAELFR 335
Cdd:cd11333 232 QELNR----EVFSKYDIMTVGEAPGVDPEEALKYVGPDRGELSMVFNFEHLDLDYGPGGKWKPKPWDLEELKKILSKWQK 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  336 YVNGtDCWSTIYLENHDQPRSITRFGDDSpKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINfknwpiekyedvevrnn 415
Cdd:cd11333 308 ALQG-DGWNALFLENHDQPRSVSRFGNDG-EYRVESAKMLATLLLTLRGTPFIYQGEEIGMTN----------------- 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  416 ydaikeehgenskemkrfleaialiSRDHARTPMQWSrEEPNAGFSgpNAKPWFYLNESFREgINAEDESKDPNSVLNFW 495
Cdd:cd11333 369 -------------------------SRDNARTPMQWD-DSPNAGFS--TGKPWLPVNPNYKE-INVEAQLADPDSVLNFY 419

                ....*...
gi 6322241  496 KEALRFRK 503
Cdd:cd11333 420 KKLIALRK 427
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
514-585 1.10e-06

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


:

Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 46.39  E-value: 1.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322241    514 DFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPN-NSSSFKLEFGNYPRSEVDASSR-TLKPWEGRI 585
Cdd:pfam16657   2 DFRFLEPDNRKVLAYLREYEDETILVVANRSAQPVELDLSAfEGRVPVELFGGEPFPPIGGLYFlTLPPYGFYW 75
 
Name Accession Description Interval E-value
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
16-503 0e+00

Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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: 200472 [Multi-domain]  Cd Length: 428  Bit Score: 616.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   16 KEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIE 95
Cdd:cd11333   1 KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFGTMEDFDELIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   96 KTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKgydaegKPIPPNNWRSYFGGSAWTFDEKTQEFYL 175
Cdd:cd11333  81 EAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGK------DGKPPNNWRSFFGGSAWEYDPETGQYYL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  176 RLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwQLSDPFTMNGPRIHEFH 255
Cdd:cd11333 155 HLFAKEQPDLNWENPEVRQEIYD-MMRFWLDKGVDGFRLDVINLISKDPDFPDAPPGDGDG--LSGHKYYANGPGVHEYL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  256 QEMNKfirnRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAELFR 335
Cdd:cd11333 232 QELNR----EVFSKYDIMTVGEAPGVDPEEALKYVGPDRGELSMVFNFEHLDLDYGPGGKWKPKPWDLEELKKILSKWQK 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  336 YVNGtDCWSTIYLENHDQPRSITRFGDDSpKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINfknwpiekyedvevrnn 415
Cdd:cd11333 308 ALQG-DGWNALFLENHDQPRSVSRFGNDG-EYRVESAKMLATLLLTLRGTPFIYQGEEIGMTN----------------- 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  416 ydaikeehgenskemkrfleaialiSRDHARTPMQWSrEEPNAGFSgpNAKPWFYLNESFREgINAEDESKDPNSVLNFW 495
Cdd:cd11333 369 -------------------------SRDNARTPMQWD-DSPNAGFS--TGKPWLPVNPNYKE-INVEAQLADPDSVLNFY 419

                ....*...
gi 6322241  496 KEALRFRK 503
Cdd:cd11333 420 KKLIALRK 427
trehalose_treC TIGR02403
alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many ...
14-587 7.58e-173

alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.


Pssm-ID: 274115 [Multi-domain]  Cd Length: 543  Bit Score: 501.10  E-value: 7.58e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     14 WWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFAL 93
Cdd:TIGR02403   1 WWQKKVIYQIYPKSFYDSTGDGTGDLRGIIEKLDYLKKLGVDYIWLNPFYVSPQKDNGYDVSDYYAINPLFGTMADFEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     94 IEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKtNPKRDWFFWRPPKGYdaegkpiPPNNWRSYFGGSAWTFDEKTQEF 173
Cdd:TIGR02403  81 VSEAKKRNIKIMLDMVFNHTSTEHEWFKKALAGD-SPYRDFYIWRDPKGK-------PPTNWQSKFGGSAWEYFGDTGQY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    174 YLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwqlsdpFTMNGPRIHE 253
Cdd:TIGR02403 153 YLHLFDKTQADLNWENPEVREELKD-VVNFWRDKGVDGFRLDVINLISKDQFFEDDEIGDGRR-------FYTDGPRVHE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    254 FHQEMNkfirNRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAEL 333
Cdd:TIGR02403 225 YLQEMN----QEVFGDNDSVTVGEMSSTTIENCIRYSNPENKELSMVFTFHHLKVDYPNGEKWTLAKFDFAKLKEIFSTW 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    334 FRYVNGTDCWSTIYLENHDQPRSITRFGDDsPKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINFKNWPIEKYEDVEVR 413
Cdd:TIGR02403 301 QTGMQAGGGWNALFWNNHDQPRAVSRFGDD-GEYRVESAKMLAAAIHLLRGTPYIYQGEEIGMTNPKFTNIEDYRDVESL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    414 NNYDAIKEEhGENSKEMkrfLEAIALISRDHARTPMQWSrEEPNAGFSgpNAKPWFYLNESFREgINAEDESKDPNSVLN 493
Cdd:TIGR02403 380 NAYDILLKK-GKSEEEA---LAILKQKSRDNSRTPMQWN-NEKNAGFT--TGKPWLGVATNYKE-INVEKALADDNSIFY 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    494 FWKEALRFRKAHKDITvYGyDFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPNNSSSFKLEFGNYPRSEVDA 573
Cdd:TIGR02403 452 FYQKLIALRKSEPVIT-DG-DYQFLLPDDPSVWAYTRTYKNQKLLVINNFYGEEKTIELPLDLLSGKILLSNYEEAEKDA 529
                         570
                  ....*....|....
gi 6322241    574 sSRTLKPWEGRIYI 587
Cdd:TIGR02403 530 -KLELKPYEAIVLL 542
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
37-400 2.33e-161

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: 463.75  E-value: 2.33e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     37 GDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSE 116
Cdd:pfam00128   1 GDLQGIIEKLDYLKELGVTAIWLSPIFDSPQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    117 HEWFKESRSSKTNPKRDWFFWRPPkgydaeGKPIPPNNWRSYFGGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAI 196
Cdd:pfam00128  81 HAWFQESRSSKDNPYRDYYFWRPG------GGPIPPNNWRSYFGGSAWTYDEKGQEYYLHLFVAGQPDLNWENPEVRNEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    197 YEsAVGYWLDHGVDGFRIDVGSLYSKVAGlpdapvidenskwqlsDPFTMNGPRIHEFHQEMNKFirnrVKDGREIMTVG 276
Cdd:pfam00128 155 YD-VVRFWLDKGIDGFRIDVVKHISKVPG----------------LPFENNGPFWHEFTQAMNET----VFGYKDVMTVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    277 EMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAELFRYVNGTDCWSTIYLENHDQPRS 356
Cdd:pfam00128 214 EVFHGDGEWARVYTTEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDALPDTNGWNFTFLGNHDQPRF 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 6322241    357 ITRFGDDSPKnrvisGKLLSVLLVSLSGTLYVYQGQELGEINFK 400
Cdd:pfam00128 294 LSRFGDDRAS-----AKLLAVFLLTLRGTPYIYQGEEIGMTGGN 332
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
10-502 1.44e-154

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 449.70  E-value: 1.44e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   10 TEPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNED 89
Cdd:COG0366   1 ADPDWWKDAVIYQIYPDSFADSNGDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSPMSDHGYDISDYRDVDPRFGTLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   90 CFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGydaegkPIPPNNWRSYFGGSAWTFDEK 169
Cdd:COG0366  81 FDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGPDSPYRDWYVWRDGKP------DLPPNNWFSIFGGSAWTWDPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  170 TQEFYLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPdapvidenskwqlsdpftMNGP 249
Cdd:COG0366 155 DGQYYLHLFFSSQPDLNWENPEVREELLD-VLRFWLDRGVDGFRLDAVNHLDKDEGLP------------------ENLP 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  250 RIHEFHQEMNKFIRNRvkdGREIMTVGEMRHATDETKRLYTsaSRHELSELFNFSHTdvgtsPKFRQNLIPYELKDWKVA 329
Cdd:COG0366 216 EVHEFLRELRAAVDEY---YPDFFLVGEAWVDPPEDVARYF--GGDELDMAFNFPLM-----PALWDALAPEDAAELRDA 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  330 LAELFRYVNGtDCWSTIYLENHDQPRSITRFGDDSPKNRVisgKLLSVLLVSLSGTLYVYQGQELGeinFKNwpiEKYED 409
Cdd:COG0366 286 LAQTPALYPE-GGWWANFLRNHDQPRLASRLGGDYDRRRA---KLAAALLLTLPGTPYIYYGDEIG---MTG---DKLQD 355
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  410 VEvrnnydaikeehgenskemkrfleaialiSRDHARTPMQWSrEEPNAGFSgpnaKPWFYLNESFREgINAEDESKDPN 489
Cdd:COG0366 356 PE-----------------------------GRDGCRTPMPWS-DDRNAGFS----TGWLPVPPNYKA-INVEAQEADPD 400
                       490
                ....*....|...
gi 6322241  490 SVLNFWKEALRFR 502
Cdd:COG0366 401 SLLNFYRKLIALR 413
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
10-589 2.69e-140

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 418.38  E-value: 2.69e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    10 TEPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNED 89
Cdd:PRK10933   3 NLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYVSPQVDNGYDVANYTAIDPTYGTLDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    90 CFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRsSKTNPKRDWFFWRppkgydaEGKP-IPPNNWRSYFGGSAWTFDE 168
Cdd:PRK10933  83 FDELVAQAKSRGIRIILDMVFNHTSTQHAWFREAL-NKESPYRQFYIWR-------DGEPeTPPNNWRSKFGGSAWRWHA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   169 KTQEFYLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwqlsdpFTMNG 248
Cdd:PRK10933 155 ESEQYYLHLFAPEQADLNWENPAVRAELKK-VCEFWADRGVDGLRLDVVNLISKDQDFPDDLDGDGRR-------FYTDG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   249 PRIHEFHQEMNKfirnRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELkdwkV 328
Cdd:PRK10933 227 PRAHEFLQEMNR----DVFTPRGLMTVGEMSSTSLEHCQRYAALTGSELSMTFNFHHLKVDYPNGEKWTLAKPDF----V 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   329 ALAELFRYVNG---TDCWSTIYLENHDQPRSITRFGDDSpKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINFKNWPIE 405
Cdd:PRK10933 299 ALKTLFRHWQQgmhNVAWNALFWCNHDQPRIVSRFGDEG-EYRVPAAKMLAMVLHGMQGTPYIYQGEEIGMTNPHFTRIT 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   406 KYEDVEVRNNYdAIKEEHGENSKEMkrfLEAIALISRDHARTPMQWSReEPNAGFSgpNAKPWFYLNESFREgINAEDES 485
Cdd:PRK10933 378 DYRDVESLNMF-AELRNDGRDADEL---LAILASKSRDNSRTPMQWDN-GDNAGFT--QGEPWIGLCDNYQE-INVEAAL 449
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   486 KDPNSVLNFWKEALRFRKAHkDITVYGyDFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPNNSSSFKLEFGN 565
Cdd:PRK10933 450 ADEDSVFYTYQKLIALRKQE-PVLTWG-DYQDLLPNHPSLWCYRREWQGQTLLVIANLSREPQPWQPGQMRGNWQLLMHN 527
                        570       580
                 ....*....|....*....|....
gi 6322241   566 YPRSEVDASSRTLKPWEGRIYISE 589
Cdd:PRK10933 528 YEEASPQPCAMTLRPFEAVWWLQK 551
Aamy smart00642
Alpha-amylase domain;
22-115 1.55e-39

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 142.08  E-value: 1.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241      22 QIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQD---DMGYDIANYEKVWPTYGTNEDCFALIEKTH 98
Cdd:smart00642   1 QIYPDRFADGNGDGGGDLQGIIEKLDYLKDLGVTAIWLSPIFESPQGypsYHGYDISDYKQIDPRFGTMEDFKELVDAAH 80
                           90
                   ....*....|....*..
gi 6322241      99 KLGMKFITDLVINHCSS 115
Cdd:smart00642  81 ARGIKVILDVVINHTSD 97
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
514-585 1.10e-06

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 46.39  E-value: 1.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322241    514 DFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPN-NSSSFKLEFGNYPRSEVDASSR-TLKPWEGRI 585
Cdd:pfam16657   2 DFRFLEPDNRKVLAYLREYEDETILVVANRSAQPVELDLSAfEGRVPVELFGGEPFPPIGGLYFlTLPPYGFYW 75
 
Name Accession Description Interval E-value
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
16-503 0e+00

Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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: 200472 [Multi-domain]  Cd Length: 428  Bit Score: 616.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   16 KEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIE 95
Cdd:cd11333   1 KEAVVYQIYPRSFKDSNGDGIGDLPGIISKLDYLKDLGVDAIWLSPIYPSPQVDNGYDISDYRAIDPEFGTMEDFDELIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   96 KTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKgydaegKPIPPNNWRSYFGGSAWTFDEKTQEFYL 175
Cdd:cd11333  81 EAHKRGIKIIMDLVVNHTSDEHPWFQESRSSRDNPYRDYYIWRDGK------DGKPPNNWRSFFGGSAWEYDPETGQYYL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  176 RLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwQLSDPFTMNGPRIHEFH 255
Cdd:cd11333 155 HLFAKEQPDLNWENPEVRQEIYD-MMRFWLDKGVDGFRLDVINLISKDPDFPDAPPGDGDG--LSGHKYYANGPGVHEYL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  256 QEMNKfirnRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAELFR 335
Cdd:cd11333 232 QELNR----EVFSKYDIMTVGEAPGVDPEEALKYVGPDRGELSMVFNFEHLDLDYGPGGKWKPKPWDLEELKKILSKWQK 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  336 YVNGtDCWSTIYLENHDQPRSITRFGDDSpKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINfknwpiekyedvevrnn 415
Cdd:cd11333 308 ALQG-DGWNALFLENHDQPRSVSRFGNDG-EYRVESAKMLATLLLTLRGTPFIYQGEEIGMTN----------------- 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  416 ydaikeehgenskemkrfleaialiSRDHARTPMQWSrEEPNAGFSgpNAKPWFYLNESFREgINAEDESKDPNSVLNFW 495
Cdd:cd11333 369 -------------------------SRDNARTPMQWD-DSPNAGFS--TGKPWLPVNPNYKE-INVEAQLADPDSVLNFY 419

                ....*...
gi 6322241  496 KEALRFRK 503
Cdd:cd11333 420 KKLIALRK 427
trehalose_treC TIGR02403
alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many ...
14-587 7.58e-173

alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.


Pssm-ID: 274115 [Multi-domain]  Cd Length: 543  Bit Score: 501.10  E-value: 7.58e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     14 WWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFAL 93
Cdd:TIGR02403   1 WWQKKVIYQIYPKSFYDSTGDGTGDLRGIIEKLDYLKKLGVDYIWLNPFYVSPQKDNGYDVSDYYAINPLFGTMADFEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     94 IEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKtNPKRDWFFWRPPKGYdaegkpiPPNNWRSYFGGSAWTFDEKTQEF 173
Cdd:TIGR02403  81 VSEAKKRNIKIMLDMVFNHTSTEHEWFKKALAGD-SPYRDFYIWRDPKGK-------PPTNWQSKFGGSAWEYFGDTGQY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    174 YLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwqlsdpFTMNGPRIHE 253
Cdd:TIGR02403 153 YLHLFDKTQADLNWENPEVREELKD-VVNFWRDKGVDGFRLDVINLISKDQFFEDDEIGDGRR-------FYTDGPRVHE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    254 FHQEMNkfirNRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAEL 333
Cdd:TIGR02403 225 YLQEMN----QEVFGDNDSVTVGEMSSTTIENCIRYSNPENKELSMVFTFHHLKVDYPNGEKWTLAKFDFAKLKEIFSTW 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    334 FRYVNGTDCWSTIYLENHDQPRSITRFGDDsPKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINFKNWPIEKYEDVEVR 413
Cdd:TIGR02403 301 QTGMQAGGGWNALFWNNHDQPRAVSRFGDD-GEYRVESAKMLAAAIHLLRGTPYIYQGEEIGMTNPKFTNIEDYRDVESL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    414 NNYDAIKEEhGENSKEMkrfLEAIALISRDHARTPMQWSrEEPNAGFSgpNAKPWFYLNESFREgINAEDESKDPNSVLN 493
Cdd:TIGR02403 380 NAYDILLKK-GKSEEEA---LAILKQKSRDNSRTPMQWN-NEKNAGFT--TGKPWLGVATNYKE-INVEKALADDNSIFY 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    494 FWKEALRFRKAHKDITvYGyDFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPNNSSSFKLEFGNYPRSEVDA 573
Cdd:TIGR02403 452 FYQKLIALRKSEPVIT-DG-DYQFLLPDDPSVWAYTRTYKNQKLLVINNFYGEEKTIELPLDLLSGKILLSNYEEAEKDA 529
                         570
                  ....*....|....
gi 6322241    574 sSRTLKPWEGRIYI 587
Cdd:TIGR02403 530 -KLELKPYEAIVLL 542
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
37-400 2.33e-161

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: 463.75  E-value: 2.33e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     37 GDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSE 116
Cdd:pfam00128   1 GDLQGIIEKLDYLKELGVTAIWLSPIFDSPQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    117 HEWFKESRSSKTNPKRDWFFWRPPkgydaeGKPIPPNNWRSYFGGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAI 196
Cdd:pfam00128  81 HAWFQESRSSKDNPYRDYYFWRPG------GGPIPPNNWRSYFGGSAWTYDEKGQEYYLHLFVAGQPDLNWENPEVRNEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    197 YEsAVGYWLDHGVDGFRIDVGSLYSKVAGlpdapvidenskwqlsDPFTMNGPRIHEFHQEMNKFirnrVKDGREIMTVG 276
Cdd:pfam00128 155 YD-VVRFWLDKGIDGFRIDVVKHISKVPG----------------LPFENNGPFWHEFTQAMNET----VFGYKDVMTVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    277 EMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAELFRYVNGTDCWSTIYLENHDQPRS 356
Cdd:pfam00128 214 EVFHGDGEWARVYTTEARMELEMGFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDALPDTNGWNFTFLGNHDQPRF 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 6322241    357 ITRFGDDSPKnrvisGKLLSVLLVSLSGTLYVYQGQELGEINFK 400
Cdd:pfam00128 294 LSRFGDDRAS-----AKLLAVFLLTLRGTPYIYQGEEIGMTGGN 332
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
10-502 1.44e-154

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 449.70  E-value: 1.44e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   10 TEPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNED 89
Cdd:COG0366   1 ADPDWWKDAVIYQIYPDSFADSNGDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSPMSDHGYDISDYRDVDPRFGTLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   90 CFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGydaegkPIPPNNWRSYFGGSAWTFDEK 169
Cdd:COG0366  81 FDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGPDSPYRDWYVWRDGKP------DLPPNNWFSIFGGSAWTWDPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  170 TQEFYLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPdapvidenskwqlsdpftMNGP 249
Cdd:COG0366 155 DGQYYLHLFFSSQPDLNWENPEVREELLD-VLRFWLDRGVDGFRLDAVNHLDKDEGLP------------------ENLP 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  250 RIHEFHQEMNKFIRNRvkdGREIMTVGEMRHATDETKRLYTsaSRHELSELFNFSHTdvgtsPKFRQNLIPYELKDWKVA 329
Cdd:COG0366 216 EVHEFLRELRAAVDEY---YPDFFLVGEAWVDPPEDVARYF--GGDELDMAFNFPLM-----PALWDALAPEDAAELRDA 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  330 LAELFRYVNGtDCWSTIYLENHDQPRSITRFGDDSPKNRVisgKLLSVLLVSLSGTLYVYQGQELGeinFKNwpiEKYED 409
Cdd:COG0366 286 LAQTPALYPE-GGWWANFLRNHDQPRLASRLGGDYDRRRA---KLAAALLLTLPGTPYIYYGDEIG---MTG---DKLQD 355
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  410 VEvrnnydaikeehgenskemkrfleaialiSRDHARTPMQWSrEEPNAGFSgpnaKPWFYLNESFREgINAEDESKDPN 489
Cdd:COG0366 356 PE-----------------------------GRDGCRTPMPWS-DDRNAGFS----TGWLPVPPNYKA-INVEAQEADPD 400
                       490
                ....*....|...
gi 6322241  490 SVLNFWKEALRFR 502
Cdd:COG0366 401 SLLNFYRKLIALR 413
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
10-589 2.69e-140

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 418.38  E-value: 2.69e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    10 TEPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNED 89
Cdd:PRK10933   3 NLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYVSPQVDNGYDVANYTAIDPTYGTLDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    90 CFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRsSKTNPKRDWFFWRppkgydaEGKP-IPPNNWRSYFGGSAWTFDE 168
Cdd:PRK10933  83 FDELVAQAKSRGIRIILDMVFNHTSTQHAWFREAL-NKESPYRQFYIWR-------DGEPeTPPNNWRSKFGGSAWRWHA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   169 KTQEFYLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSkwqlsdpFTMNG 248
Cdd:PRK10933 155 ESEQYYLHLFAPEQADLNWENPAVRAELKK-VCEFWADRGVDGLRLDVVNLISKDQDFPDDLDGDGRR-------FYTDG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   249 PRIHEFHQEMNKfirnRVKDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELkdwkV 328
Cdd:PRK10933 227 PRAHEFLQEMNR----DVFTPRGLMTVGEMSSTSLEHCQRYAALTGSELSMTFNFHHLKVDYPNGEKWTLAKPDF----V 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   329 ALAELFRYVNG---TDCWSTIYLENHDQPRSITRFGDDSpKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINFKNWPIE 405
Cdd:PRK10933 299 ALKTLFRHWQQgmhNVAWNALFWCNHDQPRIVSRFGDEG-EYRVPAAKMLAMVLHGMQGTPYIYQGEEIGMTNPHFTRIT 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   406 KYEDVEVRNNYdAIKEEHGENSKEMkrfLEAIALISRDHARTPMQWSReEPNAGFSgpNAKPWFYLNESFREgINAEDES 485
Cdd:PRK10933 378 DYRDVESLNMF-AELRNDGRDADEL---LAILASKSRDNSRTPMQWDN-GDNAGFT--QGEPWIGLCDNYQE-INVEAAL 449
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   486 KDPNSVLNFWKEALRFRKAHkDITVYGyDFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPNNSSSFKLEFGN 565
Cdd:PRK10933 450 ADEDSVFYTYQKLIALRKQE-PVLTWG-DYQDLLPNHPSLWCYRREWQGQTLLVIANLSREPQPWQPGQMRGNWQLLMHN 527
                        570       580
                 ....*....|....*....|....
gi 6322241   566 YPRSEVDASSRTLKPWEGRIYISE 589
Cdd:PRK10933 528 YEEASPQPCAMTLRPFEAVWWLQK 551
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-525 9.70e-131

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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: 200469 [Multi-domain]  Cd Length: 472  Bit Score: 390.85  E-value: 9.70e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   13 KWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFA 92
Cdd:cd11330   1 PWWRGAVIYQIYPRSFLDSNGDGIGDLPGITEKLDYIASLGVDAIWLSPFFKSPMKDFGYDVSDYCAVDPLFGTLDDFDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   93 LIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKgydAEGKPipPNNWRSYFGGSAWTFDEKTQE 172
Cdd:cd11330  81 LVARAHALGLKVMIDQVLSHTSDQHPWFEESRQSRDNPKADWYVWADPK---PDGSP--PNNWLSVFGGSAWQWDPRRGQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  173 FYLRLFCSTQPDLNWENEDCRKAIYESaVGYWLDHGVDGFRIDVGSLYSKVAGL---PDAPVIDENSKWQLSDPFTMNgP 249
Cdd:cd11330 156 YYLHNFLPSQPDLNFHNPEVQDALLDV-ARFWLDRGVDGFRLDAVNFYMHDPALrdnPPRPPDEREDGVAPTNPYGMQ-L 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  250 RIHEFHQEMN----KFIRNRVKDGREIMTVGE---------MRHATDETKRLYTSASRHELSELFNfshtdvgtSPKFRQ 316
Cdd:cd11330 234 HIHDKSQPENlaflERLRALLDEYPGRFLVGEvsdddplevMAEYTSGGDRLHMAYSFDLLGRPFS--------AAVVRD 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  317 nlipyelkdwkvALAELFRYVN-GTDCWStiyLENHDQPRSITRFGDDspKNRVISGKLLSVLLVSLSGTLYVYQGQELG 395
Cdd:cd11330 306 ------------ALEAFEAEAPdGWPCWA---FSNHDVPRAVSRWAGG--ADDPALARLLLALLLSLRGSVCLYQGEELG 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  396 ----EINFknwpiEKYEDVEVRNNYDAIKeehgenskemkrfleaialiSRDHARTPMQWSREEPNAGFSGpnAKPWFYL 471
Cdd:cd11330 369 lpeaELPF-----EELQDPYGITFWPEFK--------------------GRDGCRTPMPWQADAPHAGFST--AKPWLPV 421
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 6322241  472 NESFREGiNAEDESKDPNSVLNFWKEALRFRKAHKDItVYGyDFEFIDLDNKKL 525
Cdd:cd11330 422 PPEHLAL-AVDVQEKDPGSVLNFYRRFLAWRKAQPAL-RTG-TITFLDAPEPLL 472
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-505 3.91e-129

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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: 200470 [Multi-domain]  Cd Length: 450  Bit Score: 385.91  E-value: 3.91e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   13 KWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFA 92
Cdd:cd11331   1 LWWQTGVIYQIYPRSFQDSNGDGVGDLRGIISRLDYLSDLGVDAVWLSPIYPSPMADFGYDVSDYCGIDPLFGTLEDFDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   93 LIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKgydAEGKpiPPNNWRSYFGGSAWTFDEKTQE 172
Cdd:cd11331  81 LVAEAHARGLKVILDFVPNHTSDQHPWFLESRSSRDNPKRDWYIWRDPA---PDGG--PPNNWRSEFGGSAWTWDERTGQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  173 FYLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPvidENSKWQLSDPFTMNGPRIH 252
Cdd:cd11331 156 YYLHAFLPEQPDLNWRNPEVRAAMHD-VLRFWLDRGVDGFRVDVLWLLIKDPQFRDNP---PNPDWRGGMPPHERLLHIY 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  253 EFHQ-EMNKFIRN--RVKDG-REIMTVGEMRHATDETKRLYtSASRHELSELFNFshtdvgtspkfrqNLIpyeLKDWK- 327
Cdd:cd11331 232 TADQpETHEIVREmrRVVDEfGDRVLIGEIYLPLDRLVAYY-GAGRDGLHLPFNF-------------HLI---SLPWDa 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  328 VALAELFRYVNGT---DCWSTIYLENHDQPRSITRFGDdsPKNRVISgkllsVLLVSLSGTLYVYQGQELGeinFKNWPI 404
Cdd:cd11331 295 AALARAIEEYEAAlpaGAWPNWVLGNHDQPRIASRVGP--AQARVAA-----MLLLTLRGTPTLYYGDELG---MEDVPI 364
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  405 --EKYEDVEVRNNYDaikeehgenskemkrfleaiALISRDHARTPMQWsREEPNAGFSGpnAKPWFYLNESFREgINAE 482
Cdd:cd11331 365 ppERVQDPAELNQPG--------------------GGLGRDPERTPMPW-DASPNAGFSA--ADPWLPLSPDARQ-RNVA 420
                       490       500
                ....*....|....*....|...
gi 6322241  483 DESKDPNSVLNFWKEALRFRKAH 505
Cdd:cd11331 421 TQEADPGSMLSLYRRLLALRRAH 443
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
14-505 1.08e-121

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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: 200471 [Multi-domain]  Cd Length: 481  Bit Score: 368.14  E-value: 1.08e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   14 WWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFAL 93
Cdd:cd11332   2 WWRDAVVYQVYPRSFADANGDGIGDLAGIRARLPYLAALGVDAIWLSPFYPSPMADGGYDVADYRDVDPLFGTLADFDAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   94 IEKTHKLGMKFITDLVINHCSSEHEWFKESRSS-KTNPKRDWFFWRPPKGYDAEgkpIPPNNWRSYFGGSAWT----FDE 168
Cdd:cd11332  82 VAAAHELGLRVIVDIVPNHTSDQHPWFQAALAAgPGSPERARYIFRDGRGPDGE---LPPNNWQSVFGGPAWTrvtePDG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  169 KTQEFYLRLFCSTQPDLNWENEDCRKAiYESAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSKWQLSDPFTMNG 248
Cdd:cd11332 159 TDGQWYLHLFAPEQPDLNWDNPEVRAE-FEDVLRFWLDRGVDGFRIDVAHGLAKDPGLPDAPGGGLPVGERPGSHPYWDR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  249 PRIHEFHQEMNKFIRNRvkdGREIMTVGEMRHATDETKRLYtsASRHELSELFNFSHTDVgtspkfrqnliPYELKDWKV 328
Cdd:cd11332 238 DEVHDIYREWRAVLDEY---DPPRVLVAEAWVPDPERLARY--LRPDELHQAFNFDFLKA-----------PWDAAALRR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  329 ALAELFRYVNGTDCWSTIYLENHDQPRSITRFGDDSPKNRVISGKLLSVLLVSLS----------------GTLYVYQGQ 392
Cdd:cd11332 302 AIDRSLAAAAAVGAPPTWVLSNHDVVRHVSRYGLPTPGPDPSGIDGTDEPPDLALglrraraaallmlalpGSAYLYQGE 381
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  393 ELGeinfknwpIEKYEDVEVRNNYDAIKEEHGEnskemkrfleaiALISRDHARTPMQWSREEPNAGFSGPNAKPWFYLN 472
Cdd:cd11332 382 ELG--------LPEVEDLPDALRQDPIWERSGG------------TERGRDGCRVPLPWSGDAPPFGFSPGGAEPWLPQP 441
                       490       500       510
                ....*....|....*....|....*....|...
gi 6322241  473 ESFREgINAEDESKDPNSVLNFWKEALRFRKAH 505
Cdd:cd11332 442 AWWAR-YAVDAQEADPGSTLSLYRRALRLRREL 473
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
11-503 3.38e-119

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


Pssm-ID: 200467 [Multi-domain]  Cd Length: 470  Bit Score: 361.16  E-value: 3.38e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   11 EPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDC 90
Cdd:cd11328   1 DKDWWENAVFYQIYPRSFKDSDGDGIGDLKGITEKLDYFKDIGIDAIWLSPIFKSPMVDFGYDISDFTDIDPIFGTMEDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   91 FALIEKTHKLGMKFITDLVINHCSSEHEWFKESrSSKTNPKRDWFFWRPPKGyDAEGKPIPPNNWRSYFGGSAWTFDEKT 170
Cdd:cd11328  81 EELIAEAKKLGLKVILDFVPNHSSDEHEWFQKS-VKRDEPYKDYYVWHDGKN-NDNGTRVPPNNWLSVFGGSAWTWNEER 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  171 QEFYLRLFCSTQPDLNWENEDCRKAIYESaVGYWLDHGVDGFRID-VGSLYsKVAGLPDAPVIDENSKWQ-----LSDPF 244
Cdd:cd11328 159 QQYYLHQFAVKQPDLNYRNPKVVEEMKNV-LRFWLDKGVDGFRIDaVPHLF-EDEDFLDEPYSDEPGADPddydyLDHIY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  245 TMNGPR----IHEFHQEMNKFIRNRVKDGREIMTvgEMRHATDETKRLYTSASRHELSELFNFSH-TDVGTSPKFRQnlI 319
Cdd:cd11328 237 TKDQPEtydlVYEWREVLDEYAKENNGDTRVMMT--EAYSSLDNTMKYYGNETTYGAHFPFNFELiTNLNKNSNATD--F 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  320 PYELKDWKVALAElfryvNGTDCWstiYLENHDQPRSITRFGDDS-----------PknrvisgkllsvllvslsGTLYV 388
Cdd:cd11328 313 KDLIDKWLDNMPE-----GQTANW---VLGNHDNPRVASRFGEERvdgmnmlsmllP------------------GVAVT 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  389 YQGQELGeinfknwpiekYEDVEVRnnYDAIKEEHGENSKEMKRfleaiALISRDHARTPMQWSREEpNAGFSGpNAKPW 468
Cdd:cd11328 367 YYGEEIG-----------MEDTTIS--WEDTVDPPACNAGPENY-----EAYSRDPARTPFQWDDSK-NAGFST-ANKTW 426
                       490       500       510
                ....*....|....*....|....*....|....*
gi 6322241  469 FYLNESFREgINAEDESKDPNSVLNFWKEALRFRK 503
Cdd:cd11328 427 LPVNPNYKT-LNLEAQKKDPRSHYNIYKKLAQLRK 460
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
14-506 6.87e-105

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


Pssm-ID: 200494 [Multi-domain]  Cd Length: 456  Bit Score: 323.93  E-value: 6.87e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   14 WWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFAL 93
Cdd:cd11359   2 WWQTSVIYQIYPRSFKDSNGDGNGDLKGIREKLDYLKYLGVKTVWLSPIYKSPMKDFGYDVSDFTDIDPMFGTMEDFERL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   94 IEKTHKLGMKFITDLVINHCSSEHEWFKESRSSkTNPKRDWFFWRPPKgydAEGKPIPPNNWRSYFGGSAWTFDEKTQEF 173
Cdd:cd11359  82 LAAMHDRGMKLIMDFVPNHTSDKHEWFQLSRNS-TNPYTDYYIWADCT---ADGPGTPPNNWVSVFGNSAWEYDEKRNQC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  174 YLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVID-------ENSKWQLSDPFTM 246
Cdd:cd11359 158 YLHQFLKEQPDLNFRNPDVQQEMDD-VLRFWLDKGVDGFRVDAVKHLLEATHLRDEPQVNptqppetQYNYSELYHDYTT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  247 NGPRIHE----FHQEMNKFIRNrvkDGREIMTVGEMRHATDETKRLYTSASRHELSELFNFSHTDVGTSpkFRQNLIPYE 322
Cdd:cd11359 237 NQEGVHDiirdWRQTMDKYSSE---PGRYRFMITEVYDDIDTTMRYYGTSFKQEADFPFNFYLLDLGAN--LSGNSINEL 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  323 LKDWKVALAElfryvngtDCWSTIYLENHDQPRSITRFGDDspKNRVISgkllsVLLVSLSGTLYVYQGQELGeinfknw 402
Cdd:cd11359 312 VESWMSNMPE--------GKWPNWVLGNHDNSRIASRLGPQ--YVRAMN-----MLLLTLPGTPTTYYGEEIG------- 369
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  403 piekYEDVEVRNNydaiKEEHGENSKemkrfleaialiSRDHARTPMQWSREEpNAGFSGPNaKPWFYLNESFREgINAE 482
Cdd:cd11359 370 ----MEDVDISVD----KEKDPYTFE------------SRDPERTPMQWNNSN-NAGFSDAN-KTWLPVNSDYKT-VNVE 426
                       490       500
                ....*....|....*....|....
gi 6322241  483 DESKDPNSVLNFWKEALRFRKAHK 506
Cdd:cd11359 427 VQKTDPTSMLNLYRELLLLRSSEL 450
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
14-502 4.02e-84

Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200473 [Multi-domain]  Cd Length: 447  Bit Score: 269.82  E-value: 4.02e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   14 WWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFAL 93
Cdd:cd11334   1 WYKNAVIYQLDVRTFMDSNGDGIGDFRGLTEKLDYLQWLGVTAIWLLPFYPSPLRDDGYDIADYYGVDPRLGTLGDFVEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   94 IEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPIPPNnwrsyFGGSAWTFDEKTQEF 173
Cdd:cd11334  81 LREAHERGIRVIIDLVVNHTSDQHPWFQAARRDPDSPYRDYYVWSDTPPKYKDARIIFPD-----VEKSNWTWDEVAGAY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  174 YLRLFCSTQPDLNWENEDCRKAIYEsAVGYWLDHGVDGFRIDVGSLYSKVAGLPDApvidenskwqlsdpftmNGPRIHE 253
Cdd:cd11334 156 YWHRFYSHQPDLNFDNPAVREEILR-IMDFWLDLGVDGFRLDAVPYLIEREGTNCE-----------------NLPETHD 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  254 FHQEMNKFIRNRvkdGREIMTVGEMRHATDETKRLYTSASRheLSELFNFShtdvgtspkFRQNLI-------PYELKDw 326
Cdd:cd11334 218 FLKRLRAFVDRR---YPDAILLAEANQWPEEVREYFGDGDE--LHMAFNFP---------LNPRLFlalaredAFPIID- 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  327 kvALAELfRYVNGTDCWSTiYLENHD---------QPRSIT--RFGDDsPKNRVI------------SGKLLSVLLVSL- 382
Cdd:cd11334 283 --ALRQT-PPIPEGCQWAN-FLRNHDeltlemltdEERDYVyaAFAPD-PRMRIYnrgirrrlapmlGGDRRRIELAYSl 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  383 ----SGTLYVYQGQELGeinfknwpiekyedvevrnnydaikeeHGENskemkrfleaIALISRDHARTPMQWSrEEPNA 458
Cdd:cd11334 358 lfslPGTPVIYYGDEIG---------------------------MGDN----------LYLPDRDGVRTPMQWS-ADRNG 399
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 6322241  459 GFSGPNAK----------PWFYlnesfrEGINAEDESKDPNSVLNFWKEALRFR 502
Cdd:cd11334 400 GFSTADPQklylpviddgPYGY------ERVNVEAQRRDPSSLLNWVRRLIALR 447
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
18-505 3.42e-83

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


Pssm-ID: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 265.99  E-value: 3.42e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   18 ATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPqDDMGYDIANYEKVWPTYGTNEDCFALIEKT 97
Cdd:cd11316   1 GVFYEIFVRSFYDSDGDGIGDLNGLTEKLDYLNDLGVNGIWLMPIFPSP-SYHGYDVTDYYAIEPDYGTMEDFERLIAEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   98 HKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKgydaegkpipPNNWRSYfGGSAWtFDEKTQEFYLRL 177
Cdd:cd11316  80 HKRGIKVIIDLVINHTSSEHPWFQEAASSPDSPYRDYYIWADDD----------PGGWSSW-GGNVW-HKAGDGGYYYGA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  178 FCSTQPDLNWENEDCRKAIYESAvGYWLDHGVDGFRID-VGSLYSKVAGLPDAPvidENskwqlsdpftmngpriHEFHQ 256
Cdd:cd11316 148 FWSGMPDLNLDNPAVREEIKKIA-KFWLDKGVDGFRLDaAKHIYENGEGQADQE---EN----------------IEFWK 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  257 EMNKFIRnRVKDGReiMTVGEMRHATDETKRLYtsasRHELSELFNFSHTD-VGTSPKFRQ---NLIPYeLKDWKvalaE 332
Cdd:cd11316 208 EFRDYVK-SVKPDA--YLVGEVWDDPSTIAPYY----ASGLDSAFNFDLAEaIIDSVKNGGsgaGLAKA-LLRVY----E 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  333 LFRYVNGTDCWSTIyLENHDQPRSITRFGDDSPKNRVISGkllsvLLVSLSGTLYVYQGQELGEINFKNwpiekyeDvev 412
Cdd:cd11316 276 LYAKYNPDYIDAPF-LSNHDQDRVASQLGGDEAKAKLAAA-----LLLTLPGNPFIYYGEEIGMLGSKP-------D--- 339
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  413 rnnydaikeehgenskemkrflEAIalisrdhaRTPMQWSrEEPNAGFSgpNAKPWFYLNEsfREGINAEDESKDPNSVL 492
Cdd:cd11316 340 ----------------------ENI--------RTPMSWD-ADSGAGFT--TWIPPRPNTN--ATTASVEAQEADPDSLL 384
                       490
                ....*....|...
gi 6322241  493 NFWKEALRFRKAH 505
Cdd:cd11316 385 NHYKRLIALRNEY 397
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
19-501 1.01e-53

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The catalytic triad (DED) is not present here. 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: 200486 [Multi-domain]  Cd Length: 429  Bit Score: 188.67  E-value: 1.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   19 TIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTH 98
Cdd:cd11348   1 VFYEIYPQSFYDSNGDGIGDLQGIISKLDYIKSLGCNAIWLNPCFDSPFKDAGYDVRDYYKVAPRYGTNEDLVRLFDEAH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   99 KLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPippnnwrsYFGGSAwtfdeKTQEFYLRLF 178
Cdd:cd11348  81 KRGIHVLLDLVPGHTSDEHPWFKESKKAENNEYSDRYIWTDSIWSGGPGLP--------FVGGEA-----ERNGNYIVNF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  179 CSTQPDLN----------WENE-------DCRKAIyESAVGYWLDHGVDGFRIDV-GSLY---------SKV-------- 223
Cdd:cd11348 148 FSCQPALNygfahpptepWQQPvdapgpqATREAM-KDIMRFWLDKGADGFRVDMaDSLVkndpgnketIKLwqeirawl 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  224 -AGLPDAPVIdenSKWQLSDPFTMNGpriheFHqeMNKFIRNRvkdgreimtvgeMRHATDETKRLYTSASRHELSELFN 302
Cdd:cd11348 227 dEEYPEAVLV---SEWGNPEQSLKAG-----FD--MDFLLHFG------------GNGYNSLFRNLNTDGGHRRDNCYFD 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  303 FSHTdvGTSPKFRQNLIP-YElkdwKVALAELFRYVNGtdcwstiyleNHDQPRSITRFGDDSPknrvisgKLLSVLLVS 381
Cdd:cd11348 285 ASGK--GDIKPFVDEYLPqYE----ATKGKGYISLPTC----------NHDTPRLNARLTEEEL-------KLAFAFLLT 341
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  382 LSGTLYVYQGQELGeinfknwpiekyedvevrnnydaIKEEHGENSKEMKRfleaialiSRDHARTPMQWSrEEPNAGFS 461
Cdd:cd11348 342 MPGVPFIYYGDEIG-----------------------MRYIEGLPSKEGGY--------NRTGSRTPMQWD-SGKNAGFS 389
                       490       500       510       520
                ....*....|....*....|....*....|....*....|.
gi 6322241  462 GPnAKPWFYLNESFREG-INAEDESKDPNSVLNFWKEALRF 501
Cdd:cd11348 390 TA-PAERLYLPVDPAPDrPTVAAQEDDPNSLLNFVRDLIAL 429
Aamy smart00642
Alpha-amylase domain;
22-115 1.55e-39

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 142.08  E-value: 1.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241      22 QIYPASFKDSNNDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQD---DMGYDIANYEKVWPTYGTNEDCFALIEKTH 98
Cdd:smart00642   1 QIYPDRFADGNGDGGGDLQGIIEKLDYLKDLGVTAIWLSPIFESPQGypsYHGYDISDYKQIDPRFGTMEDFKELVDAAH 80
                           90
                   ....*....|....*..
gi 6322241      99 KLGMKFITDLVINHCSS 115
Cdd:smart00642  81 ARGIKVILDVVINHTSD 97
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
17-264 2.20e-32

Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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: 200477 [Multi-domain]  Cd Length: 389  Bit Score: 128.76  E-value: 2.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   17 EATIYQIYPASFKDSN---------------------NDGW-----------GDMKGIASKLEYIKELGTDAIWISPFYD 64
Cdd:cd11338   1 DAVFYQIFPDRFANGDpsndpkggeynyfgwpdlpdyPPPWggeptrrdfygGDLQGIIEKLDYLKDLGVNAIYLNPIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   65 SPQDDmGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPK-RDWFFWRppkgY 143
Cdd:cd11338  81 APSNH-KYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGESSAyQDWFSIY----Y 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  144 DAEGKPIPPNNWRSYFGgsawtfdektqefylrlfCSTQPDLNWENEDCRKaiYESAVG-YWLDHG-VDGFRIDVGS--- 218
Cdd:cd11338 156 FWPYFTDEPPNYESWWG------------------VPSLPKLNTENPEVRE--YLDSVArYWLKEGdIDGWRLDVADevp 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322241  219 ------LYSKVAGL-PDAPVIDEN----SKWQLSDPF--TMN------------GPRI--HEFHQEMNKFIRN 264
Cdd:cd11338 216 hefwreFRKAVKAVnPDAYIIGEVwedaRPWLQGDQFdsVMNypfrdavldflaGEEIdaEEFANRLNSLRAN 288
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
14-219 4.05e-32

Alpha amylase catalytic domain found in archaeal and 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, bacteroidetes, and proteobacteria. 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: 200452 [Multi-domain]  Cd Length: 336  Bit Score: 126.89  E-value: 4.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   14 WWKEATIYQIYPASFKDSnndgwGDMKGIASKLEYIKELGTDAIWISPFY-----------DSPqddmgYDIANYEKVWP 82
Cdd:cd11313   1 WLRDAVIYEVNVRQFTPE-----GTFKAVTKDLPRLKDLGVDILWLMPIHpigeknrkgslGSP-----YAVKDYRAVNP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   83 TYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKEsrssktNPkrDWFFWrppkgyDAEGKPIPPnnwrsYFGgs 162
Cdd:cd11313  71 EYGTLEDFKALVDEAHDRGMKVILDWVANHTAWDHPLVEE------HP--EWYLR------DSDGNITNK-----VFD-- 129
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322241  163 aWTfDektqefylrlfcstQPDLNWENEDCRKAIYEsAVGYWLD-HGVDGFRIDVGSL 219
Cdd:cd11313 130 -WT-D--------------VADLDYSNPELRDYMID-AMKYWVReFDVDGFRCDVAWG 170
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
19-397 6.99e-32

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: 124.21  E-value: 6.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   19 TIYQIYPASFKDSN---NDGWGDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDI---ANYEKVWPTYGTNEDCFA 92
Cdd:cd00551   1 VIYQLFPDRFTDGDssgGDGGGDLKGIIDKLDYLKDLGVTAIWLTPIFESPEYDGYDKDdgyLDYYEIDPRLGTEEDFKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   93 LIEKTHKLGMKFITDLVINHcssehewfkesrssktnpkrdwffwrppkgydaegkpippnnwrsyfggsawtfdektqe 172
Cdd:cd00551  81 LVKAAHKRGIKVILDLVFNH------------------------------------------------------------ 100
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  173 fylrlfcstqpdlnwenedcrkaiyeSAVGYWLDHGVDGFRIDVGSLYSKvaglpdapvidenskwqlsdpftmngPRIH 252
Cdd:cd00551 101 --------------------------DILRFWLDEGVDGFRLDAAKHVPK--------------------------PEPV 128
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  253 EFHQEMNKFIRNRVKDgreIMTVGEMRHATDETKRLYTSASRHELseLFNFSHTDVGTSPKFRQNLIPYELKDWKVALAE 332
Cdd:cd00551 129 EFLREIRKDAKLAKPD---TLLLGEAWGGPDELLAKAGFDDGLDS--VFDFPLLEALRDALKGGEGALAILAALLLLNPE 203
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322241  333 LFRYVNgtdcwstiYLENHDQPRSITRFGDDSPKNRVISGKLLSVLLVSLSGTLYVYQGQELGEI 397
Cdd:cd00551 204 GALLVN--------FLGNHDTFRLADLVSYKIVELRKARLKLALALLLTLPGTPMIYYIKKLIAL 260
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
12-215 8.74e-31

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


Pssm-ID: 200468 [Multi-domain]  Cd Length: 477  Bit Score: 125.57  E-value: 8.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   12 PKWWKEATIYQIYPASFkdsnndgwgdmkGIASKLEYIKELG-TDAIWISPFYDspqddmgydianyEKVWPTYGTNEDC 90
Cdd:cd11329  63 LKWWQKGPLVELDTESF------------FKEEHVEAISKLGaKGVIYELPADE-------------TYLNNSYGVESDL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   91 FALIEKTHKLGMKFITDLVINHCSSEHEWFKESrSSKTNPKRDWFFWRPPKGydaegkPIPPNNWRSYFGGSAWTFDEKT 170
Cdd:cd11329 118 KELVKTAKQKDIKVILDLTPNHSSKQHPLFKDS-VLKEPPYRSAFVWADGKG------HTPPNNWLSVTGGSAWKWVEDR 190
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6322241  171 QeFYLRLFCSTQPDLNWENEDCRKAiYESAVGYWLDHGVDGFRID 215
Cdd:cd11329 191 Q-YYLHQFGPDQPDLNLNNPAVVDE-LKDVLKHWLDLGVRGFRLA 233
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
8-216 3.79e-26

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 112.79  E-value: 3.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     8 PETEPKWWKEATIYQIYPASFKDSN--------------------NDGW---------------GDMKGIASKLEYIKEL 52
Cdd:PRK10785 112 PDQGPQWVADQVFYQIFPDRFARSLpreavqdhvyyhhaagqeiiLRDWdepvtaqaggstfygGDLDGISEKLPYLKKL 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    53 GTDAIWISPFYDSPQDDMgYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKT---- 128
Cdd:PRK10785 192 GVTALYLNPIFTAPSVHK-YDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTGDSHPWFDRHNRGTGgach 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   129 ---NPKRDWFFwrppkgYDAEGKPIppnNWRSYfggsawtfdektqefylrlfcSTQPDLNWENEDCRKAIY---ESAVG 202
Cdd:PRK10785 271 hpdSPWRDWYS------FSDDGRAL---DWLGY---------------------ASLPKLDFQSEEVVNEIYrgeDSIVR 320
                        250
                 ....*....|....*.
gi 6322241   203 YWLD--HGVDGFRIDV 216
Cdd:PRK10785 321 HWLKapYNIDGWRLDV 336
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
19-215 8.47e-24

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: 200479 [Multi-domain]  Cd Length: 407  Bit Score: 103.83  E-value: 8.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   19 TIYQIYPASFK--DSNND---------------GW--GDMKGIASKLEYIKELGTDAIWISPFYDspqDDM------GYD 73
Cdd:cd11340   5 VIYLIMPDRFAngDPSNDsvpgmlekadrsnpnGRhgGDIQGIIDHLDYLQDLGVTAIWLTPLLE---NDMpsysyhGYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   74 IANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESrssktnPKRDWFfwrppkgydaegkpippN 153
Cdd:cd11340  82 ATDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSEHWWMKDL------PTKDWI-----------------N 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322241  154 NWRSY----FGGSAWT---FDEKTQEFYLR-LFCSTQPDLNWENEDCRKAIYESAVgYWLDH-GVDGFRID 215
Cdd:cd11340 139 QTPEYtqtnHRRTALQdpyASQADRKLFLDgWFVPTMPDLNQRNPLVARYLIQNSI-WWIEYaGLDGIRVD 208
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
37-215 3.61e-23

Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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: 200463  Cd Length: 536  Bit Score: 103.42  E-value: 3.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   37 GDMKGIASKLEYIKELGTDAIWISPFYDSPQ--DDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCS 114
Cdd:cd11324  83 GDLKGLAEKIPYLKELGVTYLHLMPLLKPPEgdNDGGYAVSDYREVDPRLGTMEDLRALAAELRERGISLVLDFVLNHTA 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  115 SEHEWFKESRSSktNPK-RDWFFWRP----PKGYDAEGKPIPPNNWRSYFggsawTFDEKTQEFYLRLFCSTQPDLNWEN 189
Cdd:cd11324 163 DEHEWAQKARAG--DPEyQDYYYMFPdrtlPDAYERTLPEVFPDTAPGNF-----TWDEEMGKWVWTTFNPFQWDLNYAN 235
                       170       180
                ....*....|....*....|....*.
gi 6322241  190 EDCRKAIYESAVgYWLDHGVDGFRID 215
Cdd:cd11324 236 PAVFNEMLDEML-FLANQGVDVLRLD 260
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
19-215 1.14e-21

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


Pssm-ID: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 97.36  E-value: 1.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   19 TIYQIYPASFKD---SNNDG----------------WG-DMKGIASKLEYIKELGTDAIWISPFYD---SPQDDM----- 70
Cdd:cd11320   6 VIYQILTDRFYDgdtSNNPPgspglydpthsnlkkyWGgDWQGIIDKLPYLKDLGVTAIWISPPVEninSPIEGGgntgy 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   71 -GYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHcssehewfkesrSSKTNPKRDWFFWRPPKgyDAEGKP 149
Cdd:cd11320  86 hGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNH------------SSPADYAEDGALYDNGT--LVGDYP 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322241  150 IPPNNWRSYFGGSAWtFDEKTQEFYLRLFcsTQPDLNWENEDCRKAIyESAVGYWLDHGVDGFRID 215
Cdd:cd11320 152 NDDNGWFHHNGGIDD-WSDREQVRYKNLF--DLADLNQSNPWVDQYL-KDAIKFWLDHGIDGIRVD 213
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
21-215 4.31e-18

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


Pssm-ID: 200489 [Multi-domain]  Cd Length: 443  Bit Score: 86.99  E-value: 4.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   21 YQIYPASFKDSNNDGW--GDMKGIASKLEYIKELGTDAIWISPFYDSPQDDM---GYDIANYEKVWPTYGTNEDCFALIE 95
Cdd:cd11352  29 ATWEDNFGWESQGQRFqgGTLKGVRSKLGYLKRLGVTALWLSPVFKQRPELEtyhGYGIQNFLDVDPRFGTREDLRDLVD 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   96 KTHKLGMKFITDLVINH-------------CSSEH-EWFKESRSSKTNPKRDWFFwrPPKGYDAEGKPIP-----PNNWR 156
Cdd:cd11352 109 AAHARGIYVILDIILNHsgdvfsydddrpySSSPGyYRGFPNYPPGGWFIGGDQD--ALPEWRPDDAIWPaelqnLEYYT 186
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322241  157 SYFGGSAWTFDEKTQE---FYLRLFCSTQPDLNWENEDCRKAIYEsavgYWL---DhgVDGFRID 215
Cdd:cd11352 187 RKGRIRNWDGYPEYKEgdfFSLKDFRTGSGSIPSAALDILARVYQ----YWIayaD--IDGFRID 245
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
19-215 3.34e-17

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: 83.07  E-value: 3.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   19 TIYQIYPASFKD---SNN---------------DGW--GDMKGIASKLEYIKELGTDAIWISPFYDSPQDDM------GY 72
Cdd:cd11339   4 TIYFVMTDRFYDgdpSNDngggdgdprsnptdnGPYhgGDFKGLIDKLDYIKDLGFTAIWITPVVKNRSVQAgsagyhGY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   73 DIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSsehewfkesrssktnpkrdwffwrppkgydaegkpipp 152
Cdd:cd11339  84 WGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG-------------------------------------- 125
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322241  153 nnwrsyfggsawtfdektqefylrlfcstqpDLNWENEDCRKAIyESAVGYWLDHGVDGFRID 215
Cdd:cd11339 126 -------------------------------DLNTENPEVVDYL-IDAYKWWIDTGVDGFRID 156
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
17-216 2.53e-16

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


Pssm-ID: 200490 [Multi-domain]  Cd Length: 366  Bit Score: 80.68  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   17 EATIYQIYPASFKDS--NNDGWGD----MKGIASKLEYIKELGTDAIWISPFYDSpqDDMGYDIANYEKVWPTYGTNEDC 90
Cdd:cd11353   1 EAVFYHIYPLGFCGApkENDFDGEtehrILKLEDWIPHLKKLGINAIYFGPVFES--DSHGYDTRDYYKIDRRLGTNEDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   91 FALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTN-PKRDWFfwrppKGYDAEGKpippNNWRSYFGGSAWtfdek 169
Cdd:cd11353  79 KAVCKKLHENGIKVVLDGVFNHVGRDFFAFKDVQENRENsPYKDWF-----KGVNFDGN----SPYNDGFSYEGW----- 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6322241  170 tqEFYLRLfcstqPDLNWENEDCRKAIYEsAVGYWLDH-GVDGFRIDV 216
Cdd:cd11353 145 --EGHYEL-----VKLNLHNPEVVDYLFD-AVRFWIEEfDIDGLRLDV 184
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
15-215 6.56e-15

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: 76.45  E-value: 6.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   15 WKEATIYQIYPASFKDSNNDGW------------GDMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGYDIA------- 75
Cdd:cd11319   6 WRSRSIYQVLTDRFARTDGSSTapcdtadrtycgGTWKGIINKLDYIQGMGFDAIWISPIVKNIEGNTAYGEAyhgywaq 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   76 NYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCssehewfkesrssktnpkrdwffwrppkGYDAEGKPIP---- 151
Cdd:cd11319  86 DLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM----------------------------ASAGPGSDVDyssf 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322241  152 -PNNWRSYF----GGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAIYESAVGYWLDHGVDGFRID 215
Cdd:cd11319 138 vPFNDSSYYhpycWITDYNNQTSVEDCWLGDDVVALPDLNTENPFVVSTLNDWIKNLVSNYSIDGLRID 206
malS PRK09505
alpha-amylase; Reviewed
9-215 6.01e-14

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 75.09  E-value: 6.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     9 ETEPKWWKEATIYQIYPASFK--DSNND--------------GW--GDMKGIASKLEYIKELGTDAIWISPFY------- 63
Cdd:PRK09505 181 AAAPFDWHNATVYFVLTDRFEngDPSNDhsygrhkdgmqeigTFhgGDLRGLTEKLDYLQQLGVNALWISSPLeqihgwv 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    64 ------DSPQDDM-GYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCS----SEHEWF-------KESRS 125
Cdd:PRK09505 261 gggtkgDFPHYAYhGYYTLDWTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTGyatlADMQEFqfgalylSGDEN 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   126 SKTNPKRdWFFWRPPKGydaegkpippNNWRSY-----FG---------GSAWT-----------FDEktqefyLRLFCS 180
Cdd:PRK09505 341 KKTLGER-WSDWQPAAG----------QNWHSFndyinFSdstawdkwwGKDWIrtdigdydnpgFDD------LTMSLA 403
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322241   181 TQPDLNWENE-------------DCR-KAIYESAVG----YWL-----DHGVDGFRID 215
Cdd:PRK09505 404 FLPDIKTESTqasglpvfyankpDTRaKAIDGYTPRdyltHWLsqwvrDYGIDGFRVD 461
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
37-401 5.21e-13

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


Pssm-ID: 200488 [Multi-domain]  Cd Length: 390  Bit Score: 70.77  E-value: 5.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   37 GDMKGIASKLEYIKELGTDAIWISPFYDSPQD-DMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSS 115
Cdd:cd11350  30 GDFKGVIDKLDYLQDLGVNAIELMPVQEFPGNdSWGYNPRHYFALDKAYGTPEDLKRLVDECHQRGIAVILDVVYNHAEG 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  116 EhewfkesrssktNP--KRDWFFWRPPKGYDaegkPIPPNNWRSYFGgsawtfdektQEFYlrlfcstqpDLNWENEDCR 193
Cdd:cd11350 110 Q------------SPlaRLYWDYWYNPPPAD----PPWFNVWGPHFY----------YVGY---------DFNHESPPTR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  194 KAIYEsAVGYWLD-HGVDGFRIDVgslyskVAGLPDAPVIDENSKwqlsdpftMNGPRIHEFHQEMNKFIRNRVKDgreI 272
Cdd:cd11350 155 DFVDD-VNRYWLEeYHIDGFRFDL------TKGFTQKPTGGGAWG--------GYDAARIDFLKRYADEAKAVDKD---F 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  273 MTVGEMRHATDETKRL--YTSASRHELSELFNFSH-TDVGTSPKFRQNLIPYELKDW--KVALAelfryvngtdcwstiY 347
Cdd:cd11350 217 YVIAEHLPDNPEETELatYGMSLWGNSNYSFSQAAmGYQGGSLLLDYSGDPYQNGGWspKNAVN---------------Y 281
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322241  348 LENHDQPRSITRFGDDSPKNR--VISGKLLSVLLVSLSGTLY-------VYQGQELGEINFKN 401
Cdd:cd11350 282 MESHDEERLMYKLGAYGNGNSylGINLETALKRLKLAAAFLFtapgppmIWQGGEFGYDYSIP 344
AmyAc_Sucrose_phosphorylase-like cd11343
Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose ...
59-215 8.92e-13

Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase); Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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: 200481  Cd Length: 445  Bit Score: 70.60  E-value: 8.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   59 ISPFYDSPQDDmGYDIANYEKVWPTYGTNEDcFALIEKTHKLgMkfiTDLVINHCSSEHEWFKESRsSKTNPKRDWFFWR 138
Cdd:cd11343  41 ILPFFPYSSDD-GFSVIDYTEVDPRLGDWDD-IEALAEDYDL-M---FDLVINHISSQSPWFQDFL-AGGDPSKDYFIEA 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  139 PPKgYDAEG----KPIPPNNWRSYFGGS--AWTfdekTqefylrlFCSTQPDLNWENEDCRKAIyESAVGYWLDHGVDGF 212
Cdd:cd11343 114 DPE-EDLSKvvrpRTSPLLTEFETAGGTkhVWT----T-------FSEDQIDLNFRNPEVLLEF-LDILLFYAANGARII 180

                ...
gi 6322241  213 RID 215
Cdd:cd11343 181 RLD 183
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
20-119 5.64e-12

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


Pssm-ID: 200476 [Multi-domain]  Cd Length: 328  Bit Score: 67.16  E-value: 5.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   20 IYQIYPASF--KDSNNDGWGD----MKGIASKLEYIKELGTDAIWISPFYDSpqDDMGYDIANYEKVWPTYGTNEDCFAL 93
Cdd:cd11337   2 FYHIYPLGFcgAPIRNDFDGPpehrLLKLEDWLPHLKELGCNALYLGPVFES--DSHGYDTRDYYRIDRRLGTNEDFKAL 79
                        90       100
                ....*....|....*....|....*.
gi 6322241   94 IEKTHKLGMKFITDLVINHCSSEHEW 119
Cdd:cd11337  80 VAALHERGIRVVLDGVFNHVGRDFFW 105
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
11-214 1.81e-11

Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. 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: 200483 [Multi-domain]  Cd Length: 326  Bit Score: 65.54  E-value: 1.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   11 EPKWWKEATIYQIY-PASFKDSNNdgwgdMKGIASKLEYIKELGTDAIWISPFYDSPQDDMGydIANYEKVWPTYGTNED 89
Cdd:cd11345   9 EMNWWNEGPLYQIGdLQAFSEAGG-----LKGVEGKLDYLSQLKVKGLVLGPIHVVQADQPG--ELNLTEIDPDLGTLED 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   90 CFALIEKTHKLGMKFITDLVinhcssehewfkesrssktnpkrdwffwrppkgydaegkpipPNnwrsYFGGSAWTFDEk 169
Cdd:cd11345  82 FTSLLTAAHKKGISVVLDLT------------------------------------------PN----YRGESSWAFSD- 114
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6322241  170 TQEFYLRLfcstqpdlnwenedcrkaiyESAVGYWLDHGVDGFRI 214
Cdd:cd11345 115 AENVAEKV--------------------KEALEFWLNQGVDGIQV 139
AmyAc_Sucrose_phosphorylase-like_1 cd11356
Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called ...
47-215 9.32e-11

Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase); Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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: 200493  Cd Length: 458  Bit Score: 64.07  E-value: 9.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   47 EYIKELGTDaIWISPFYDSPQDDmGYDIANYEKVWPTYGTNEDCFAlIEKTHKLgMkfiTDLVINHCSSEHEWFKESRSS 126
Cdd:cd11356  32 EHLKDTISG-VHILPFFPYSSDD-GFSVIDYRQVNPELGDWEDIEA-LAKDFRL-M---FDLVINHVSSSSPWFQQFLAG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  127 KtNPKRDWFFwrppkgydaegKPIPPNNWRSYF--------------GGSAW---TFDEKtqefylrlfcstQPDLNWEN 189
Cdd:cd11356 105 E-PPYKDYFI-----------EADPDTDLSQVVrprtsplltpfetaDGTKHvwtTFSPD------------QVDLNFRN 160
                       170       180
                ....*....|....*....|....*.
gi 6322241  190 EDCRKAIYESAVGYwLDHGVDGFRID 215
Cdd:cd11356 161 PEVLLEFLDILLFY-LERGARIIRLD 185
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
46-216 8.33e-10

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


Pssm-ID: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 60.80  E-value: 8.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   46 LEYIKELGTDAIWISPFYDSpqDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRS 125
Cdd:cd11354  37 LDYAVELGCNGLLLGPVFES--ASHGYDTLDHYRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALE 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  126 SKTNPKRDWFFWRPPKGYDAEgkpippnnwrsyFGGSAWTfdektqefylrlfcstqPDLNWENEDCRKAIYEsAVGYWL 205
Cdd:cd11354 115 DGPGSEEDRWHGHAGGGTPAV------------FEGHEDL-----------------VELDHSDPAVVDMVVD-VMCHWL 164
                       170
                ....*....|.
gi 6322241  206 DHGVDGFRIDV 216
Cdd:cd11354 165 DRGIDGWRLDA 175
AmyAc_GlgE_like cd11344
Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan: ...
18-215 1.41e-09

Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. 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: 200482 [Multi-domain]  Cd Length: 355  Bit Score: 59.92  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   18 ATIYQIYPASFKdSNNDGWGDMKGIASKLEYIKELGTDAIWISPFY-----------DSPQ---DDMG--YDIANYE--- 78
Cdd:cd11344   2 SAWYEFFPRSAG-ADPGRHGTFRDAEARLPRIAAMGFDVLYLPPIHpigrtnrkgknNALVagpGDPGspWAIGSEEggh 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   79 -KVWPTYGTNEDCFALIEKTHKLGMKFITDLVINhCSSEHEWFKEsrssktNPkrDWFFWRPpkgyD-----AEGkpiPP 152
Cdd:cd11344  81 dAIHPELGTLEDFDRLVAEARELGIEVALDIALQ-CSPDHPYVKE------HP--EWFRHRP----DgsiqyAEN---PP 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322241  153 nnwrsyfggsawtfdEKTQEFYlrlfcstqpDLNWENEDcRKAIYE---SAVGYWLDHGVDGFRID 215
Cdd:cd11344 145 ---------------KKYQDIY---------PLDFETED-WKGLWQelkRVFLFWIEHGVRIFRVD 185
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
30-129 1.02e-06

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 51.43  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    30 DSNNDG--WgdmKGIASKLEYIKELGTDAIWISPFY--DSPQDDMGYDIANY---------EKVWPTYGTNEDCFALIEK 96
Cdd:PRK09441  13 YLPNDGklW---NRLAERAPELAEAGITAVWLPPAYkgTSGGYDVGYGVYDLfdlgefdqkGTVRTKYGTKEELLNAIDA 89
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6322241    97 THKLGMKFITDLVINHCSS--EHEWFKESRSSKTN 129
Cdd:PRK09441  90 LHENGIKVYADVVLNHKAGadEKETFRVVEVDPDD 124
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
514-585 1.10e-06

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 46.39  E-value: 1.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322241    514 DFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPN-NSSSFKLEFGNYPRSEVDASSR-TLKPWEGRI 585
Cdd:pfam16657   2 DFRFLEPDNRKVLAYLREYEDETILVVANRSAQPVELDLSAfEGRVPVELFGGEPFPPIGGLYFlTLPPYGFYW 75
AmyAc_MTase_N cd11335
Alpha amylase catalytic domain found in maltosyltransferase; Maltosyltransferase (MTase), a ...
2-152 1.22e-06

Alpha amylase catalytic domain found in maltosyltransferase; Maltosyltransferase (MTase), a maltodextrin glycosyltransferase, acts on starch and maltooligosaccharides. It catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or maltooligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose. MTase is a homodimer. The catalytic core domain has the (beta/alpha) 8 barrel fold with the active-site cleft formed at the C-terminal end of the barrel. Substrate binding experiments have led to the location of two distinct maltose-binding sites: one lies in the active-site cleft and the other is located in a pocket adjacent to the active-site cleft. It is a member of the alpha-amylase family, but unlike typical alpha-amylases, MTase does not require calcium for activity and lacks two histidine residues which are predicted to be critical for binding the glucose residue adjacent to the scissile bond in the substrates. The common reaction chemistry of the alpha-amylase family of enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. 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: 200474 [Multi-domain]  Cd Length: 538  Bit Score: 51.15  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    2 TISSAHPETEPKWWKEATIYQIYP---ASFkDSNNDGWGDM-------------KGIASkLEYIKELGTDAIWISPF--- 62
Cdd:cd11335  30 KLSKLKGASKGDWIKSSSVYSLFVrttTAW-DHDGDGALEPenlygfretgtflKMIAL-LPYLKRMGINTIYLLPItki 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   63 -YDSPQDDMG--YDIANYEKVWPTYG--------TNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKEsrssktNPk 131
Cdd:cd11335 108 sKKFKKGELGspYAVKNFFEIDPLLHdpllgdlsVEEEFKAFVEACHMLGIRVVLDFIPRTAARDSDLILE------HP- 180
                       170       180
                ....*....|....*....|.
gi 6322241  132 rDWFFWRPpkgYDAEGKPIPP 152
Cdd:cd11335 181 -EWFYWIK---VDELNNYHPP 197
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
30-112 2.68e-06

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: 49.53  E-value: 2.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   30 DSNNDG-WGDMkgIASKLEYIKELGTDAIWISPFYDSPQ-DDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITD 107
Cdd:cd11314   9 DSPKDGtWWNH--LESKAPELAAAGFTAIWLPPPSKSVSgSSMGYDPGDLYDLNSRYGSEAELRSLIAALHAKGIKVIAD 86

                ....*
gi 6322241  108 LVINH 112
Cdd:cd11314  87 IVINH 91
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
19-215 3.80e-06

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes 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: 49.20  E-value: 3.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   19 TIYQIYPASFKDsnndgwgdmkgIASKLEYIKELGTDAIWISP---FYDS------------PQDdmgYDIANYekvwpT 83
Cdd:cd11315   3 VILHAFDWSFNT-----------IKENLPEIAAAGYTAIQTSPpqkSKEGgneggnwwyryqPTD---YRIGNN-----Q 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   84 YGTNEDCFALIEKTHKLGMKFITDLVINHCSSEhewfkesrssktnPKRDWFFWRPPKGYDAEGkpipPNNWRSYFGGSA 163
Cdd:cd11315  64 LGTEDDFKALCAAAHKYGIKIIVDVVFNHMANE-------------GSAIEDLWYPSADIELFS----PEDFHGNGGISN 126
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322241  164 WTfdektqefylRLFCSTQ------PDLNWEN---EDCRKAIYESAVGYwldhGVDGFRID 215
Cdd:cd11315 127 WN----------DRWQVTQgrlgglPDLNTENpavQQQQKAYLKALVAL----GVDGFRFD 173
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
30-112 7.59e-06

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: 48.28  E-value: 7.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   30 DSNNDG--WgdmKGIASKLEYIKELGTDAIWISPFY--DSPQDDMGYDIanYEkVW-----------PT-YGTNEDCFAL 93
Cdd:cd11318  11 YLPADGqhW---KRLAEDAPELAELGITAVWLPPAYkgASGTEDVGYDV--YD-LYdlgefdqkgtvRTkYGTKEELLEA 84
                        90
                ....*....|....*....
gi 6322241   94 IEKTHKLGMKFITDLVINH 112
Cdd:cd11318  85 IKALHENGIQVYADAVLNH 103
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
20-112 8.74e-06

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


Pssm-ID: 200487 [Multi-domain]  Cd Length: 456  Bit Score: 48.44  E-value: 8.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   20 IYQIYPASFKDSNN----------DGWGDMKGIASK-LEYIKELGTDAIWIS-----------PFYDSPQDD-------M 70
Cdd:cd11349   3 IYQLLPRLFGNKNTtnipngtieeNGVGKFNDFDDTaLKEIKSLGFTHVWYTgvirhatqtdySAYGIPPDDpdivkgrA 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6322241   71 G--YDIANYEKVWPTYGTN-----EDCFALIEKTHKLGMKFITDLVINH 112
Cdd:cd11349  83 GspYAIKDYYDVDPDLATDptnrmEEFEALVERTHAAGLKVIIDFVPNH 131
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
41-215 3.04e-05

pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.


Pssm-ID: 273975 [Multi-domain]  Cd Length: 605  Bit Score: 46.93  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241     41 GIASKLEYIKELGTDAIWISPFYD---------SPQDDMGYDIANYEKVWPTYGTN--------EDCFALIEKTHKLGMK 103
Cdd:TIGR02104 165 GVSTGLDYLKELGVTHVQLLPVFDfagvdeedpNNAYNWGYDPLNYNVPEGSYSTNpydpatriRELKQMIQALHENGIR 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    104 FITDLVINHCSSEhewfKESRSSKTNPKrdwFFWRppkgYDAEGkpippnnwrSYFGGSAwtfdektqefylrlfCSTqp 183
Cdd:TIGR02104 245 VIMDVVYNHTYSR----EESPFEKTVPG---YYYR----YNEDG---------TLSNGTG---------------VGN-- 287
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6322241    184 DLNWENEDCRKAIYESaVGYWL-DHGVDGFRID 215
Cdd:TIGR02104 288 DTASEREMMRKFIVDS-VLYWVkEYNIDGFRFD 319
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
43-142 5.75e-05

malto-oligosyltrehalose synthase;


Pssm-ID: 237740 [Multi-domain]  Cd Length: 879  Bit Score: 46.12  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    43 ASKLEYIKELGTDAIWISPFYDS-PQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHC---SSEHE 118
Cdd:PRK14511  23 AELVPYFADLGVSHLYLSPILAArPGSTHGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMavgGPDNP 102
                         90       100       110
                 ....*....|....*....|....*....|
gi 6322241   119 WF----KESRSSktnPKRDWF--FWRPPKG 142
Cdd:PRK14511 103 WWwdvlEWGRSS---PYADFFdiDWDSGEG 129
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
46-148 1.72e-04

Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. 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: 200475 [Multi-domain]  Cd Length: 660  Bit Score: 44.41  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   46 LEYIKELGTDAIWISPFYDSPQDDM-GYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINH-CSSEHE--WF- 120
Cdd:cd11336  20 VPYLADLGISHLYASPILTARPGSThGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHmAVSGAEnpWWw 99
                        90       100       110
                ....*....|....*....|....*....|...
gi 6322241  121 ---KESRSSktnPKRDWF--FWRPPKGydAEGK 148
Cdd:cd11336 100 dvlENGPDS---PYAGFFdiDWEPPKE--LRGK 127
AmyAc_bac_euk_BE cd11321
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching ...
46-115 2.10e-04

Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic 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: 200460 [Multi-domain]  Cd Length: 406  Bit Score: 43.76  E-value: 2.10e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322241   46 LEYIKELGTDAIWI-----SPFYDSpqddMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSS 115
Cdd:cd11321  45 LPRIKKLGYNAIQLmaimeHAYYAS----FGYQVTNFFAASSRFGTPEDLKYLIDTAHGMGIAVLLDVVHSHASK 115
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
37-215 3.11e-04

Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase); Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. 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: 200462 [Multi-domain]  Cd Length: 569  Bit Score: 43.82  E-value: 3.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   37 GDMKGIASKLEYIKELGTDAIWI--SPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVI---- 110
Cdd:cd11323  94 GDIVGLVDSLDYLQGMGIKGIYIagTPFINMPWGADGYSPLDFTLLDHHFGTIADWRAAIDEIHRRGMYVVLDNTVatmg 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  111 ------NHCSS-------EHE--WfkesrssKTNPK-RDWFF---WRP----PKGYDAEGKPIPPNNWRSYFGGSAWTFD 167
Cdd:cd11323 174 dligfeGYLNTsapfslkEYKaeW-------KTPRRyVDFNFtntYNEtceyPRFWDEDGTPVTADVTETLTGCYDSDFD 246
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241  168 E--KTQEF--------YLRLFCSTQPDLNWENEDCRKAI--YESAVGYWLDhgVDGFRID 215
Cdd:cd11323 247 QygDVEAFgvhpdwqrQLSKFASVQDRLREWRPSVAQKLkhFSCLTIQMLD--IDGFRID 304
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
46-112 4.37e-04

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 43.55  E-value: 4.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322241     46 LEYIKELGTDAIWISPFYDS-PQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINH 112
Cdd:PRK14507  764 LPYLAALGISHVYASPILKArPGSTHGYDIVDHSQINPEIGGEEGFERFCAALKAHGLGQLLDIVPNH 831
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
6-117 7.87e-04

1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 440065 [Multi-domain]  Cd Length: 625  Bit Score: 42.43  E-value: 7.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    6 AHPETEPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKL-EYIKELGTDAIW---IS--PFYDSpqddMGYDIANYEK 79
Cdd:COG0296 132 GPRAKRNALDAPMSIYEVHLGSWRRKEGGRFLTYRELAERLvPYLKELGFTHIElmpVAehPFDGS----WGYQPTGYFA 207
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322241   80 VWPTYGTNEDCFALIEKTHKLGMKFITDLVINH-CSSEH 117
Cdd:COG0296 208 PTSRYGTPDDFKYFVDACHQAGIGVILDWVPNHfPPDGH 246
AmyAc_1 cd11347
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
44-119 1.07e-03

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp 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: 200485 [Multi-domain]  Cd Length: 391  Bit Score: 41.84  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241   44 SKLEYIKELGTDAIW------ISP--------------FYDS------PQDDMG--YDIANYeKVWPTYGTNEDCFALIE 95
Cdd:cd11347  31 EEFDRLAALGFDYVWlmgvwqRGPygraiarsnpglraEYREvlpdltPDDIIGspYAITDY-TVNPDLGGEDDLAALRE 109
                        90       100
                ....*....|....*....|....
gi 6322241   96 KTHKLGMKFITDLVINHCSSEHEW 119
Cdd:cd11347 110 RLAARGLKLMLDFVPNHVALDHPW 133
PLN02784 PLN02784
alpha-amylase
42-112 1.90e-03

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 41.15  E-value: 1.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322241    42 IASKLEYIKELGTDAIWISPFYDS--PQDDMGYDIANYEKvwpTYGTNEDCFALIEKTHKLGMKFITDLVINH 112
Cdd:PLN02784 523 LGEKAAELSSLGFTVVWLPPPTESvsPEGYMPKDLYNLNS---RYGTIDELKDLVKSFHEVGIKVLGDAVLNH 592
glyc_debranch TIGR01531
glycogen debranching enzymye; glycogen debranching enzyme possesses two different catalytic ...
45-122 3.56e-03

glycogen debranching enzymye; glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4-->1,4-glucantransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). Site directed mutagenesis studies in S. cerevisiae indicate that the transferase and glucosidase activities are independent and located in different regions of the polypeptide chain. Proteins in this model belong to the larger alpha-amylase family. The model covers eukaryotic proteins with a seed composed of human, nematode and yeast sequences. Yeast seed sequence is well characterized. The model is quite rigorous; either query sequence yields large bit score or it fails to hit the model altogether. There doesn't appear to be any middle ground. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273673 [Multi-domain]  Cd Length: 1464  Bit Score: 40.59  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241      45 KLEYIKELGTDAIWISPFYDSPQDDMGYDIANYEKVWPTY----GTNEDCFALIEKTHK-LGMKFITDLVINHCSSEHEW 119
Cdd:TIGR01531  137 RLRVAKEKGYNMIHFTPLQELGGSNSCYSLYDQLQLNQHFksqkDGKNDVQALVEKLHRdWNVLSITDIVFNHTANNSPW 216

                   ...
gi 6322241     120 FKE 122
Cdd:TIGR01531  217 LLE 219
PLN00196 PLN00196
alpha-amylase; Provisional
33-118 5.30e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 39.52  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322241    33 NDGWGDMkgIASKLEYIKELGTDAIWISPFYDSPQDDmGYDIAN-YEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVIN 111
Cdd:PLN00196  39 NGGWYNF--LMGKVDDIAAAGITHVWLPPPSHSVSEQ-GYMPGRlYDLDASKYGNEAQLKSLIEAFHGKGVQVIADIVIN 115

                 ....*..
gi 6322241   112 HCSSEHE 118
Cdd:PLN00196 116 HRTAEHK 122
 
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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