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Conserved domains on  [gi|33357016|pdb|1HT6|A]
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Chain A, ALPHA-AMYLASE ISOZYME 1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00196 super family cl31537
alpha-amylase; Provisional
 2-405 0e+00

alpha-amylase; Provisional


The actual alignment was detected with superfamily member PLN00196:

Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 792.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         2 QVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGK 81
Cdd:PLN00196  25 QVLFQGFNWESWKQNGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVSEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        82 GVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQREL 161
Cdd:PLN00196 105 GVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWGPHMICRDDTQYSDGTGNLDTGADFAAAPDIDHLNKRVQREL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       162 KEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAAS 241
Cdd:PLN00196 185 IGWLLWLKSDIGFDAWRLDFAKGYSAEVAKVYIDGTEPSFAVAEIWTSMAYGGDGKPEYDQNAHRQELVNWVDRVGGAAS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       242 AGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIPC 321
Cdd:PLN00196 265 PATVFDFTTKGILNVAVEGELWRLRGADGKAPGVIGWWPAKAVTFVDNHDTGSTQHMWPFPSDKVMQGYAYILTHPGNPC 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       322 IFYDHFFNWGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAV 401
Cdd:PLN00196 345 IFYDHFFDWGLKEEIAALVSIRNRNGITPTSELRIMEADADLYLAEIDGKVIVKIGSRYDVSHLIPEGFQVVAHGNGYAV 424


                 ....
1HT6_A       402 WEKN 405
Cdd:PLN00196 425 WEKI 428
 
Name Accession Description Interval E-value
PLN00196 PLN00196
alpha-amylase; Provisional
 2-405 0e+00

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 792.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         2 QVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGK 81
Cdd:PLN00196  25 QVLFQGFNWESWKQNGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVSEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        82 GVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQREL 161
Cdd:PLN00196 105 GVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWGPHMICRDDTQYSDGTGNLDTGADFAAAPDIDHLNKRVQREL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       162 KEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAAS 241
Cdd:PLN00196 185 IGWLLWLKSDIGFDAWRLDFAKGYSAEVAKVYIDGTEPSFAVAEIWTSMAYGGDGKPEYDQNAHRQELVNWVDRVGGAAS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       242 AGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIPC 321
Cdd:PLN00196 265 PATVFDFTTKGILNVAVEGELWRLRGADGKAPGVIGWWPAKAVTFVDNHDTGSTQHMWPFPSDKVMQGYAYILTHPGNPC 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       322 IFYDHFFNWGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAV 401
Cdd:PLN00196 345 IFYDHFFDWGLKEEIAALVSIRNRNGITPTSELRIMEADADLYLAEIDGKVIVKIGSRYDVSHLIPEGFQVVAHGNGYAV 424


                 ....
1HT6_A       402 WEKN 405
Cdd:PLN00196 425 WEKI 428
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 3-354 4.42e-173

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: 485.19  E-value: 4.42e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        3 VLFQGFNWESWKQsGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVS--NEGYMPGRLYDIDaSKYGNAAELKSLIGALHG 80
Cdd:cd11314   1 VMLQGFYWDSPKD-GTWWNHLESKAPELAAAGFTAIWLPPPSKSVSgsSMGYDPGDLYDLN-SRYGSEAELRSLIAALHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       81 KGVQAIADIVINHRCAdykdsrgiycifeggtsdgrldwgphmicrddtkysdgtanLDTGADFAAAPDIDHLNDRVQRE 160
Cdd:cd11314  79 KGIKVIADIVINHRSG-----------------------------------------PDTGEDFGGAPDLDHTNPEVQND 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      161 LKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATggdgkpnYDQDAHRQNLVNWVDKVGGAA 240
Cdd:cd11314 118 LKAWLNWLKNDIGFDGWRFDFVKGYAPSYVKEYNEATSPSFSVGEYWDGLSY-------ENQDAHRQRLVDWIDATGGGS 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      241 SAgmvFDFTTKGILNAAVEG-ELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGI 319
Cdd:cd11314 191 AA---FDFTTKYILQEAVNNnEYWRLRDGQGKPPGLIGWWPQKAVTFVDNHDTGSTQGHWPFPTDNVLQGYAYILTHPGT 267

                       330       340       350
                ....*....|....*....|....*....|....*
1HT6_A      320 PCIFYDHFFNWGFKDQIAALVAIRKRNGITATSAL 354
Cdd:cd11314 268 PCVFWDHYYDWGLKDEIKALIAARKRAGIGSTSKV 302
Alpha-amyl_C2 smart00810
Alpha-amylase C-terminal beta-sheet domain; This entry represents the beta-sheet domain that ...
 344-404 8.67e-29

Alpha-amylase C-terminal beta-sheet domain; This entry represents the beta-sheet domain that is found in several alpha-amylases, usually at the C-terminus. This domain is organised as a five-stranded anti-parallel beta-sheet.


Pssm-ID: 129046 [Multi-domain]  Cd Length: 61  Bit Score: 106.99  E-value: 8.67e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
1HT6_A         344 KRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWEK 404
Cdd:smart00810   1 KRNGIHSRSSLKILAAEADLYVAMIDEKVIMKIGPRYDVGNLIPSGFHLAASGNDYAVWEK 61
Alpha-amyl_C2 pfam07821
Alpha-amylase C-terminal beta-sheet domain; This domain is organized as a five-stranded ...
 345-403 5.52e-21

Alpha-amylase C-terminal beta-sheet domain; This domain is organized as a five-stranded anti-parallel beta-sheet. It is the probable result of a decay of the common-fold.


Pssm-ID: 400259 [Multi-domain]  Cd Length: 59  Bit Score: 85.69  E-value: 5.52e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
1HT6_A        345 RNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWE 403
Cdd:pfam07821   1 RNGIHARSKVKILAAEADLYVAEIDGKLAVKIGPRYDWSPSGGREWKLAASGNDYAVWE 59
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
26-324 1.67e-18

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 86.46  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPP--PSHSVSNeGYMPGRLYDIDASkYGNAAELKSLIGALHGKGVQAIADIVINHrCAD----YK 99
Cdd:COG0366  36 KLDYLKDLGVDAIWLSPffPSPMSDH-GYDISDYRDVDPR-FGTLADFDELVAEAHARGIKVILDLVLNH-TSDehpwFQ 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      100 DSRgiycifEGGTS---------DGRLDWGPHMICRDDTK----YSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLL 166
Cdd:COG0366 113 EAR------AGPDSpyrdwyvwrDGKPDLPPNNWFSIFGGsawtWDPEDGQYYLHLFFSSQPDLNWENPEVREELLDVLR 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      167 -WLksDLGFDAWRLDFARGYSP----------------EMAKVyIDGTSP-SLAVAEVWdnmatggdgkpnydqDAHRQN 228
Cdd:COG0366 187 fWL--DRGVDGFRLDAVNHLDKdeglpenlpevheflrELRAA-VDEYYPdFFLVGEAW---------------VDPPED 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      229 LVNWVdkvgGAASAGMVFDFTTKGILNAAVEG----ELWRLIDPQGKAPGVMGWWpakaVTFVDNHDTG--STQAMWPFP 302
Cdd:COG0366 249 VARYF----GGDELDMAFNFPLMPALWDALAPedaaELRDALAQTPALYPEGGWW----ANFLRNHDQPrlASRLGGDYD 320

                       330       340
                ....*....|....*....|..
1HT6_A      303 SDKVMQGYAYILTHPGIPCIFY 324
Cdd:COG0366 321 RRRAKLAAALLLTLPGTPYIYY 342
 
Name Accession Description Interval E-value
PLN00196 PLN00196
alpha-amylase; Provisional
 2-405 0e+00

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 792.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         2 QVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGK 81
Cdd:PLN00196  25 QVLFQGFNWESWKQNGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVSEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        82 GVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQREL 161
Cdd:PLN00196 105 GVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWGPHMICRDDTQYSDGTGNLDTGADFAAAPDIDHLNKRVQREL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       162 KEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAAS 241
Cdd:PLN00196 185 IGWLLWLKSDIGFDAWRLDFAKGYSAEVAKVYIDGTEPSFAVAEIWTSMAYGGDGKPEYDQNAHRQELVNWVDRVGGAAS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       242 AGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIPC 321
Cdd:PLN00196 265 PATVFDFTTKGILNVAVEGELWRLRGADGKAPGVIGWWPAKAVTFVDNHDTGSTQHMWPFPSDKVMQGYAYILTHPGNPC 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       322 IFYDHFFNWGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAV 401
Cdd:PLN00196 345 IFYDHFFDWGLKEEIAALVSIRNRNGITPTSELRIMEADADLYLAEIDGKVIVKIGSRYDVSHLIPEGFQVVAHGNGYAV 424


                 ....
1HT6_A       402 WEKN 405
Cdd:PLN00196 425 WEKI 428
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 3-354 4.42e-173

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: 485.19  E-value: 4.42e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        3 VLFQGFNWESWKQsGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVS--NEGYMPGRLYDIDaSKYGNAAELKSLIGALHG 80
Cdd:cd11314   1 VMLQGFYWDSPKD-GTWWNHLESKAPELAAAGFTAIWLPPPSKSVSgsSMGYDPGDLYDLN-SRYGSEAELRSLIAALHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       81 KGVQAIADIVINHRCAdykdsrgiycifeggtsdgrldwgphmicrddtkysdgtanLDTGADFAAAPDIDHLNDRVQRE 160
Cdd:cd11314  79 KGIKVIADIVINHRSG-----------------------------------------PDTGEDFGGAPDLDHTNPEVQND 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      161 LKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATggdgkpnYDQDAHRQNLVNWVDKVGGAA 240
Cdd:cd11314 118 LKAWLNWLKNDIGFDGWRFDFVKGYAPSYVKEYNEATSPSFSVGEYWDGLSY-------ENQDAHRQRLVDWIDATGGGS 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      241 SAgmvFDFTTKGILNAAVEG-ELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGI 319
Cdd:cd11314 191 AA---FDFTTKYILQEAVNNnEYWRLRDGQGKPPGLIGWWPQKAVTFVDNHDTGSTQGHWPFPTDNVLQGYAYILTHPGT 267

                       330       340       350
                ....*....|....*....|....*....|....*
1HT6_A      320 PCIFYDHFFNWGFKDQIAALVAIRKRNGITATSAL 354
Cdd:cd11314 268 PCVFWDHYYDWGLKDEIKALIAARKRAGIGSTSKV 302
PLN02361 PLN02361
alpha-amylase
 2-404 1.05e-154

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 442.33  E-value: 1.05e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         2 QVLFQGFNWESWKQSggWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDaSKYGNAAELKSLIGALHGK 81
Cdd:PLN02361  12 EILLQAFNWESHKHD--WWRNLEGKVPDLAKSGFTSAWLPPPSQSLAPEGYLPQNLYSLN-SAYGSEHLLKSLLRKMKQY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        82 GVQAIADIVINHRCADYKDSRGIYCIFEGGTsdgrLDWGPHMIcrddTKYSDGTANLDTGADFAAAPDIDHLNDRVQREL 161
Cdd:PLN02361  89 NVRAMADIVINHRVGTTQGHGGMYNRYDGIP----LPWDEHAV----TSCTGGLGNRSTGDNFNGVPNIDHTQHFVRKDI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       162 KEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMA-TGGDGKPNYDQDAHRQNLVNWVDKVGGAA 240
Cdd:PLN02361 161 IGWLIWLRNDVGFQDFRFDFAKGYSAKFVKEYIEAAKPLFSVGEYWDSCNySGPDYRLDYNQDSHRQRIVNWIDGTGGLS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       241 SAgmvFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIP 320
Cdd:PLN02361 241 AA---FDFTTKGILQEAVKGQWWRLRDAQGKPPGVMGWWPSRAVTFIDNHDTGSTQAHWPFPSDHIMEGYAYILTHPGIP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       321 CIFYDHFFNWG--FKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSrydvGAVIPAG--FVTSAHG 396
Cdd:PLN02361 318 TVFYDHFYDWGgsIHDQIVKLIDIRKRQDIHSRSSIRILEAQSNLYSAIIDEKLCMKIGD----GSWCPSGreWTLATSG 393


                 ....*...
1HT6_A       397 NDYAVWEK 404
Cdd:PLN02361 394 HRYAVWHK 401
PLN02784 PLN02784
alpha-amylase
 1-404 1.47e-153

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 456.40  E-value: 1.47e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         1 HQVLFQGFNWESWKqSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDaSKYGNAAELKSLIGALHG 80
Cdd:PLN02784 502 FEILCQGFNWESHK-SGRWYMELGEKAAELSSLGFTVVWLPPPTESVSPEGYMPKDLYNLN-SRYGTIDELKDLVKSFHE 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        81 KGVQAIADIVINHRCADYKDSRGIYCIFeggtsDGRLDWGPHMICRDDTKYSdGTANLDTGADFAAAPDIDHLNDRVQRE 160
Cdd:PLN02784 580 VGIKVLGDAVLNHRCAHFQNQNGVWNIF-----GGRLNWDDRAVVADDPHFQ-GRGNKSSGDNFHAAPNIDHSQDFVRKD 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       161 LKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGdGKPNYDQDAHRQNLVNWVDKVGGAA 240
Cdd:PLN02784 654 LKEWLCWMRKEVGYDGWRLDFVRGFWGGYVKDYMEASEPYFAVGEYWDSLSYTY-GEMDYNQDAHRQRIVDWINATNGTA 732

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       241 SAgmvFDFTTKGILNAAVE-GELWRLIDPQGKAPGVMGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGI 319
Cdd:PLN02784 733 GA---FDVTTKGILHSALErCEYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPEGKEMQGYAYILTHPGT 809

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       320 PCIFYDHFFNwGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDY 399
Cdd:PLN02784 810 PAVFYDHIFS-HYHPEIASLISLRNRQKIHCRSEVKITKAERDVYAAIIDEKVAMKIGPGHYEPPNGPQNWSVALEGQDY 888


                 ....*
1HT6_A       400 AVWEK 404
Cdd:PLN02784 889 KVWET 893
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 2-345 9.56e-45

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 161.21  E-value: 9.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         2 QVLFQGFNWESwKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNE---GYMPGRLYDID--------ASKYGNAAE 70
Cdd:PRK09441   4 GTMMQYFEWYL-PNDGKLWNRLAERAPELAEAGITAVWLPPAYKGTSGGydvGYGVYDLFDLGefdqkgtvRTKYGTKEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        71 LKSLIGALHGKGVQAIADIVINHRC-ADYK----------DSR-----GIYCI-------FEGGT---SDGRLDW----G 120
Cdd:PRK09441  83 LLNAIDALHENGIKVYADVVLNHKAgADEKetfrvvevdpDDRtqiisEPYEIegwtrftFPGRGgkySDFKWHWyhfsG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       121 PHMICRDDTK-----------YSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEM 189
Cdd:PRK09441 163 TDYDENPDESgifkivgdgkgWDDQVDDENGNFDYLMGADIDFRHPEVREELKYWAKWYMETTGFDGFRLDAVKHIDAWF 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       190 AKVYID-----GTSPSLAVAEVWDNmatggdgkpnyDQDAhrqnLVNWVDKVGGAAsagMVFDFTTKGILNAAVEG---- 260
Cdd:PRK09441 243 IKEWIEhvrevAGKDLFIVGEYWSH-----------DVDK----LQDYLEQVEGKT---DLFDVPLHYNFHEASKQgrdy 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       261 ELWRLIDpqgkaPGVMGWWPAKAVTFVDNHDTGSTQAM--WPFPSDKvMQGYAYILTHP-GIPCIFYDHFFNW------- 330
Cdd:PRK09441 305 DMRNIFD-----GTLVEADPFHAVTFVDNHDTQPGQALesPVEPWFK-PLAYALILLREeGYPCVFYGDYYGAsgyyidm 378

                        410
                 ....*....|....*
1HT6_A       331 GFKDQIAALVAIRKR 345
Cdd:PRK09441 379 PFKEKLDKLLLARKN 393
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 1-345 9.18e-32

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: 124.17  E-value: 9.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        1 HQVLFQGFNWESwKQSGGWYNMMMGKVDDIAAAGVTHVWLPP------PSHSVsneGYMPGRLYDI---D-----ASKYG 66
Cdd:cd11318   1 NGTMMQYFEWYL-PADGQHWKRLAEDAPELAELGITAVWLPPaykgasGTEDV---GYDVYDLYDLgefDqkgtvRTKYG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       67 NAAELKSLIGALHGKGVQAIADIVINHRC-ADYK----------DSR-----GIYCIfEGGTS---DGRLDwgphmicrd 127
Cdd:cd11318  77 TKEELLEAIKALHENGIQVYADAVLNHKAgADETetvkavevdpNDRnkeisEPYEI-EAWTKftfPGRGG--------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      128 dtKYSDGTANLD--TGADFAAAP--------------------------------DIDHLNDRVQRELKEWLLWLKSDLG 173
Cdd:cd11318 147 --KYSDFKWNWQhfSGVDYDQKTkkkgifkinfegkgwdedvddengnydylmgaDIDYSNPEVREELKRWGKWYINTTG 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      174 FDAWRLDFARGYSPEMAKVYID----GTSPSL-AVAEVWdnmatggdgKPNYDqdahrqNLVNWVDKVGGAASagmVFDF 248
Cdd:cd11318 225 LDGFRLDAVKHISASFIKDWIDhlrrETGKDLfAVGEYW---------SGDLE------ALEDYLDATDGKMS---LFDV 286

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      249 TtkgiL-----NAAVEGELWRLIDPQGKApgVMGWWPAKAVTFVDNHDTGSTQAM--WPFPSDKVmQGYAYILTHP-GIP 320
Cdd:cd11318 287 P----LhynfhEASKSGGNYDLRKIFDGT--LVQSRPDKAVTFVDNHDTQPGQSLesWVEPWFKP-LAYALILLRKdGYP 359

                       410       420       430
                ....*....|....*....|....*....|..
1HT6_A      321 CIFYDHFFNWG-------FKDQIAALVAIRKR 345
Cdd:cd11318 360 CVFYGDYYGIPgedpippKKELLDKLLKARKL 391
Alpha-amyl_C2 smart00810
Alpha-amylase C-terminal beta-sheet domain; This entry represents the beta-sheet domain that ...
 344-404 8.67e-29

Alpha-amylase C-terminal beta-sheet domain; This entry represents the beta-sheet domain that is found in several alpha-amylases, usually at the C-terminus. This domain is organised as a five-stranded anti-parallel beta-sheet.


Pssm-ID: 129046 [Multi-domain]  Cd Length: 61  Bit Score: 106.99  E-value: 8.67e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
1HT6_A         344 KRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWEK 404
Cdd:smart00810   1 KRNGIHSRSSLKILAAEADLYVAMIDEKVIMKIGPRYDVGNLIPSGFHLAASGNDYAVWEK 61
Aamy smart00642
Alpha-amylase domain;
2-97 3.20e-24

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 97.79  E-value: 3.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A           2 QVLFQGFNWESWKQSGGWYNMMMgKVDDIAAAGVTHVWLPPPSHSVSneGYMPGRLYDIDA-----SKYGNAAELKSLIG 76
Cdd:smart00642   1 QIYPDRFADGNGDGGGDLQGIIE-KLDYLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDykqidPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
1HT6_A          77 ALHGKGVQAIADIVINHRCAD 97
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDG 98
Alpha-amyl_C2 pfam07821
Alpha-amylase C-terminal beta-sheet domain; This domain is organized as a five-stranded ...
 345-403 5.52e-21

Alpha-amylase C-terminal beta-sheet domain; This domain is organized as a five-stranded anti-parallel beta-sheet. It is the probable result of a decay of the common-fold.


Pssm-ID: 400259 [Multi-domain]  Cd Length: 59  Bit Score: 85.69  E-value: 5.52e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
1HT6_A        345 RNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWE 403
Cdd:pfam07821   1 RNGIHARSKVKILAAEADLYVAEIDGKLAVKIGPRYDWSPSGGREWKLAASGNDYAVWE 59
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 17-324 8.30e-19

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: 85.30  E-value: 8.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       17 GGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGR----LYDIDaSKYGNAAELKSLIGALHGKGVQAIADIVIN 92
Cdd:cd00551  21 GGDLKGIIDKLDYLKDLGVTAIWLTPIFESPEYDGYDKDDgyldYYEID-PRLGTEEDFKELVKAAHKRGIKVILDLVFN 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       93 HRCADYkdsrgiycifeggtsdgrldwgphmicrddtkysdgtanldtgadfaaapdidhlndrvqrelkeWLlwlksDL 172
Cdd:cd00551 100 HDILRF-----------------------------------------------------------------WL-----DE 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      173 GFDAWRLDFARGYSP--------EMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQdahrqnlvnwvdkvggaasAGM 244
Cdd:cd00551 110 GVDGFRLDAAKHVPKpepveflrEIRKDAKLAKPDTLLLGEAWGGPDELLAKAGFDDG-------------------LDS 170

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      245 VFDFTTKGILNAAVEGELWRLIdpQGKAPGVMGWWPAKAVTFVDNHDT-----GSTQAMWPFPSDKVMQGYAYILTHPGI 319
Cdd:cd00551 171 VFDFPLLEALRDALKGGEGALA--ILAALLLLNPEGALLVNFLGNHDTfrladLVSYKIVELRKARLKLALALLLTLPGT 248


                ....*
1HT6_A      320 PCIFY 324
Cdd:cd00551 249 PMIYY 253
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
26-324 1.67e-18

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 86.46  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPP--PSHSVSNeGYMPGRLYDIDASkYGNAAELKSLIGALHGKGVQAIADIVINHrCAD----YK 99
Cdd:COG0366  36 KLDYLKDLGVDAIWLSPffPSPMSDH-GYDISDYRDVDPR-FGTLADFDELVAEAHARGIKVILDLVLNH-TSDehpwFQ 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      100 DSRgiycifEGGTS---------DGRLDWGPHMICRDDTK----YSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLL 166
Cdd:COG0366 113 EAR------AGPDSpyrdwyvwrDGKPDLPPNNWFSIFGGsawtWDPEDGQYYLHLFFSSQPDLNWENPEVREELLDVLR 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      167 -WLksDLGFDAWRLDFARGYSP----------------EMAKVyIDGTSP-SLAVAEVWdnmatggdgkpnydqDAHRQN 228
Cdd:COG0366 187 fWL--DRGVDGFRLDAVNHLDKdeglpenlpevheflrELRAA-VDEYYPdFFLVGEAW---------------VDPPED 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      229 LVNWVdkvgGAASAGMVFDFTTKGILNAAVEG----ELWRLIDPQGKAPGVMGWWpakaVTFVDNHDTG--STQAMWPFP 302
Cdd:COG0366 249 VARYF----GGDELDMAFNFPLMPALWDALAPedaaELRDALAQTPALYPEGGWW----ANFLRNHDQPrlASRLGGDYD 320

                       330       340
                ....*....|....*....|..
1HT6_A      303 SDKVMQGYAYILTHPGIPCIFY 324
Cdd:COG0366 321 RRRAKLAAALLLTLPGTPYIYY 342
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 26-324 4.07e-15

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: 75.86  E-value: 4.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         26 KVDDIAAAGVTHVWLPPPSHS-VSNEGYMPGRLYDIDaSKYGNAAELKSLIGALHGKGVQAIADIVINHrCAD----YKD 100
Cdd:pfam00128   9 KLDYLKELGVTAIWLSPIFDSpQADHGYDIADYYKID-PHYGTMEDFKELISKAHERGIKVILDLVVNH-TSDehawFQE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        101 SRgiycifEGGTSDGR--LDWGPHMICRDDTK---YSDGTA-NLDTGAD-------FAAAPDIDHLNDRVQRELKEwLLW 167
Cdd:pfam00128  87 SR------SSKDNPYRdyYFWRPGGGPIPPNNwrsYFGGSAwTYDEKGQeyylhlfVAGQPDLNWENPEVRNELYD-VVR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        168 LKSDLGFDAWRLD------------------FARGYSPEMaKVYIDGTSPSLAVAEVWDnmATGGDGKPnyDQDAHRQNL 229
Cdd:pfam00128 160 FWLDKGIDGFRIDvvkhiskvpglpfenngpFWHEFTQAM-NETVFGYKDVMTVGEVFH--GDGEWARV--YTTEARMEL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        230 VnwvdkvggaasagMVFDFTTKGILNAAveGELWRLIDPQGKA------------PGVMGWwpakAVTFVDNHDTGSTQA 297
Cdd:pfam00128 235 E-------------MGFNFPHNDVALKP--FIKWDLAPISARKlkemitdwldalPDTNGW----NFTFLGNHDQPRFLS 295

                         330       340
                  ....*....|....*....|....*..
1HT6_A        298 MWPFPSDKVMQGYAYILTHPGIPCIFY 324
Cdd:pfam00128 296 RFGDDRASAKLLAVFLLTLRGTPYIYQ 322
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 26-324 7.97e-14

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


Pssm-ID: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 72.32  E-value: 7.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPPPSHSVSN----------EGYMPGRLYDIDaSKYGNAAELKSLIGALHGKGVQAIADIVINHRC 95
Cdd:cd11320  52 KLPYLKDLGVTAIWISPPVENINSpiegggntgyHGYWARDFKRTN-EHFGTWEDFDELVDAAHANGIKVIIDFVPNHSS 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       96 -ADYKDSRGIYCI--FEGGTSDGRLDWGPHM--ICRDDTKYSDGTANLdtgADFAaapDIDHLNDRVQRELKE-WLLWLk 169
Cdd:cd11320 131 pADYAEDGALYDNgtLVGDYPNDDNGWFHHNggIDDWSDREQVRYKNL---FDLA---DLNQSNPWVDQYLKDaIKFWL- 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      170 sDLGFDAWRLDFARGYSPEMAKVY---IDGTSPSLAVAEVWDNMATGGDgkpnydqdahrqnlvnwVDKVGGAASAGM-V 245
Cdd:cd11320 204 -DHGIDGIRVDAVKHMPPGWQKSFadaIYSKKPVFTFGEWFLGSPDPGY-----------------EDYVKFANNSGMsL 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      246 FDFTtkgiLNAAVE-------GELWRLIDPQGKAPGVMGwWPAKAVTFVDNHDTGSTQAmWPFPSDKVMQGYAYILTHPG 318
Cdd:cd11320 266 LDFP----LNQAIRdvfagftATMYDLDAMLQQTSSDYN-YENDLVTFIDNHDMPRFLT-LNNNDKRLHQALAFLLTSRG 339


                ....*.
1HT6_A      319 IPCIFY 324
Cdd:cd11320 340 IPVIYY 345
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 23-324 1.04e-13

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: 72.24  E-value: 1.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       23 MMGKVDDIAAAGVTHVWLPP----PSHSVSNEGYMPGRLYDIDAsKYGNAAELKSLIGALHGKGVQAIADIVINHRCADY 98
Cdd:cd11340  47 IIDHLDYLQDLGVTAIWLTPllenDMPSYSYHGYAATDFYRIDP-RFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSEH 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       99 ---KDSrgiycifegGTSDGRLDWGPHmicrDDTKYsDGTANLD---TGADFAAA---------PDIDHLNDRVQRELKE 163
Cdd:cd11340 126 wwmKDL---------PTKDWINQTPEY----TQTNH-RRTALQDpyaSQADRKLFldgwfvptmPDLNQRNPLVARYLIQ 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      164 WLLWLKSDLGFDAWRLD--------FARGYSPEMAKVYidgtsPSL-AVAEVWDNMATGG----DGKPNYDqdahrqnlv 230
Cdd:cd11340 192 NSIWWIEYAGLDGIRVDtypysdkdFMSEWTKAIMEEY-----PNFnIVGEEWSGNPAIVaywqKGKKNPD--------- 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      231 nwvdkvGGAASAGMVFDFTTKGILNAAVEGElwrlidpqgkapgvmGWW-------------------PAKAVTFVDNHD 291
Cdd:cd11340 258 ------GYDSHLPSVMDFPLQDALRDALNEE---------------EGWdtglnrlyetlandflypdPNNLVIFLDNHD 316

                       330       340       350
                ....*....|....*....|....*....|...
1HT6_A      292 TGSTQAMWPFPSDKVMQGYAYILTHPGIPCIFY 324
Cdd:cd11340 317 TSRFYSQVGEDLDKFKLALALLLTTRGIPQLYY 349
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 17-324 3.40e-11

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: 64.12  E-value: 3.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       17 GGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNE--------GYMPGRLYDIDaSKYGNAAELKSLIGALHGKGVQAIAD 88
Cdd:cd11319  39 GGTWKGIINKLDYIQGMGFDAIWISPIVKNIEGNtaygeayhGYWAQDLYSLN-PHFGTADDLKALSKALHKRGMYLMVD 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       89 IVINH-----RCADYKDSRGI----------YCIFEggtsdgrlDWG-PHMI--CRddtkysdgtanldTGADFAAAPDI 150
Cdd:cd11319 118 VVVNHmasagPGSDVDYSSFVpfndssyyhpYCWIT--------DYNnQTSVedCW-------------LGDDVVALPDL 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      151 DHLNDRVQRELKEWLLWLKSDLGFDAWRLD--------FARGYSpEMAKVYidgtspslAVAEVWdnmatggDGKPNYdq 222
Cdd:cd11319 177 NTENPFVVSTLNDWIKNLVSNYSIDGLRIDtakhvrkdFWPGFV-EAAGVF--------AIGEVF-------DGDPNY-- 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      223 dahrqnLVNWVDKVGGAASAGM----VFDFT-TKGILNAAVEGelWRLIDPQGKAPGVMGwwpakavTFVDNHDtgstQA 297
Cdd:cd11319 239 ------VCPYQNYLDGVLNYPLyyplVDAFQsTKGSMSALVDT--INSVQSSCKDPTLLG-------TFLENHD----NP 299

                       330       340       350
                ....*....|....*....|....*....|
1HT6_A      298 MWP-FPSDK--VMQGYAYILTHPGIPCIFY 324
Cdd:cd11319 300 RFLsYTSDQalAKNALAFTLLSDGIPIIYY 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 3-325 5.28e-10

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes 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: 60.37  E-value: 5.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        3 VLFQGFNWEswkqsggwYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEG--------YMPgRLYDIDASKYGNAAELKSL 74
Cdd:cd11315   3 VILHAFDWS--------FNTIKENLPEIAAAGYTAIQTSPPQKSKEGGNeggnwwyrYQP-TDYRIGNNQLGTEDDFKAL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       75 IGALHGKGVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANldtgaDFAAAPDIDHLN 154
Cdd:cd11315  74 CAAAHKYGIKIIVDVVFNHMANEGSAIEDLWYPSADIELFSPEDFHGNGGISNWNDRWQVTQG-----RLGGLPDLNTEN 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      155 DRVQRELKEWLLWLKsDLGFDAWRLDFAR----GYSPEMAKVYIDgtspslavaEVWDNMatGGDGKPNY--------DQ 222
Cdd:cd11315 149 PAVQQQQKAYLKALV-ALGVDGFRFDAAKhielPDEPSKASDFWT---------NILNNL--DKDGLFIYgevlqdggSR 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      223 DAHRQNLvnwVDKVGGAASAgmvFDFTtkgILNAAVEGELW-RLIDPQGKAPGVMgwwPAKAVTFVDNHDT---GSTQAM 298
Cdd:cd11315 217 DSDYASY---LSLGGVTASA---YGFP---LRGALKNAFLFgGSLDPASYGQALP---SDRAVTWVESHDTynnDGFEST 284

                       330       340
                ....*....|....*....|....*..
1HT6_A      299 WPFPSDKVMqGYAYILTHPGIPCIFYD 325
Cdd:cd11315 285 GLDDEDERL-AWAYLAARDGGTPLFFS 310
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 26-324 1.08e-08

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: 56.49  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPPPSHSVSNE-------GYMPGRLYDIDaSKYGNAAELKSLIGALHGKGVQAIADIVINHrcady 98
Cdd:cd11339  50 KLDYIKDLGFTAIWITPVVKNRSVQagsagyhGYWGYDFYRID-PHLGTDADLQDLIDAAHARGIKVILDIVVNH----- 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       99 kdsrgiycifeggtsdgrldwgphmicrddtkysdgTANLDTGadfaaapdidhlNDRVQRELKEWLLWLKsDLGFDAWR 178
Cdd:cd11339 124 ------------------------------------TGDLNTE------------NPEVVDYLIDAYKWWI-DTGVDGFR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      179 LDFARGYSPEMAKVYidgtspslaVAEVWDnmatgGDGKPN-------YDQDAhrQNLVNWVDKVGGAAsagmVFDFTTK 251
Cdd:cd11339 155 IDTVKHVPREFWQEF---------APAIRQ-----AAGKPDffmfgevYDGDP--SYIAPYTTTAGGDS----VLDFPLY 214

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1HT6_A      252 GILNAAVEGelWRLIDPQGKAPGVMGWW--PAKAVTFVDNHDTG----STQAMWPFPSDKVMQGYAYILTHPGIPCIFY 324
Cdd:cd11339 215 GAIRDAFAG--GGSGDLLQDLFLSDDLYndATELVTFLDNHDMGrflsSLKDGSADGTARLALALALLFTSRGIPCIYY 291
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 10-346 3.18e-08

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: 55.18  E-value: 3.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       10 WESWKQSGGWYNMMMG-------KVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDaSKYGNAAELKSLIGALHGKG 82
Cdd:cd11338  38 PPPWGGEPTRRDFYGGdlqgiieKLDYLKDLGVNAIYLNPIFEAPSNHKYDTADYFKID-PHLGTEEDFKELVEEAHKRG 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       83 VQAIADIVINHrCADykDSrgIYciF----EGGTSDGRLDWgpHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQ 158
Cdd:cd11338 117 IRVILDGVFNH-TGD--DS--PY--FqdvlKYGESSAYQDW--FSIYYFWPYFTDEPPNYESWWGVPSLPKLNTENPEVR 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      159 RELKEWLL-WLKSDlGFDAWRLDFARGYSPE-MAKVY--IDGTSP-SLAVAEVWDN---MATGG--DGKPNYdqdahrqn 228
Cdd:cd11338 188 EYLDSVARyWLKEG-DIDGWRLDVADEVPHEfWREFRkaVKAVNPdAYIIGEVWEDarpWLQGDqfDSVMNY-------- 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      229 lvnwvdkvggaASAGMVFDFTTKGILNAA-VEGELWRLidpQGKAPgvmgwWPAKAVTF--VDNHDTgsTQAMWPFPSDK 305
Cdd:cd11338 259 -----------PFRDAVLDFLAGEEIDAEeFANRLNSL---RANYP-----KQVLYAMMnlLDSHDT--PRILTLLGGDK 317

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1HT6_A      306 --VMQGYAYILTHPGIPCIFY----------DHF----FNWGFKDQ-------IAALVAIRKRN 346
Cdd:cd11338 318 arLKLALALQFTLPGAPCIYYgdeigleggkDPDnrrpMPWDEEKWdqdllefYKKLIALRKEH 381
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
 26-180 2.62e-07

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: 52.36  E-value: 2.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPP--PSHSVSNeGYMPGRLYDIDASkYGNAAELKSLIGALHGKGVQAIADIVINH---------- 93
Cdd:cd11359  33 KLDYLKYLGVKTVWLSPiyKSPMKDF-GYDVSDFTDIDPM-FGTMEDFERLLAAMHDRGMKLIMDFVPNHtsdkhewfql 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       94 ---RCADYKDsrgiYCIFEGGTSDGRLD--------WGPHMICRDDTK---YSDgtanldtgADFAAAPDIDHLNDRVQR 159
Cdd:cd11359 111 srnSTNPYTD----YYIWADCTADGPGTppnnwvsvFGNSAWEYDEKRnqcYLH--------QFLKEQPDLNFRNPDVQQ 178

                       170       180
                ....*....|....*....|..
1HT6_A      160 ELKEWL-LWLksDLGFDAWRLD 180
Cdd:cd11359 179 EMDDVLrFWL--DKGVDGFRVD 198
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 26-324 8.27e-07

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: 50.78  E-value: 8.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPPP----SHSVSNEGYMPGRLYDIDAsKYGNAAELKSLIGALHGKGVQAIADIVINH-------- 93
Cdd:cd11352  55 KLGYLKRLGVTALWLSPVfkqrPELETYHGYGIQNFLDVDP-RFGTREDLRDLVDAAHARGIYVILDIILNHsgdvfsyd 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       94 ----RCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDT-----------------GADFAAAPDIDH 152
Cdd:cd11352 134 ddrpYSSSPGYYRGFPNYPPGGWFIGGDQDALPEWRPDDAIWPAELQNLEYytrkgrirnwdgypeykEGDFFSLKDFRT 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      153 LNDRVQRELKEWLL-----WL-KSDLgfDAWRLDFARGYSPEMAKVY---IDGTSPSLA------VAEVWdnmatGGDGK 217
Cdd:cd11352 214 GSGSIPSAALDILArvyqyWIaYADI--DGFRIDTVKHMEPGAARYFcnaIKEFAQSIGkdnfflFGEIT-----GGREA 286

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      218 PNYDqdahrQNLVNWVDKVGGAASAGMVFDFTTKGILNAAVEGELWRLIDPQGKapGVMGWWPAKAVTFVDNHDTGSTQA 297
Cdd:cd11352 287 AAYE-----DLDVTGLDAALDIPEIPFKLENVAKGLAPPAEYFQLFENSKLVGM--GSHRWYGKFHVTFLDDHDQVGRFY 359

                       330       340       350
                ....*....|....*....|....*....|..
1HT6_A      298 MWPFPSDK-----VMQGYAYILTHPGIPCIFY 324
Cdd:cd11352 360 KKRRAADAagdaqLAAALALNLFTLGIPCIYY 391
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 58-329 2.22e-06

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


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 49.10  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       58 YDIDaSKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKDSRgiycifeggtsDGRLdwgphmicrddtkysDGTAN 137
Cdd:cd11317  56 YKLN-SRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMAGDANEVR-----------NCEL---------------VGLAD 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      138 LDTGadfaaapdidhlNDRVQRELKEWL--LWlksDLGFDAWRLDFARGYSPE-MAKVYidgtspslavAEVWDNMATGG 214
Cdd:cd11317 109 LNTE------------SDYVRDKIADYLndLI---SLGVAGFRIDAAKHMWPEdLAAIL----------ARLKDLNGGPL 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      215 DGKPNYDQDAHRQNlvnwvdkvGGAASA------GMVFDFT-TKGILNAAVEGELWRLIDPQGKAPGVMGwwPAKAVTFV 287
Cdd:cd11317 164 GSRPYIYQEVIDGG--------GEAIQPseytgnGDVTEFRyARGLSNAFRGKIKLLLLKNFGEGWGLLP--SERAVVFV 233

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
1HT6_A      288 DNHDT-----GSTQAMWPFPSDKVMQGYAYILTHP-GIPCIFYDHFFN 329
Cdd:cd11317 234 DNHDNqrghgGGGDMLTYKDGRRYKLANAFMLAWPyGTPRVMSSYYFS 281
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
34-235 1.40e-05

bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 47.57  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A         34 GVTHVWLPPPSHSVSNE-----------GYMPGRLYDIDAS-KYGNAAELKSLIGALHGKGVQAIADIVINHRCAD--YK 99
Cdd:PRK14510  200 GVSIVELNPIFASVDEHhlpqlglsnywGYNTVAFLAPDPRlAPGGEEEFAQAIKEAQSAGIAVILDVVFNHTGESnhYG 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A        100 DSRGIYcifegGTSDG---RLDWGphmicrDDTKYSDgtanlDTGADFAAAPDIDHLNDRVQRELKEWLLwlksdLGFDA 176
Cdd:PRK14510  280 PTLSAY-----GSDNSpyyRLEPG------NPKEYEN-----WWGCGNLPNLERPFILRLPMDVLRSWAK-----RGVDG 338

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1HT6_A        177 WRLD-----------FARGYSPEMAKVYIDGTSPSLA-VAEVWDNmatgGDGKpnYDQDAHRQNLVNWVDK 235
Cdd:PRK14510  339 FRLDladelarepdgFIDEFRQFLKAMDQDPVLRRLKmIAEVWDD----GLGG--YQYGKFPQYWGEWNDP 403
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 26-180 4.27e-05

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


Pssm-ID: 200473 [Multi-domain]  Cd Length: 447  Bit Score: 45.25  E-value: 4.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       26 KVDDIAAAGVTHVWLPP--PShsvsnegymPGR--------LYDIDaSKYGNAAELKSLIGALHGKGVQAIADIVINHRC 95
Cdd:cd11334  32 KLDYLQWLGVTAIWLLPfyPS---------PLRddgydiadYYGVD-PRLGTLGDFVEFLREAHERGIRVIIDLVVNHTS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       96 ADY---------KDSRgiYCIFEGGTSDGRLDWGPHMICRDdtkYSDGTANLDTGAD-------FAAAPDIDHLNDRVQR 159
Cdd:cd11334 102 DQHpwfqaarrdPDSP--YRDYYVWSDTPPKYKDARIIFPD---VEKSNWTWDEVAGayywhrfYSHQPDLNFDNPAVRE 176

                       170       180
                ....*....|....*....|..
1HT6_A      160 ELKEWL-LWLksDLGFDAWRLD 180
Cdd:cd11334 177 EILRIMdFWL--DLGVDGFRLD 196
Glyco_hydro_70 pfam02324
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ...
 2-90 5.66e-05

Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain.


Pssm-ID: 426720 [Multi-domain]  Cd Length: 831  Bit Score: 45.43  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A          2 QVLFQGF-NWESWKQSGGWY-NMMMGK-VDDIAAAGVTHVWLPPPS---------HSVSNEGYMPGRLYDIDASK---YG 66
Cdd:pfam02324 585 QLIFEGFsNFQAFATKDEDYtNKKIAKnVDKFAEWGVTDFEMAPQYvssedgsflDSIIQNGYAFEDRYDLAISKnnkYG 664

                          90       100
                  ....*....|....*....|....
1HT6_A         67 NAAELKSLIGALHGKGVQAIADIV 90
Cdd:pfam02324 665 SADDLIKAIKALHKKGIKVIADWV 688
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
 26-93 1.44e-03

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


Pssm-ID: 200467 [Multi-domain]  Cd Length: 470  Bit Score: 40.68  E-value: 1.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1HT6_A       26 KVDDIAAAGVTHVWLPPPSHS-VSNEGYMPGRLYDIDaSKYGNAAELKSLIGALHGKGVQAIADIVINH 93
Cdd:cd11328  35 KLDYFKDIGIDAIWLSPIFKSpMVDFGYDISDFTDID-PIFGTMEDFEELIAEAKKLGLKVILDFVPNH 102
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
 25-346 1.86e-03

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: 39.84  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       25 GKVDDIAAAGVTHVWLPP--PSHSVSNEGYMpGRLYDID-----ASKYGNAAELKSLIGALHGKGVQAIADIVINHRCAD 97
Cdd:cd11313  26 KDLPRLKDLGVDILWLMPihPIGEKNRKGSL-GSPYAVKdyravNPEYGTLEDFKALVDEAHDRGMKVILDWVANHTAWD 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       98 -----------YKDSRGIYCIFEGGTSDGrldwgphmicrddtkysdgtanldtgadfaaaPDIDHLNDRVQRE----LK 162
Cdd:cd11313 105 hplveehpewyLRDSDGNITNKVFDWTDV--------------------------------ADLDYSNPELRDYmidaMK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      163 EWLLWLKSDlGF---DAW--RLDFARGYSPEMAKVYidgtSPSLAVAEVWDnmatggdgkpnYDQDAHRQNLvnwvDkvg 237
Cdd:cd11313 153 YWVREFDVD-GFrcdVAWgvPLDFWKEARAELRAVK----PDVFMLAEAEP-----------RDDDELYSAF----D--- 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A      238 gaasagMVFDFTTKGILNAAVEGE--LWRLIDpQGKAPGVMgwWPAKAV--TFVDNHDTGSTQAMwPFPSDKVMQGYAYI 313
Cdd:cd11313 210 ------MTYDWDLHHTLNDVAKGKasASDLLD-ALNAQEAG--YPKNAVkmRFLENHDENRWAGT-VGEGDALRAAAALS 279

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
1HT6_A      314 LTHPGIPCIF------YDH---FFNW---------GFKDQIAALVAIRKRN 346
Cdd:cd11313 280 FTLPGMPLIYngqeygLDKrpsFFEKdpidwtknhDLTDLYQKLIALKKEN 330
AmyAc_plant_IsoA cd11346
Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching ...
 15-161 4.50e-03

Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like 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: 200484 [Multi-domain]  Cd Length: 347  Bit Score: 38.99  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       15 QSGGWYNMMMGKVDDIAAAGVTHVWLPP--PSHSVSNEGYMPGRLYDIDA-----SKYGNAAELKSLIGALHGKGVQAIA 87
Cdd:cd11346  26 QHAGTFLGVLEKVDHLKSLGVNTVLLQPifAFARVKGPYYPPSFFSAPDPygagdSSLSASAELRAMVKGLHSNGIEVLL 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1HT6_A       88 DIVINHrcadykdsrgiycifeggTSDGRlDWGPHMIC----RDDTKYSDGTANLDTGADFAAAPDIDhLNDRVQREL 161
Cdd:cd11346 106 EVVLTH------------------TAEGT-DESPESESlrgiDAASYYILGKSGVLENSGVPGAAVLN-CNHPVTQSL 163
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
 34-93 5.24e-03

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 38.96  E-value: 5.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
1HT6_A        34 GVTHVWLPP--PSHSVSNeGYMPGRLYDIDASkYGNAAELKSLIGALHGKGVQAIADIVINH 93
Cdd:PRK10933  46 GVDAIWLTPfyVSPQVDN-GYDVANYTAIDPT-YGTLDDFDELVAQAKSRGIRIILDMVFNH 105
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
 12-122 5.79e-03

Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme); The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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: 200461 [Multi-domain]  Cd Length: 402  Bit Score: 38.66  E-value: 5.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HT6_A       12 SWKQ--SGGWYNM--MMGK-VDDIAAAGVTHVWLPPPSHSVSNE--GYMPGRLYDIDaSKYGNAAELKSLIGALHGKGVQ 84
Cdd:cd11322  45 SWKRkeDGRFLSYreLADElIPYVKEMGYTHVELMPVMEHPFDGswGYQVTGYFAPT-SRYGTPDDFKYFVDACHQAGIG 123

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
1HT6_A       85 AIADIVINHRCadyKDSRGIYCiFEGGT----SDGRL----DWGPH 122
Cdd:cd11322 124 VILDWVPGHFP---KDDHGLAR-FDGTPlyeyPDPRKgehpDWGTL 165
 
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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