NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2053295504|gb|QWR39319|]
View 

alpha-glycosidase [Clostridioides difficile]

Protein Classification

glycoside hydrolase family 13 protein( domain architecture ID 11139521)

glycoside hydrolase family 13 protein similar to Bacillus subtilis Intracellular maltogenic amylase and Bacillus acidopullulyticus maltogenic alpha-amylase

CAZY:  GH13
EC:  3.2.1.-
Gene Ontology:  GO:0004553|GO:0005975
SCOP:  4003138

Graphical summary

 Zoom to residue level

show extra options Â»

Show site features     Horizontal zoom: Ã—

List of domain hits

Name Accession Description Interval E-value
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
175-555 0e+00

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: 577.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 175 DTVWYQIFPDRFANGDPSINPEGVDK--------------WGAIPTRDNFTGGDLQGVIEHLDYLSDLGINGIYFCPITI 240
Cdd:cd11338     1 DAVFYQIFPDRFANGDPSNDPKGGEYnyfgwpdlpdypppWGGEPTRRDFYGGDLQGIIEKLDYLKDLGVNAIYLNPIFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 241 GKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKENSRYKNWFYIKDmskid 320
Cdd:cd11338    81 APSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGESSAYQDWFSIYY----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 321 TPIEQIDEKNiPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIY 400
Cdd:cd11338   156 FWPYFTDEPP-NYESWWGVPSLPKLNTENPEVREYLDSVARYWLKEGDIDGWRLDVADEVPHEFWREFRKAVKAVNPDAY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 401 ILGEIWHGSLPWLMGDQFDSVMNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPIQVSEVIFNLLGSHDTTRILTYAN 480
Cdd:cd11338   235 IIGEVWEDARPWLQGDQFDSVMNYPFRDAVLDFLAGEEIDAEEFANRLNSLRANYPKQVLYAMMNLLDSHDTPRILTLLG 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053295504 481 GNIDRFKLAYMFMFVQTGCPCIYYGDEIGMEGElssISEGQRKCMEWNEEKWNKDIFDFMKKIIRLRKENKELRS 555
Cdd:cd11338   315 GDKARLKLALALQFTLPGAPCIYYGDEIGLEGG---KDPDNRRPMPWDEEKWDQDLLEFYKKLIALRKEHPALRT 386
Alpha-amylase_N pfam02903
Alpha amylase, N-terminal ig-like domain;
25-162 7.27e-30

Alpha amylase, N-terminal ig-like domain;


:

Pssm-ID: 397170  Cd Length: 120  Bit Score: 113.94  E-value: 7.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  25 KEAILHIPMSNYAYGYDRETLHIRLRTKKNEAKRVILRIGDQYVWDKggagggnlnasgvGWSGGTnIVMSKEVETELFD 104
Cdd:pfam02903   3 LEAIYHRPESEYAYAYNGNTLHIRLRTKKDDVERVYLIYGDPYEWDG-------------KWYSET-APMKKIGSDELFD 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2053295504 105 YWIAKCKPLNKRSRYGFIIEGQEEKLLFTEKriielgNENDEKELCEIGNFFGYPYLN 162
Cdd:pfam02903  69 YWEAELTPPYKRLRYGFELEGDGESLVYGEK------GFYDEAPLDDTGGYFQFPYIH 120
 
Name Accession Description Interval E-value
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
175-555 0e+00

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: 577.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 175 DTVWYQIFPDRFANGDPSINPEGVDK--------------WGAIPTRDNFTGGDLQGVIEHLDYLSDLGINGIYFCPITI 240
Cdd:cd11338     1 DAVFYQIFPDRFANGDPSNDPKGGEYnyfgwpdlpdypppWGGEPTRRDFYGGDLQGIIEKLDYLKDLGVNAIYLNPIFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 241 GKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKENSRYKNWFYIKDmskid 320
Cdd:cd11338    81 APSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGESSAYQDWFSIYY----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 321 TPIEQIDEKNiPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIY 400
Cdd:cd11338   156 FWPYFTDEPP-NYESWWGVPSLPKLNTENPEVREYLDSVARYWLKEGDIDGWRLDVADEVPHEFWREFRKAVKAVNPDAY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 401 ILGEIWHGSLPWLMGDQFDSVMNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPIQVSEVIFNLLGSHDTTRILTYAN 480
Cdd:cd11338   235 IIGEVWEDARPWLQGDQFDSVMNYPFRDAVLDFLAGEEIDAEEFANRLNSLRANYPKQVLYAMMNLLDSHDTPRILTLLG 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053295504 481 GNIDRFKLAYMFMFVQTGCPCIYYGDEIGMEGElssISEGQRKCMEWNEEKWNKDIFDFMKKIIRLRKENKELRS 555
Cdd:cd11338   315 GDKARLKLALALQFTLPGAPCIYYGDEIGLEGG---KDPDNRRPMPWDEEKWDQDLLEFYKKLIALRKEHPALRT 386
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
170-547 1.14e-108

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 333.37  E-value: 1.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 170 PNWVKDTVWYQIFPDRFANGDpsinpegvdkwgaiptrdNFTGGDLQGVIEHLDYLSDLGINGIYFCPITIG-KTNHRYD 248
Cdd:COG0366     3 PDWWKDAVIYQIYPDSFADSN------------------GDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSpMSDHGYD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 249 TVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKeNSRYKNWFYIKD----------MSK 318
Cdd:COG0366    65 ISDYRDVDPRFGTLADFDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGP-DSPYRDWYVWRDgkpdlppnnwFSI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 319 IDTPIEQIDEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVSNEVD------------HVFWR 386
Cdd:COG0366   144 FGGSAWTWDPEDGQYYLHLFFSSQPDLNWENPEVREELLDVLRFWL-DRGVDGFRLDAVNHLDkdeglpenlpevHEFLR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 387 KFREEVKKVKPDIYILGEIWHGS----LPWLMGDQFDSVMNYLMSEAMKKFFctDEINAEEFKYMINDVMVSYPIQVSEV 462
Cdd:COG0366   223 ELRAAVDEYYPDFFLVGEAWVDPpedvARYFGGDELDMAFNFPLMPALWDAL--APEDAAELRDALAQTPALYPEGGWWA 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 463 IFnlLGSHDTTRILTYANGN--IDRFKLAYMFMFVQTGCPCIYYGDEIGMEGEL---SSISEGQRKCMEWN--------- 528
Cdd:COG0366   301 NF--LRNHDQPRLASRLGGDydRRRAKLAAALLLTLPGTPYIYYGDEIGMTGDKlqdPEGRDGCRTPMPWSddrnagfst 378
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2053295504 529 ----------------EEKWNKDIFDFMKKIIRLR 547
Cdd:COG0366   379 gwlpvppnykainveaQEADPDSLLNFYRKLIALR 413
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
161-564 7.17e-96

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 306.16  E-value: 7.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 161 LNYIDIPkvPNWVKDTVWYQIFPDRFANGDPSIN-PEGV------------DKWGAIPTRDN----FTGGDLQGVIEHLD 223
Cdd:PRK10785  109 VDVPDQG--PQWVADQVFYQIFPDRFARSLPREAvQDHVyyhhaagqeiilRDWDEPVTAQAggstFYGGDLDGISEKLP 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 224 YLSDLGINGIYFCPITIGKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGyYSKQWQDVVQNKE 303
Cdd:PRK10785  187 YLKKLGVTALYLNPIFTAPSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTG-DSHPWFDRHNRGT 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 304 N-------SRYKNWFYIKDMSKidtpieQIDEKNIPyetfgcekYMPKLNTENSEVIKYLL----DVGKYWIQE-FDIDA 371
Cdd:PRK10785  266 GgachhpdSPWRDWYSFSDDGR------ALDWLGYA--------SLPKLDFQSEEVVNEIYrgedSIVRHWLKApYNIDG 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 372 WRLDV----------SNEVDHVfwRKFREEVKKVKPDIYILGEIWHGSLPWLMGDQFDSVMNYL-MSEAMKKFFC-TD-- 437
Cdd:PRK10785  332 WRLDVvhmlgegggaRNNLQHV--AGITQAAKEENPEAYVLGEHFGDARQWLQADVEDAAMNYRgFAFPLRAFLAnTDia 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 438 ----EINAEEFKYMIND--VMVSYPIQVSEviFNLLGSHDTTRILTYANGNIDRFKLAYMFMFVQTGCPCIYYGDEIGME 511
Cdd:PRK10785  410 yhpqQIDAQTCAAWMDEyrAGLPHQQQLRQ--FNQLDSHDTARFKTLLGGDKARMPLALVWLFTWPGVPCIYYGDEVGLD 487
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053295504 512 GELSSISegqRKCMEWNEEKWNKDIFDFMKKIIRLRKENKELRSISNEWVLAD 564
Cdd:PRK10785  488 GGNDPFC---RKPFPWDEAKQDGALLALYQRMIALRKKSQALRRGGCQVLYAE 537
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
213-512 2.77e-82

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: 262.29  E-value: 2.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 213 GDLQGVIEHLDYLSDLGINGIYFCPITI-GKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYY 291
Cdd:pfam00128   1 GDLQGIIEKLDYLKELGVTAIWLSPIFDsPQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 292 SKQWQDVVQNKENSrYKNWFYIKDMSKIDTPIEQI----------DEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGK 361
Cdd:pfam00128  81 HAWFQESRSSKDNP-YRDYYFWRPGGGPIPPNNWRsyfggsawtyDEKGQEYYLHLFVAGQPDLNWENPEVRNELYDVVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 362 YWIQEFdIDAWRLDVSNEVDHV----------FWRKFREEVKK---VKPDIYILGEIWHGSLPWLMGDQFDSVMNYLMS- 427
Cdd:pfam00128 160 FWLDKG-IDGFRIDVVKHISKVpglpfenngpFWHEFTQAMNEtvfGYKDVMTVGEVFHGDGEWARVYTTEARMELEMGf 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 428 -----EAMKKFFCTD---EINAEEFKYMINDVMVSYPiQVSEVIFNLLGSHDTTRILTYANGNIDRFKLAYMFMFVQTGC 499
Cdd:pfam00128 239 nfphnDVALKPFIKWdlaPISARKLKEMITDWLDALP-DTNGWNFTFLGNHDQPRFLSRFGDDRASAKLLAVFLLTLRGT 317
                         330
                  ....*....|...
gi 2053295504 500 PCIYYGDEIGMEG 512
Cdd:pfam00128 318 PYIYQGEEIGMTG 330
Aamy smart00642
Alpha-amylase domain;
180-358 6.88e-37

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 135.15  E-value: 6.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  180 QIFPDRFANGDPSinpegvdkwgaiptrdnfTGGDLQGVIEHLDYLSDLGINGIYFCPIT----IGKTNHRYDTVDYMEV 255
Cdd:smart00642   1 QIYPDRFADGNGD------------------GGGDLQGIIEKLDYLKDLGVTAIWLSPIFespqGYPSYHGYDISDYKQI 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  256 DPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWqDVVQ---NKENSRYKNWFYIKDMSKIDTpIEQIDEKNIP 332
Cdd:smart00642  63 DPRFGTMEDFKELVDAAHARGIKVILDVVINHTSDGGFRL-DAAKfplNGSAFSLLDFFALALLLKILG-IGMTNLPIID 140
                          170       180
                   ....*....|....*....|....*.
gi 2053295504  333 YETFGCEKYMPKLNTENSEVIKYLLD 358
Cdd:smart00642 141 YEQYRDGGGDPNMWWDGTCQWREITK 166
Alpha-amylase_N pfam02903
Alpha amylase, N-terminal ig-like domain;
25-162 7.27e-30

Alpha amylase, N-terminal ig-like domain;


Pssm-ID: 397170  Cd Length: 120  Bit Score: 113.94  E-value: 7.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  25 KEAILHIPMSNYAYGYDRETLHIRLRTKKNEAKRVILRIGDQYVWDKggagggnlnasgvGWSGGTnIVMSKEVETELFD 104
Cdd:pfam02903   3 LEAIYHRPESEYAYAYNGNTLHIRLRTKKDDVERVYLIYGDPYEWDG-------------KWYSET-APMKKIGSDELFD 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2053295504 105 YWIAKCKPLNKRSRYGFIIEGQEEKLLFTEKriielgNENDEKELCEIGNFFGYPYLN 162
Cdd:pfam02903  69 YWEAELTPPYKRLRYGFELEGDGESLVYGEK------GFYDEAPLDDTGGYFQFPYIH 120
E_set_CDase_PDE_N cd02857
N-terminal Early set domain associated with the catalytic domain of cyclomaltodextrinase and ...
28-160 1.50e-22

N-terminal Early set domain associated with the catalytic domain of cyclomaltodextrinase and pullulan-degrading enzymes; E or "early" set domains are associated with the catalytic domain of the cyclomaltodextrinase (CDase) and pullulan-degrading enzymes at the N-terminal end. Members of this subgroup include CDase, maltogenic amylase, and neopullulanase, all of which are capable of hydrolyzing all or two of the following three types of substrates: 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. The N-terminal domain of the CDase and pullulan-degrading enzymes may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199887 [Multi-domain]  Cd Length: 109  Bit Score: 92.77  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  28 ILHIPMS-NYAYGYDRETLHIRLRTKKNEAKRVILRIGDQYVWdkggagggnlnasgvgwsGGTNIVMSKEVETELFDYW 106
Cdd:cd02857     1 IYHDPTSyAYAYPGAGDTVTIRLRTAKDDVDSVFLRYGDDYDG------------------EEKLVPMKKVGSDGLFDYY 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053295504 107 IAKCKPLNKRSRYGFIIEGQEEKLLFTEKRIIELGNENDekelceiGNFFGYPY 160
Cdd:cd02857    63 EAEIPLPEKRLRYYFELEDGGETLYYGERGVSEEGPDDD-------SYYFQIPY 109
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
222-549 7.02e-15

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: 77.74  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 222 LDYLSDLGINGIYFCPI----------TIGKTNHRYDTVDYM---------EVDPTLGDKEtLKKLIEEAHKRNIKIMLD 282
Cdd:TIGR02104 170 LDYLKELGVTHVQLLPVfdfagvdeedPNNAYNWGYDPLNYNvpegsystnPYDPATRIRE-LKQMIQALHENGIRVIMD 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 283 AVFNHigyyskqwqdvVQNKENSRYK----NWFYikdmskidtpieQIDEKNIPYETFGC------EKYMpklntenseV 352
Cdd:TIGR02104 249 VVYNH-----------TYSREESPFEktvpGYYY------------RYNEDGTLSNGTGVgndtasEREM---------M 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 353 IKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIWHGSLPwLMGDQFDSVMN-YLMS---- 427
Cdd:TIGR02104 297 RKFIVDSVLYWVKEYNIDGFRFDLMGIHDIETMNEIRKALNKIDPNILLYGEGWDLGTP-LPPEQKATKANaYQMPgiaf 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 428 --------------EAMKKFFCTDEINAEE-FKYMI-----NDVMVSYPIQVSEVIfNLLGSHDTTRI---LTYANGN-- 482
Cdd:TIGR02104 376 fndefrdalkgsvfHLKKKGFVSGNPGTEEiVKKGIlgsieLDAVKPSALDPSQSI-NYVECHDNHTLwdkLSLANPDet 454
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2053295504 483 ----IDRFKLAYMFMFVQTGCPCIYYGDEI-----GMEGEL-SSISEGQrkcMEWNEEKWNKDIFDFMKKIIRLRKE 549
Cdd:TIGR02104 455 eeqlKKRQKLATAILLLSQGIPFLHAGQEFmrtkqGDENSYnSPDSINQ---LDWDRKATFKDDVNYIKGLIALRKA 528
 
Name Accession Description Interval E-value
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
175-555 0e+00

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: 577.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 175 DTVWYQIFPDRFANGDPSINPEGVDK--------------WGAIPTRDNFTGGDLQGVIEHLDYLSDLGINGIYFCPITI 240
Cdd:cd11338     1 DAVFYQIFPDRFANGDPSNDPKGGEYnyfgwpdlpdypppWGGEPTRRDFYGGDLQGIIEKLDYLKDLGVNAIYLNPIFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 241 GKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKENSRYKNWFYIKDmskid 320
Cdd:cd11338    81 APSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGESSAYQDWFSIYY----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 321 TPIEQIDEKNiPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIY 400
Cdd:cd11338   156 FWPYFTDEPP-NYESWWGVPSLPKLNTENPEVREYLDSVARYWLKEGDIDGWRLDVADEVPHEFWREFRKAVKAVNPDAY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 401 ILGEIWHGSLPWLMGDQFDSVMNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPIQVSEVIFNLLGSHDTTRILTYAN 480
Cdd:cd11338   235 IIGEVWEDARPWLQGDQFDSVMNYPFRDAVLDFLAGEEIDAEEFANRLNSLRANYPKQVLYAMMNLLDSHDTPRILTLLG 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053295504 481 GNIDRFKLAYMFMFVQTGCPCIYYGDEIGMEGElssISEGQRKCMEWNEEKWNKDIFDFMKKIIRLRKENKELRS 555
Cdd:cd11338   315 GDKARLKLALALQFTLPGAPCIYYGDEIGLEGG---KDPDNRRPMPWDEEKWDQDLLEFYKKLIALRKEHPALRT 386
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
170-547 1.14e-108

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 333.37  E-value: 1.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 170 PNWVKDTVWYQIFPDRFANGDpsinpegvdkwgaiptrdNFTGGDLQGVIEHLDYLSDLGINGIYFCPITIG-KTNHRYD 248
Cdd:COG0366     3 PDWWKDAVIYQIYPDSFADSN------------------GDGGGDLKGIIEKLDYLKDLGVDAIWLSPFFPSpMSDHGYD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 249 TVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKeNSRYKNWFYIKD----------MSK 318
Cdd:COG0366    65 ISDYRDVDPRFGTLADFDELVAEAHARGIKVILDLVLNHTSDEHPWFQEARAGP-DSPYRDWYVWRDgkpdlppnnwFSI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 319 IDTPIEQIDEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVSNEVD------------HVFWR 386
Cdd:COG0366   144 FGGSAWTWDPEDGQYYLHLFFSSQPDLNWENPEVREELLDVLRFWL-DRGVDGFRLDAVNHLDkdeglpenlpevHEFLR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 387 KFREEVKKVKPDIYILGEIWHGS----LPWLMGDQFDSVMNYLMSEAMKKFFctDEINAEEFKYMINDVMVSYPIQVSEV 462
Cdd:COG0366   223 ELRAAVDEYYPDFFLVGEAWVDPpedvARYFGGDELDMAFNFPLMPALWDAL--APEDAAELRDALAQTPALYPEGGWWA 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 463 IFnlLGSHDTTRILTYANGN--IDRFKLAYMFMFVQTGCPCIYYGDEIGMEGEL---SSISEGQRKCMEWN--------- 528
Cdd:COG0366   301 NF--LRNHDQPRLASRLGGDydRRRAKLAAALLLTLPGTPYIYYGDEIGMTGDKlqdPEGRDGCRTPMPWSddrnagfst 378
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2053295504 529 ----------------EEKWNKDIFDFMKKIIRLR 547
Cdd:COG0366   379 gwlpvppnykainveaQEADPDSLLNFYRKLIALR 413
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
161-564 7.17e-96

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 306.16  E-value: 7.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 161 LNYIDIPkvPNWVKDTVWYQIFPDRFANGDPSIN-PEGV------------DKWGAIPTRDN----FTGGDLQGVIEHLD 223
Cdd:PRK10785  109 VDVPDQG--PQWVADQVFYQIFPDRFARSLPREAvQDHVyyhhaagqeiilRDWDEPVTAQAggstFYGGDLDGISEKLP 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 224 YLSDLGINGIYFCPITIGKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGyYSKQWQDVVQNKE 303
Cdd:PRK10785  187 YLKKLGVTALYLNPIFTAPSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTG-DSHPWFDRHNRGT 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 304 N-------SRYKNWFYIKDMSKidtpieQIDEKNIPyetfgcekYMPKLNTENSEVIKYLL----DVGKYWIQE-FDIDA 371
Cdd:PRK10785  266 GgachhpdSPWRDWYSFSDDGR------ALDWLGYA--------SLPKLDFQSEEVVNEIYrgedSIVRHWLKApYNIDG 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 372 WRLDV----------SNEVDHVfwRKFREEVKKVKPDIYILGEIWHGSLPWLMGDQFDSVMNYL-MSEAMKKFFC-TD-- 437
Cdd:PRK10785  332 WRLDVvhmlgegggaRNNLQHV--AGITQAAKEENPEAYVLGEHFGDARQWLQADVEDAAMNYRgFAFPLRAFLAnTDia 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 438 ----EINAEEFKYMIND--VMVSYPIQVSEviFNLLGSHDTTRILTYANGNIDRFKLAYMFMFVQTGCPCIYYGDEIGME 511
Cdd:PRK10785  410 yhpqQIDAQTCAAWMDEyrAGLPHQQQLRQ--FNQLDSHDTARFKTLLGGDKARMPLALVWLFTWPGVPCIYYGDEVGLD 487
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053295504 512 GELSSISegqRKCMEWNEEKWNKDIFDFMKKIIRLRKENKELRSISNEWVLAD 564
Cdd:PRK10785  488 GGNDPFC---RKPFPWDEAKQDGALLALYQRMIALRKKSQALRRGGCQVLYAE 537
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
213-512 2.77e-82

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: 262.29  E-value: 2.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 213 GDLQGVIEHLDYLSDLGINGIYFCPITI-GKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYY 291
Cdd:pfam00128   1 GDLQGIIEKLDYLKELGVTAIWLSPIFDsPQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 292 SKQWQDVVQNKENSrYKNWFYIKDMSKIDTPIEQI----------DEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGK 361
Cdd:pfam00128  81 HAWFQESRSSKDNP-YRDYYFWRPGGGPIPPNNWRsyfggsawtyDEKGQEYYLHLFVAGQPDLNWENPEVRNELYDVVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 362 YWIQEFdIDAWRLDVSNEVDHV----------FWRKFREEVKK---VKPDIYILGEIWHGSLPWLMGDQFDSVMNYLMS- 427
Cdd:pfam00128 160 FWLDKG-IDGFRIDVVKHISKVpglpfenngpFWHEFTQAMNEtvfGYKDVMTVGEVFHGDGEWARVYTTEARMELEMGf 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 428 -----EAMKKFFCTD---EINAEEFKYMINDVMVSYPiQVSEVIFNLLGSHDTTRILTYANGNIDRFKLAYMFMFVQTGC 499
Cdd:pfam00128 239 nfphnDVALKPFIKWdlaPISARKLKEMITDWLDALP-DTNGWNFTFLGNHDQPRFLSRFGDDRASAKLLAVFLLTLRGT 317
                         330
                  ....*....|...
gi 2053295504 500 PCIYYGDEIGMEG 512
Cdd:pfam00128 318 PYIYQGEEIGMTG 330
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
175-554 3.41e-76

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: 247.47  E-value: 3.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 175 DTVWYQIFPDRFAnGDPSINPEGvdkwGAIPTRdnftggdLQGVIEHLDYLSDLGINGIYFCPItIGKTNHRYDTVDYME 254
Cdd:cd11353     1 EAVFYHIYPLGFC-GAPKENDFD----GETEHR-------ILKLEDWIPHLKKLGINAIYFGPV-FESDSHGYDTRDYYK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 255 VDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKENSRYKNWFYIKDMSKiDTPIEQidekNIPYE 334
Cdd:cd11353    68 IDRRLGTNEDFKAVCKKLHENGIKVVLDGVFNHVGRDFFAFKDVQENRENSPYKDWFKGVNFDG-NSPYND----GFSYE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 335 TFGCEKYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIWHGSLP-WL 413
Cdd:cd11353   143 GWEGHYELVKLNLHNPEVVDYLFDAVRFWIEEFDIDGLRLDVADCLDFDFLRELRDFCKSLKPDFWLMGEVIHGDYNrWA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 414 MGDQFDSVMNYlmsEAMKKFF-CTDEINAEEFKYMINDVMVSYPIQVSEVIFNLLGSHDTTRILTYANgNIDRFKLAYMF 492
Cdd:cd11353   223 NDEMLDSVTNY---ECYKGLYsSHNDHNYFEIAHSLNRQFGLEGIYRGKHLYNFVDNHDVNRIASILK-NKEHLPPIYAL 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053295504 493 MFVQTGCPCIYYGDEIGMEGELSSISEGQ-RKCMEWNE--EKWNkDIFDFMKKIIRLRKENKELR 554
Cdd:cd11353   299 LFTMPGIPSIYYGSEWGIEGVKGNGSDAAlRPALDEPElsGENN-ELTDLIAKLARIRRASPALC 362
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
177-554 5.00e-72

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: 235.11  E-value: 5.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 177 VWYQIFPDRFAnGDPSINPEGvdkwGAIPTRdnftggdLQGVIEHLDYLSDLGINGIYFCPItIGKTNHRYDTVDYMEVD 256
Cdd:cd11337     1 IFYHIYPLGFC-GAPIRNDFD----GPPEHR-------LLKLEDWLPHLKELGCNALYLGPV-FESDSHGYDTRDYYRID 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 257 PTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGyyskqwqdvvqnkensryknwfyikdmskidtpieqideKNIPYEtf 336
Cdd:cd11337    68 RRLGTNEDFKALVAALHERGIRVVLDGVFNHVG---------------------------------------RDFFWE-- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 337 GCEKyMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIWHGSLP-WLMG 415
Cdd:cd11337   107 GHYD-LVKLNLDNPAVVDYLFDVVRFWIEEFDIDGLRLDAAYCLDPDFWRELRPFCRELKPDFWLMGEVIHGDYNrWVND 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 416 DQFDSVMNYlmsEAMKKFF-CTDEINAEEFKYMINDVMVSYPIQVSEVIFNLLGSHDTTRILTYAnGNIDRFKLAYMFMF 494
Cdd:cd11337   186 SMLDSVTNY---ELYKGLWsSHNDHNFFEIAHSLNRLFRHNGLYRGFHLYTFVDNHDVTRIASIL-GDKAHLPLAYALLF 261
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053295504 495 VQTGCPCIYYGDEIGMEGELSSISEGQRKCM---EWNEEKWNKDIFDFMKKIIRLRKENKELR 554
Cdd:cd11337   262 TMPGIPSIYYGSEWGIEGVKEEGSDADLRPLplrPAELSPLGNELTRLIQALIALRRRSPALC 324
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
177-554 3.39e-66

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: 222.07  E-value: 3.39e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 177 VWYQIFPDRFA--NGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPITIGKTNHRYDTVDYME 254
Cdd:cd11316     2 VFYEIFVRSFYdsDGD------GI--------------GDLNGLTEKLDYLNDLGVNGIWLMPIFPSPSYHGYDVTDYYA 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 255 VDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--W-QDVVQNKeNSRYKNWFYIKDmskiDTPIEQIDEKNI 331
Cdd:cd11316    62 IEPDYGTMEDFERLIAEAHKRGIKVIIDLVINHT---SSEhpWfQEAASSP-DSPYRDYYIWAD----DDPGGWSSWGGN 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 332 PYETFGCEKY--------MPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLD-----VSNEVD-------HVFWRKFREE 391
Cdd:cd11316   134 VWHKAGDGGYyygafwsgMPDLNLDNPAVREEIKKIAKFWL-DKGVDGFRLDaakhiYENGEGqadqeenIEFWKEFRDY 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 392 VKKVKPDIYILGEIWHGS---LPWLmGDQFDSVMNYLMSEAMKKFFCTDEINAEEFKYmINDVMVSYPIQVSEVIF-NLL 467
Cdd:cd11316   213 VKSVKPDAYLVGEVWDDPstiAPYY-ASGLDSAFNFDLAEAIIDSVKNGGSGAGLAKA-LLRVYELYAKYNPDYIDaPFL 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 468 GSHDTTRILTYANGNIDRFKLA---YMFMfvqTGCPCIYYGDEIGMEGelSSISEGQRKCMEWNEE------KWNKD--- 535
Cdd:cd11316   291 SNHDQDRVASQLGGDEAKAKLAaalLLTL---PGNPFIYYGEEIGMLG--SKPDENIRTPMSWDADsgagftTWIPPrpn 365
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2053295504 536 -----------------IFDFMKKIIRLRKENKELR 554
Cdd:cd11316   366 tnattasveaqeadpdsLLNHYKRLIALRNEYPALA 401
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
174-548 5.85e-63

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: 213.61  E-value: 5.85e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 174 KDTVwYQIFPDRFANGDPSINP-----EGVDkwgaiptRDNFT---GGDLQGVIEHLDYLSDLGINGIYFCPITigkTN- 244
Cdd:cd11340     3 SDVI-YLIMPDRFANGDPSNDSvpgmlEKAD-------RSNPNgrhGGDIQGIIDHLDYLQDLGVTAIWLTPLL---ENd 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 245 ------HRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYY--------SKQWQDVVQNKENSRYKNW 310
Cdd:cd11340    72 mpsysyHGYAATDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSEhwwmkdlpTKDWINQTPEYTQTNHRRT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 311 fyikdmSKIDTPIEQIDEKNIPYETFGceKYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFRE 390
Cdd:cd11340   152 ------ALQDPYASQADRKLFLDGWFV--PTMPDLNQRNPLVARYLIQNSIWWIEYAGLDGIRVDTYPYSDKDFMSEWTK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 391 EVKKVKPDIYILGEIWHGSLP----WLMG----DQFDS----VMNYLMSEAMKKFFctdeiNAEE---------FKYMIN 449
Cdd:cd11340   224 AIMEEYPNFNIVGEEWSGNPAivayWQKGkknpDGYDShlpsVMDFPLQDALRDAL-----NEEEgwdtglnrlYETLAN 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 450 DVMvsYPIQVSEVIFnlLGSHDTTRILTYANGNIDRFKLAYMFMFVQTGCPCIYYGDEIGMEGELSSISEGQRKCME--W 527
Cdd:cd11340   299 DFL--YPDPNNLVIF--LDNHDTSRFYSQVGEDLDKFKLALALLLTTRGIPQLYYGTEILMKGTKKKDDGAIRRDFPggW 374
                         410       420       430
                  ....*....|....*....|....*....|..
gi 2053295504 528 NEEKWN-----------KDIFDFMKKIIRLRK 548
Cdd:cd11340   375 AGDKVNaftaagrtpeqNEAFDFVRKLLNWRK 406
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
179-550 1.69e-60

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: 205.18  E-value: 1.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 179 YQIFPDRFANGDPSINPEGVDKWGAIPTRDN--FTGGDLQGVIEHLDYLSDLGINGIYFCPITigkTN----------HR 246
Cdd:cd11339     6 YFVMTDRFYDGDPSNDNGGGDGDPRSNPTDNgpYHGGDFKGLIDKLDYIKDLGFTAIWITPVV---KNrsvqagsagyHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 247 YDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGyyskqwqDvvqnkensryknwfyikdmskidtpieqi 326
Cdd:cd11339    83 YWGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG-------D----------------------------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 327 deknipyetfgcekympkLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVSNEVDHVFWRKFREEVKK--VKPDIYILGE 404
Cdd:cd11339   127 ------------------LNTENPEVVDYLIDAYKWWI-DTGVDGFRIDTVKHVPREFWQEFAPAIRQaaGKPDFFMFGE 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 405 IWHG----SLPWLMGDQFDSVMNYLMSEAMKKFFCTDEINAEEFKYMIND-------VMVSYpiqvsevifnlLGSHDTT 473
Cdd:cd11339   188 VYDGdpsyIAPYTTTAGGDSVLDFPLYGAIRDAFAGGGSGDLLQDLFLSDdlyndatELVTF-----------LDNHDMG 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 474 RILTYANGN----IDRFKLAYMFMFVQTGCPCIYYGDEIGMEG--------ELSSISEGQRKCMEWNEEKwNKDIFDFMK 541
Cdd:cd11339   257 RFLSSLKDGsadgTARLALALALLFTSRGIPCIYYGTEQGFTGggdpdngrRNMFASTGDLTSADDNFDT-DHPLYQYIA 335

                  ....*....
gi 2053295504 542 KIIRLRKEN 550
Cdd:cd11339   336 RLNRIRRAY 344
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
172-555 5.54e-59

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: 200.85  E-value: 5.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 172 WVKDTVWYQIFPDRFAngdpsinPEGvdkwgaiptrdnftggDLQGVIEHLDYLSDLGINGIYFCPI-TIGKTN------ 244
Cdd:cd11313     1 WLRDAVIYEVNVRQFT-------PEG----------------TFKAVTKDLPRLKDLGVDILWLMPIhPIGEKNrkgslg 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 245 HRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDvvqnkensrYKNWFYIkdmskidtpie 324
Cdd:cd11313    58 SPYAVKDYRAVNPEYGTLEDFKALVDEAHDRGMKVILDWVANHTAWDHPLVEE---------HPEWYLR----------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 325 qiDEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGE 404
Cdd:cd11313   118 --DSDGNITNKVFDWTDVADLDYSNPELRDYMIDAMKYWVREFDVDGFRCDVAWGVPLDFWKEARAELRAVKPDVFMLAE 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 405 iWHGSLPWLMGDQFDSVMNYLMSEAMKKFFcTDEINAEEFKYMINDVMVSYPiqVSEVIFNLLGSHDTTRILTYAnGNID 484
Cdd:cd11313   196 -AEPRDDDELYSAFDMTYDWDLHHTLNDVA-KGKASASDLLDALNAQEAGYP--KNAVKMRFLENHDENRWAGTV-GEGD 270
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053295504 485 RFKLAYMFMFVQTGCPCIYYGDEIGMEGELSSisegqrkcMEWNEEKWNK--DIFDFMKKIIRLRKENKELRS 555
Cdd:cd11313   271 ALRAAAALSFTLPGMPLIYNGQEYGLDKRPSF--------FEKDPIDWTKnhDLTDLYQKLIALKKENPALRG 335
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
177-504 9.43e-45

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: 160.03  E-value: 9.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 177 VWYQIFPDRFANGDPSinpegvdkwgaiptrDNFTGGDLQGVIEHLDYLSDLGINGIYFCPITIGKTNHRYDT----VDY 252
Cdd:cd00551     1 VIYQLFPDRFTDGDSS---------------GGDGGGDLKGIIDKLDYLKDLGVTAIWLTPIFESPEYDGYDKddgyLDY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 253 MEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHigyyskqwqdvvqnkensryknwfyikdmskidtpieqideknip 332
Cdd:cd00551    66 YEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH--------------------------------------------- 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 333 yetfgcekympklntensevikyllDVGKYWIqEFDIDAWRLD----VSNEVDHVFWRKFREEVKKVKPDIYILGEIWHG 408
Cdd:cd00551   101 -------------------------DILRFWL-DEGVDGFRLDaakhVPKPEPVEFLREIRKDAKLAKPDTLLLGEAWGG 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 409 SLPWL----MGDQFDSVMNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPiqvsevIFNLLGSHDTTRILTYANGNI- 483
Cdd:cd00551   155 PDELLakagFDDGLDSVFDFPLLEALRDALKGGEGALAILAALLLLNPEGAL------LVNFLGNHDTFRLADLVSYKIv 228
                         330       340
                  ....*....|....*....|....*
gi 2053295504 484 ----DRFKLAYMFMFVQTGCPCIYY 504
Cdd:cd00551   229 elrkARLKLALALLLTLPGTPMIYY 253
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
175-513 1.11e-42

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: 157.49  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 175 DTVWYQIFPDRFANGDPSINPEGVDKwgaiptrdnftGGDLQGVIEHLDYLSDLGINGIYFCPItIGKTNHRYDTVDYME 254
Cdd:cd11354     1 HAIWWHVYPLGFVGAPIRPREPEAAV-----------EHRLDRLEPWLDYAVELGCNGLLLGPV-FESASHGYDTLDHYR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 255 VDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKENSRYKNWFyikdmskidtpieqIDEKNIPYE 334
Cdd:cd11354    69 IDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALEDGPGSEEDRWH--------------GHAGGGTPA 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 335 TFGCEKYMPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIWHGSLPWLM 414
Cdd:cd11354   135 VFEGHEDLVELDHSDPAVVDMVVDVMCHWL-DRGIDGWRLDAAYAVPPEFWARVLPRVRERHPDAWILGEVIHGDYAGIV 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 415 GDQ-FDSVMNYLMSEAM------KKFFctdeinaeEFKYMI---NDVMVSYPIQvsevifNLLGSHDTTRILTYAnGNiD 484
Cdd:cd11354   214 AASgMDSVTQYELWKAIwssikdRNFF--------ELDWALgrhNEFLDSFVPQ------TFVGNHDVTRIASQV-GD-D 277
                         330       340
                  ....*....|....*....|....*....
gi 2053295504 485 RFKLAYMFMFVQTGCPCIYYGDEIGMEGE 513
Cdd:cd11354   278 GAALAAAVLFTVPGIPSIYYGDEQGFTGV 306
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
174-549 7.63e-42

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: 156.85  E-value: 7.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 174 KDTVWYQIFPDRFA--NGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPITI------Gktnh 245
Cdd:cd11333     1 KEAVVYQIYPRSFKdsNGD------GI--------------GDLPGIISKLDYLKDLGVDAIWLSPIYPspqvdnG---- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 246 rYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--W-QDVVQNKENSrYKNWFYIKD------- 315
Cdd:cd11333    57 -YDISDYRAIDPEFGTMEDFDELIKEAHKRGIKIIMDLVVNHT---SDEhpWfQESRSSRDNP-YRDYYIWRDgkdgkpp 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 316 ---MSKIDTPIEQIDEKNIPY--ETFGceKYMPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDV-----------SNE 379
Cdd:cd11333   132 nnwRSFFGGSAWEYDPETGQYylHLFA--KEQPDLNWENPEVRQEIYDMMRFWL-DKGVDGFRLDVinliskdpdfpDAP 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 380 VD-----------------HVFWRKFREEVKKvKPDIYILGEIWHGSLPWLM------GDQFDSVMNY---LMSEAMKKF 433
Cdd:cd11333   209 PGdgdglsghkyyangpgvHEYLQELNREVFS-KYDIMTVGEAPGVDPEEALkyvgpdRGELSMVFNFehlDLDYGPGGK 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 434 FCTDEINAEEFKYMINDVMVSYPIQVSEVIFnlLGSHDTTRILT-YANGNIDRF---KLAYMFMFVQTGCPCIYYGDEIG 509
Cdd:cd11333   288 WKPKPWDLEELKKILSKWQKALQGDGWNALF--LENHDQPRSVSrFGNDGEYRVesaKMLATLLLTLRGTPFIYQGEEIG 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2053295504 510 MEGelssiS-EGQRKCMEWNEEK---------W---NKD---------------IFDFMKKIIRLRKE 549
Cdd:cd11333   366 MTN-----SrDNARTPMQWDDSPnagfstgkpWlpvNPNykeinveaqladpdsVLNFYKKLIALRKE 428
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
174-548 1.09e-41

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: 155.52  E-value: 1.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 174 KDTVwYQIFPDRFANGDPSINPEGVDKwGAIPTRDNF---TGGDLQGVIEHLDYLSDLGINGIYFCP--------ITIGK 242
Cdd:cd11320     4 TDVI-YQILTDRFYDGDTSNNPPGSPG-LYDPTHSNLkkyWGGDWQGIIDKLPYLKDLGVTAIWISPpveninspIEGGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 243 TN--HRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKqwqdvvqnKENSR-YKNWFYIKDMSKI 319
Cdd:cd11320    82 NTgyHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPADY--------AEDGAlYDNGTLVGDYPND 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 320 DTPIEQ----IDEKNIPYETFGCEKY-MPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVSNEVDHVFWRKFREEVkK 394
Cdd:cd11320   154 DNGWFHhnggIDDWSDREQVRYKNLFdLADLNQSNPWVDQYLKDAIKFWL-DHGIDGIRVDAVKHMPPGWQKSFADAI-Y 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 395 VKPDIYILGEIWHGSLPWLMGDQFD-------SVMNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPIQVSEVIFnlL 467
Cdd:cd11320   232 SKKPVFTFGEWFLGSPDPGYEDYVKfannsgmSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTF--I 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 468 GSHDTTRILTYaNGNIDRFKLAYMFMFVQTGCPCIYYGDEIGMEGELSSISE-GQRKCME-WNEekwNKDIFDFMKKIIR 545
Cdd:cd11320   310 DNHDMPRFLTL-NNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGTQVGGDpYNRPMMPsFDT---TTTAYKLIKKLAD 385

                  ...
gi 2053295504 546 LRK 548
Cdd:cd11320   386 LRK 388
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
179-512 1.54e-41

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: 154.65  E-value: 1.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 179 YQIFPDRFANGDPSINPEgvdkwgAIPTRDNFTGGDLQGVIEHLDYLSDLGINGIYFCPIT--IGKTN------HRYDTV 250
Cdd:cd11319    12 YQVLTDRFARTDGSSTAP------CDTADRTYCGGTWKGIINKLDYIQGMGFDAIWISPIVknIEGNTaygeayHGYWAQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 251 DYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSK-QWQDVVQ----NKEnSRYKNWFYIKDMSKIdTPIEQ 325
Cdd:cd11319    86 DLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPgSDVDYSSfvpfNDS-SYYHPYCWITDYNNQ-TSVED 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 326 --IDEKNIPyetfgcekyMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVkkvkpDIYILG 403
Cdd:cd11319   164 cwLGDDVVA---------LPDLNTENPFVVSTLNDWIKNLVSNYSIDGLRIDTAKHVRKDFWPGFVEAA-----GVFAIG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 404 EIWHGSLPWLMGDQ--FDSVMNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPiqVSEVIFNLLGSHDTTRILTYaNG 481
Cdd:cd11319   230 EVFDGDPNYVCPYQnyLDGVLNYPLYYPLVDAFQSTKGSMSALVDTINSVQSSCK--DPTLLGTFLENHDNPRFLSY-TS 306
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2053295504 482 NIDRFKLAYMFMFVQTGCPCIYYGDEIGMEG 512
Cdd:cd11319   307 DQALAKNALAFTLLSDGIPIIYYGQEQGFNG 337
Aamy smart00642
Alpha-amylase domain;
180-358 6.88e-37

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 135.15  E-value: 6.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  180 QIFPDRFANGDPSinpegvdkwgaiptrdnfTGGDLQGVIEHLDYLSDLGINGIYFCPIT----IGKTNHRYDTVDYMEV 255
Cdd:smart00642   1 QIYPDRFADGNGD------------------GGGDLQGIIEKLDYLKDLGVTAIWLSPIFespqGYPSYHGYDISDYKQI 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  256 DPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWqDVVQ---NKENSRYKNWFYIKDMSKIDTpIEQIDEKNIP 332
Cdd:smart00642  63 DPRFGTMEDFKELVDAAHARGIKVILDVVINHTSDGGFRL-DAAKfplNGSAFSLLDFFALALLLKILG-IGMTNLPIID 140
                          170       180
                   ....*....|....*....|....*.
gi 2053295504  333 YETFGCEKYMPKLNTENSEVIKYLLD 358
Cdd:smart00642 141 YEQYRDGGGDPNMWWDGTCQWREITK 166
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
172-531 1.38e-33

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: 133.84  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 172 WVKDTVWYQIFPDRF--ANGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPI--TIGKTNHrY 247
Cdd:cd11334     1 WYKNAVIYQLDVRTFmdSNGD------GI--------------GDFRGLTEKLDYLQWLGVTAIWLLPFypSPLRDDG-Y 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 248 DTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--W-QDVVQNKeNSRYKNWFYIKdmskiDTPIE 324
Cdd:cd11334    60 DIADYYGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHT---SDQhpWfQAARRDP-DSPYRDYYVWS-----DTPPK 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 325 QIDEKNI--PYET----------------FgcEKYMPKLNTENSEVIKYLLDVGKYWIQeFDIDAWRLD----------- 375
Cdd:cd11334   131 YKDARIIfpDVEKsnwtwdevagayywhrF--YSHQPDLNFDNPAVREEILRIMDFWLD-LGVDGFRLDavpylieregt 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 376 -VSNEVD-HVFWRKFREEVKKVKPDIYILGEI--WHGSLPWLMGD------QFD-SVMNYL-MSEAMKKFFCT------- 436
Cdd:cd11334   208 nCENLPEtHDFLKRLRAFVDRRYPDAILLAEAnqWPEEVREYFGDgdelhmAFNfPLNPRLfLALAREDAFPIidalrqt 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 437 ----------------DEIN-----AEEFKYMindvMVSYPIQVSEVIFNlLGSHdtTRILTYANGNIDRFKLAYMFMFV 495
Cdd:cd11334   288 ppipegcqwanflrnhDELTlemltDEERDYV----YAAFAPDPRMRIYN-RGIR--RRLAPMLGGDRRRIELAYSLLFS 360
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 2053295504 496 QTGCPCIYYGDEIGMeGELSSISE--GQRKCMEWNEEK 531
Cdd:cd11334   361 LPGTPVIYYGDEIGM-GDNLYLPDrdGVRTPMQWSADR 397
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
207-555 3.25e-32

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: 128.55  E-value: 3.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 207 RDnFTG-GDLQGVIEHLDYLSDLGINGIYFCPIT--IGKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDA 283
Cdd:cd11350    24 RD-FTErGDFKGVIDKLDYLQDLGVNAIELMPVQefPGNDSWGYNPRHYFALDKAYGTPEDLKRLVDECHQRGIAVILDV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 284 VFNHIGY---YSKQWQDvvqnkensrykNWFYikdmskidTPIEQIDEKNIPYETFGCEKYmpKLNTENSEVIKYLLDVG 360
Cdd:cd11350   103 VYNHAEGqspLARLYWD-----------YWYN--------PPPADPPWFNVWGPHFYYVGY--DFNHESPPTRDFVDDVN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 361 KYWIQEFDIDAWRLDVS------------------NEVDhvFWRKFREEVKKVKPDIYILGEIW-----------HGSLP 411
Cdd:cd11350   162 RYWLEEYHIDGFRFDLTkgftqkptgggawggydaARID--FLKRYADEAKAVDKDFYVIAEHLpdnpeetelatYGMSL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 412 W--LMGDQFDSVMNYLMSEAMKKFFctdeINAEEFKYMINDVMVSYpiqvsevifnlLGSHDTTRI----LTYANGN--- 482
Cdd:cd11350   240 WgnSNYSFSQAAMGYQGGSLLLDYS----GDPYQNGGWSPKNAVNY-----------MESHDEERLmyklGAYGNGNsyl 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 483 -------IDRFKLAYMFMFVQTGCPCIYYGDEIGMEgelSSISEGQRKCMEWNEEKW-------NKDIFDFMKKIIRLRK 548
Cdd:cd11350   305 ginletaLKRLKLAAAFLFTAPGPPMIWQGGEFGYD---YSIPEDGRGTTLPKPIRWdylydpeRKRLYELYRKLIKLRR 381

                  ....*..
gi 2053295504 549 ENKELRS 555
Cdd:cd11350   382 EHPALRT 388
malS PRK09505
alpha-amylase; Reviewed
167-529 7.62e-31

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 128.25  E-value: 7.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 167 PKVP-NWVKDTVwYQIFPDRFANGDPS-INPEGVDKWGA--IPTrdnFTGGDLQGVIEHLDYLSDLGINGIYFCPI---- 238
Cdd:PRK09505  181 AAAPfDWHNATV-YFVLTDRFENGDPSnDHSYGRHKDGMqeIGT---FHGGDLRGLTEKLDYLQQLGVNALWISSPleqi 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 239 ---TIGKTN--------HRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGY--------------YSK 293
Cdd:PRK09505  257 hgwVGGGTKgdfphyayHGYYTLDWTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTGYatladmqefqfgalYLS 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 294 -------------QWQ-----------DVVQNKENSRYKNWfYIKDMSKIDTPieqiDEKNIPYETF-GCEKYMPKLNTE 348
Cdd:PRK09505  337 gdenkktlgerwsDWQpaagqnwhsfnDYINFSDSTAWDKW-WGKDWIRTDIG----DYDNPGFDDLtMSLAFLPDIKTE 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 349 NSEVIK-----------------------YLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFR-------EEVKKVKPD 398
Cdd:PRK09505  412 STQASGlpvfyankpdtrakaidgytprdYLTHWLSQWVRDYGIDGFRVDTAKHVELPAWQQLKqeasaalAEWKKANPD 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 399 -------IYILGEIW-HGSL--PWLMgDQFDSVMNYLMSEAMKKffctdeiNAEEFKYMiNDVMVSYPIQVSEviFNLL- 467
Cdd:PRK09505  492 kalddapFWMTGEAWgHGVMksDYYR-HGFDAMINFDYQEQAAK-------AVDCLAQM-DPTYQQMAEKLQD--FNVLs 560
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2053295504 468 --GSHDtTRILTYANGNIDRFKLAYMFMFVQTGCPCIYYGDEIGMEGE--LSSISEGQRKCMEWNE 529
Cdd:PRK09505  561 ylSSHD-TRLFFEGGQSYAKQRRAAELLLLAPGAVQIYYGDESARPFGptGSDPLQGTRSDMNWQE 625
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
177-546 1.69e-30

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: 124.74  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 177 VWYQIFPDRFANG--DPSINPEGVDKWGAiPTRDN---------FTGGDLQGVIEHLDYLSDLGINGIYFCPI----TIG 241
Cdd:cd11352     1 VLYFLLVDRFSDGkeRPRPLFDGNDPAVA-TWEDNfgwesqgqrFQGGTLKGVRSKLGYLKRLGVTALWLSPVfkqrPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 242 KTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIG---YYSKQWQDVVQNKENSRYKN-WFYIKDMS 317
Cdd:cd11352    80 ETYHGYGIQNFLDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSGdvfSYDDDRPYSSSPGYYRGFPNyPPGGWFIG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 318 KIDTPIEQIDEKN--IPYETFGCEKYMPK----------------------LNTEN----SEVIKYLLDVGKYWIQEFDI 369
Cdd:cd11352   160 GDQDALPEWRPDDaiWPAELQNLEYYTRKgrirnwdgypeykegdffslkdFRTGSgsipSAALDILARVYQYWIAYADI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 370 DAWRLDVSNEVDHVFWRKFREEVKKV-----KPDIYILGEIWHGS--LPWLMGDQ--------FDSVMNYLmsEAMKKFF 434
Cdd:cd11352   240 DGFRIDTVKHMEPGAARYFCNAIKEFaqsigKDNFFLFGEITGGReaAAYEDLDVtgldaaldIPEIPFKL--ENVAKGL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 435 CTDEINAEEFKYMINDVMVSYpIQVSEVIFNLLGSHDTTRILTY----ANGNIDRFKLAYMFMFVQT-GCPCIYYGDEIG 509
Cdd:cd11352   318 APPAEYFQLFENSKLVGMGSH-RWYGKFHVTFLDDHDQVGRFYKkrraADAAGDAQLAAALALNLFTlGIPCIYYGTEQG 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2053295504 510 MEGELSS---ISEG----------QRKCMEWNEEKWnkdIFDFMKKIIRL 546
Cdd:cd11352   397 LDGSGDSdryVREAmfggdfgafrSRGRHFFNEEHP---IYRRIAALSEL 443
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
172-511 6.75e-30

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: 122.82  E-value: 6.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 172 WVKDTVWYQIFPDRF--ANGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPI------TIGkt 243
Cdd:cd11331     2 WWQTGVIYQIYPRSFqdSNGD------GV--------------GDLRGIISRLDYLSDLGVDAVWLSPIypspmaDFG-- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 244 nhrYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--W-QDVVQNKENSRyKNWFYIKD----- 315
Cdd:cd11331    60 ---YDVSDYCGIDPLFGTLEDFDRLVAEAHARGLKVILDFVPNHT---SDQhpWfLESRSSRDNPK-RDWYIWRDpapdg 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 316 ------MSKIDTPIEQIDEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIQEfDIDAWRLDV------------- 376
Cdd:cd11331   133 gppnnwRSEFGGSAWTWDERTGQYYLHAFLPEQPDLNWRNPEVRAAMHDVLRFWLDR-GVDGFRVDVlwllikdpqfrdn 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 377 ----------------------SNEVDHVFWRKFREEVKKVkPDIYILGEIwHGSLPWLM------GDQFDSVMNYLMSE 428
Cdd:cd11331   212 ppnpdwrggmppherllhiytaDQPETHEIVREMRRVVDEF-GDRVLIGEI-YLPLDRLVayygagRDGLHLPFNFHLIS 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 429 AmkkffctdEINAEEFKYMINDVMVSYPIQVSEvifN-LLGSHDTTRILTYANGniDRFKLAYMFMFVQTGCPCIYYGDE 507
Cdd:cd11331   290 L--------PWDAAALARAIEEYEAALPAGAWP---NwVLGNHDQPRIASRVGP--AQARVAAMLLLTLRGTPTLYYGDE 356

                  ....
gi 2053295504 508 IGME 511
Cdd:cd11331   357 LGME 360
Alpha-amylase_N pfam02903
Alpha amylase, N-terminal ig-like domain;
25-162 7.27e-30

Alpha amylase, N-terminal ig-like domain;


Pssm-ID: 397170  Cd Length: 120  Bit Score: 113.94  E-value: 7.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  25 KEAILHIPMSNYAYGYDRETLHIRLRTKKNEAKRVILRIGDQYVWDKggagggnlnasgvGWSGGTnIVMSKEVETELFD 104
Cdd:pfam02903   3 LEAIYHRPESEYAYAYNGNTLHIRLRTKKDDVERVYLIYGDPYEWDG-------------KWYSET-APMKKIGSDELFD 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2053295504 105 YWIAKCKPLNKRSRYGFIIEGQEEKLLFTEKriielgNENDEKELCEIGNFFGYPYLN 162
Cdd:pfam02903  69 YWEAELTPPYKRLRYGFELEGDGESLVYGEK------GFYDEAPLDDTGGYFQFPYIH 120
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
159-554 1.67e-29

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


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 125.00  E-value: 1.67e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  159 PYLNYIDIPkvpNWVKDTvwyqIFPDRFANGDPSI------NPEGV--DKWGAIPT----------------------RD 208
Cdd:PRK14510   101 PYARPLDRP---FWLHQA----IFDDRFFNGDEDLtdsavlVPKVVvpTPFTWAPRsplhgdwddsplyemnvrgftlRH 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  209 NFTGGDLQGVI------EHLDYLSDLGINGIYFCPITIGKTNHR-----------YDTVDYMEVDPTLG--DKETLKKLI 269
Cdd:PRK14510   174 DFFPGNLRGTFaklaapEAISYLKKLGVSIVELNPIFASVDEHHlpqlglsnywgYNTVAFLAPDPRLApgGEEEFAQAI 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  270 EEAHKRNIKIMLDAVFNHIGyyskqwqdvvqnkENSRYKNWFYIKDMSkiDTPIEQIDEKN-IPYETF-GCEKYmpkLNT 347
Cdd:PRK14510   254 KEAQSAGIAVILDVVFNHTG-------------ESNHYGPTLSAYGSD--NSPYYRLEPGNpKEYENWwGCGNL---PNL 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  348 ENSEVIKYLLDVGKYWIQeFDIDAWRLDVSNEVDHV---FWRKFREEVKKVKPDiYILGEIWHGSLPWLMGDQFDSV--- 421
Cdd:PRK14510   316 ERPFILRLPMDVLRSWAK-RGVDGFRLDLADELAREpdgFIDEFRQFLKAMDQD-PVLRRLKMIAEVWDDGLGGYQYgkf 393
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  422 ------MNYLMSEAMKKFFCTDEINAEEFKYMINDVMVSYPIQ---VSEVIfNLLGSHDTTRILT---------YANGNI 483
Cdd:PRK14510   394 pqywgeWNDPLRDIMRRFWLGDIGMAGELATRLAGSADIFPHRrrnFSRSI-NFITAHDGFTLLDlvsfnhkhnEANGED 472
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  484 DR-----------------------------FKLAYMFMFVQTGCPCIYYGDEIGMEGELSSISEGQ---RKCMEWNEEk 531
Cdd:PRK14510   473 NRdgtpdnqswncgvegytldaairslrrrrLRLLLLTLMSFPGVPMLYYGDEAGRSQNGNNNGYAQdnnRGTYPWGNE- 551
                          490       500
                   ....*....|....*....|...
gi 2053295504  532 wNKDIFDFMKKIIRLRKENKELR 554
Cdd:PRK14510   552 -DEELLSFFRRLIKLRREYGVLR 573
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
177-531 3.48e-28

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: 117.41  E-value: 3.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 177 VWYQIFPDRFA--NGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPI------TIGktnhrYD 248
Cdd:cd11348     1 VFYEIYPQSFYdsNGD------GI--------------GDLQGIISKLDYIKSLGCNAIWLNPCfdspfkDAG-----YD 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 249 TVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--WQDVVQNKENSRYKNWFYIKDMSKIDTP---- 322
Cdd:cd11348    56 VRDYYKVAPRYGTNEDLVRLFDEAHKRGIHVLLDLVPGHT---SDEhpWFKESKKAENNEYSDRYIWTDSIWSGGPglpf 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 323 IEQIDEKNIPYET--FGCEkymPKLNTENSEVIKY-----------------LLDVGKYWIqEFDIDAWRLD-----VSN 378
Cdd:cd11348   133 VGGEAERNGNYIVnfFSCQ---PALNYGFAHPPTEpwqqpvdapgpqatreaMKDIMRFWL-DKGADGFRVDmadslVKN 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 379 EVDHV----FWRKFREEVKKVKPDIYILGEiWHG---SLPwlMGDQFDSVMNYLMSEAMKKFFCTDEINAEE-----F-- 444
Cdd:cd11348   209 DPGNKetikLWQEIRAWLDEEYPEAVLVSE-WGNpeqSLK--AGFDMDFLLHFGGNGYNSLFRNLNTDGGHRrdncyFda 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 445 ------KYMINDVMVSYPIQVSEVIFNLL-GSHDTTRILtyANGNIDRFKLAYMFMFVQTGCPCIYYGDEIGME-GELSS 516
Cdd:cd11348   286 sgkgdiKPFVDEYLPQYEATKGKGYISLPtCNHDTPRLN--ARLTEEELKLAFAFLLTMPGVPFIYYGDEIGMRyIEGLP 363
                         410       420
                  ....*....|....*....|.
gi 2053295504 517 ISE------GQRKCMEWNEEK 531
Cdd:cd11348   364 SKEggynrtGSRTPMQWDSGK 384
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
171-514 6.54e-28

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: 117.36  E-value: 6.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 171 NWVKDTVWYQIFPDRFA--NGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPI------TIGk 242
Cdd:cd11330     1 PWWRGAVIYQIYPRSFLdsNGD------GI--------------GDLPGITEKLDYIASLGVDAIWLSPFfkspmkDFG- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 243 tnhrYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--W-QDVVQNKENSRyKNWFYIKDMSKI 319
Cdd:cd11330    60 ----YDVSDYCAVDPLFGTLDDFDRLVARAHALGLKVMIDQVLSHT---SDQhpWfEESRQSRDNPK-ADWYVWADPKPD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 320 DTPieqideKNIPYETFG----------CEKYM-------PKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVSNEVDH 382
Cdd:cd11330   132 GSP------PNNWLSVFGgsawqwdprrGQYYLhnflpsqPDLNFHNPEVQDALLDVARFWL-DRGVDGFRLDAVNFYMH 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 383 ----------------------------------------VFWRKFREEVKKVkPDIYILGEIwHGSLPWLM-------G 415
Cdd:cd11330   205 dpalrdnpprppderedgvaptnpygmqlhihdksqpenlAFLERLRALLDEY-PGRFLVGEV-SDDDPLEVmaeytsgG 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 416 DQFDSVMNYLMSEAmkkffctdEINAEEFKYMINDVMVSYPIQVSEVIFnllGSHDTTRILTYANGNIDRFKLAYMFMFV 495
Cdd:cd11330   283 DRLHMAYSFDLLGR--------PFSAAVVRDALEAFEAEAPDGWPCWAF---SNHDVPRAVSRWAGGADDPALARLLLAL 351
                         410       420
                  ....*....|....*....|...
gi 2053295504 496 QT---GCPCIYYGDEIGM-EGEL 514
Cdd:cd11330   352 LLslrGSVCLYQGEELGLpEAEL 374
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
170-511 7.87e-27

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: 114.25  E-value: 7.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 170 PNWVKDTVWYQIFPDRF--ANGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPI-TIGKTNHR 246
Cdd:cd11328     2 KDWWENAVFYQIYPRSFkdSDGD------GI--------------GDLKGITEKLDYFKDIGIDAIWLSPIfKSPMVDFG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 247 YDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKEnsRYKNwFYIKDMSKIDTpieqi 326
Cdd:cd11328    62 YDISDFTDIDPIFGTMEDFEELIAEAKKLGLKVILDFVPNHSSDEHEWFQKSVKRDE--PYKD-YYVWHDGKNND----- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 327 DEKNIP-----------------------YETFgcEKYMPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLD-------- 375
Cdd:cd11328   134 NGTRVPpnnwlsvfggsawtwneerqqyyLHQF--AVKQPDLNYRNPKVVEEMKNVLRFWL-DKGVDGFRIDavphlfed 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 376 -------VSNEV----------DHVF-------------WRKFREEVKKVK--PDIYILGEIWHGslpwlmgdqFDSVMN 423
Cdd:cd11328   211 edfldepYSDEPgadpddydylDHIYtkdqpetydlvyeWREVLDEYAKENngDTRVMMTEAYSS---------LDNTMK 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 424 YLMSEAMKK-------FFCTD---EINAEEFKYMINDVMVSYPiqvSEVIFN-LLGSHDTTRILTYANGniDRFKLAYMF 492
Cdd:cd11328   282 YYGNETTYGahfpfnfELITNlnkNSNATDFKDLIDKWLDNMP---EGQTANwVLGNHDNPRVASRFGE--ERVDGMNML 356
                         410
                  ....*....|....*....
gi 2053295504 493 MFVQTGCPCIYYGDEIGME 511
Cdd:cd11328   357 SMLLPGVAVTYYGEEIGME 375
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
168-380 8.17e-24

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 105.60  E-value: 8.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 168 KVPNWVKDTVWYQIFPDRFANgdpsinpegvdkwgaipTRDNFTGgDLQGVIEHLDYLSDLGINGIYFCPITIG-KTNHR 246
Cdd:PRK10933    3 NLPHWWQNGVIYQIYPKSFQD-----------------TTGSGTG-DLRGVTQRLDYLQKLGVDAIWLTPFYVSpQVDNG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 247 YDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--WQDVVQNKeNSRYKNwFYI-KD-------- 315
Cdd:PRK10933   65 YDVANYTAIDPTYGTLDDFDELVAQAKSRGIRIILDMVFNHT---STQhaWFREALNK-ESPYRQ-FYIwRDgepetppn 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2053295504 316 --MSKIDTPIEQIDEKNIPY--ETFGCEKymPKLNTENSEVIKYLLDVGKYWiQEFDIDAWRLDVSNEV 380
Cdd:PRK10933  140 nwRSKFGGSAWRWHAESEQYylHLFAPEQ--ADLNWENPAVRAELKKVCEFW-ADRGVDGLRLDVVNLI 205
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
172-530 9.05e-24

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: 104.75  E-value: 9.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 172 WVKDTVWYQIFPDRF--ANGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPITIG-KTNHRYD 248
Cdd:cd11359     2 WWQTSVIYQIYPRSFkdSNGD------GN--------------GDLKGIREKLDYLKYLGVKTVWLSPIYKSpMKDFGYD 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 249 TVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIG------------------YYSkqWQDVVQNKENSRYKNW 310
Cdd:cd11359    62 VSDFTDIDPMFGTMEDFERLLAAMHDRGMKLIMDFVPNHTSdkhewfqlsrnstnpytdYYI--WADCTADGPGTPPNNW 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 311 fyikdMSKIDTPIEQIDEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLDVsneVDHVFWRK-FR 389
Cdd:cd11359   140 -----VSVFGNSAWEYDEKRNQCYLHQFLKEQPDLNFRNPDVQQEMDDVLRFWL-DKGVDGFRVDA---VKHLLEAThLR 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 390 EE--VKKVKPD--IYILGEIWHGSLPWLMG-----DQFDSVMNYLMSEAMKKFFCTDEIN--------------AEEFKY 446
Cdd:cd11359   211 DEpqVNPTQPPetQYNYSELYHDYTTNQEGvhdiiRDWRQTMDKYSSEPGRYRFMITEVYddidttmryygtsfKQEADF 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 447 MINDVMVSYP-----IQVSEVIFN-------------LLGSHDTTRILTYAnGNiDRFKLAYMFMFVQTGCPCIYYGDEI 508
Cdd:cd11359   291 PFNFYLLDLGanlsgNSINELVESwmsnmpegkwpnwVLGNHDNSRIASRL-GP-QYVRAMNMLLLTLPGTPTTYYGEEI 368
                         410       420       430
                  ....*....|....*....|....*....|...
gi 2053295504 509 GME---GELSSISEG--------QRKCMEWNEE 530
Cdd:cd11359   369 GMEdvdISVDKEKDPytfesrdpERTPMQWNNS 401
E_set_CDase_PDE_N cd02857
N-terminal Early set domain associated with the catalytic domain of cyclomaltodextrinase and ...
28-160 1.50e-22

N-terminal Early set domain associated with the catalytic domain of cyclomaltodextrinase and pullulan-degrading enzymes; E or "early" set domains are associated with the catalytic domain of the cyclomaltodextrinase (CDase) and pullulan-degrading enzymes at the N-terminal end. Members of this subgroup include CDase, maltogenic amylase, and neopullulanase, all of which are capable of hydrolyzing all or two of the following three types of substrates: 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. The N-terminal domain of the CDase and pullulan-degrading enzymes may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199887 [Multi-domain]  Cd Length: 109  Bit Score: 92.77  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  28 ILHIPMS-NYAYGYDRETLHIRLRTKKNEAKRVILRIGDQYVWdkggagggnlnasgvgwsGGTNIVMSKEVETELFDYW 106
Cdd:cd02857     1 IYHDPTSyAYAYPGAGDTVTIRLRTAKDDVDSVFLRYGDDYDG------------------EEKLVPMKKVGSDGLFDYY 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053295504 107 IAKCKPLNKRSRYGFIIEGQEEKLLFTEKRIIELGNENDekelceiGNFFGYPY 160
Cdd:cd02857    63 EAEIPLPEKRLRYYFELEDGGETLYYGERGVSEEGPDDD-------SYYFQIPY 109
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
172-522 5.92e-22

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: 99.27  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 172 WVKDTVWYQIFPDRFA--NGDpsinpeGVdkwgaiptrdnftgGDLQGVIEHLDYLSDLGINGIYFCPITI-GKTNHRYD 248
Cdd:cd11332     2 WWRDAVVYQVYPRSFAdaNGD------GI--------------GDLAGIRARLPYLAALGVDAIWLSPFYPsPMADGGYD 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 249 TVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQ--W-----QDVVQNKENSRY-------------- 307
Cdd:cd11332    62 VADYRDVDPLFGTLADFDALVAAAHELGLRVIVDIVPNHT---SDQhpWfqaalAAGPGSPERARYifrdgrgpdgelpp 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 308 KNWfyikdMSKIDTPI-EQIDEkniPYETFGcEKYM-------PKLNTENSEVIKYLLDVGKYWiqeFD--IDAWRLDVS 377
Cdd:cd11332   139 NNW-----QSVFGGPAwTRVTE---PDGTDG-QWYLhlfapeqPDLNWDNPEVRAEFEDVLRFW---LDrgVDGFRIDVA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 378 N---------------------EVDHVFWRkfREEVKKV-----------KPDIYILGEIWHGSLpwlmgdqfDSVMNYL 425
Cdd:cd11332   207 HglakdpglpdapggglpvgerPGSHPYWD--RDEVHDIyrewravldeyDPPRVLVAEAWVPDP--------ERLARYL 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 426 MSEAMKKFFCTD----EINAEEFKYMINDVMVSYPIQVSEVIFnLLGSHDTTRILT--------YANGNID--------- 484
Cdd:cd11332   277 RPDELHQAFNFDflkaPWDAAALRRAIDRSLAAAAAVGAPPTW-VLSNHDVVRHVSryglptpgPDPSGIDgtdeppdla 355
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 2053295504 485 ----RFKLAYMFMFVQTGCPCIYYGDEIGMEgELSSISEGQR 522
Cdd:cd11332   356 lglrRARAAALLMLALPGSAYLYQGEELGLP-EVEDLPDALR 396
AmyAc_GTHase cd11325
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called ...
190-375 9.39e-18

Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase); Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase


Pssm-ID: 200464 [Multi-domain]  Cd Length: 436  Bit Score: 86.06  E-value: 9.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 190 DPSINPEGVDKWGAIPTRD---------NFTG-GDLQGVIEHLDYLSDLGINGIYFCPIT--IGKTNHRYDTVDYMEVDP 257
Cdd:cd11325    19 DPSAFWWTDAGWRGPPLEElviyelhvgTFTPeGTFDAAIERLDYLADLGVTAIELMPVAefPGERNWGYDGVLPFAPES 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 258 TLGDKETLKKLIEEAHKRNIKIMLDAVFNHIG----YyskQWQDvvqnkensrYKNWFYikdmSKIDTPieqideknipy 333
Cdd:cd11325    99 SYGGPDDLKRLVDAAHRRGLAVILDVVYNHFGpdgnY---LWQF---------AGPYFT----DDYSTP----------- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2053295504 334 etFGcekymPKLN--TENSEVIKYLLDVGKYWIQEFDIDAWRLD 375
Cdd:cd11325   152 --WG-----DAINfdGPGDEVRQFFIDNALYWLREYHVDGLRLD 188
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
214-313 1.08e-16

malto-oligosyltrehalose synthase;


Pssm-ID: 237740 [Multi-domain]  Cd Length: 879  Bit Score: 84.26  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 214 DLQGVIEHLDYLSDLGINGIYFCPI---TIGKTnHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGY 290
Cdd:PRK14511   18 TFDDAAELVPYFADLGVSHLYLSPIlaaRPGST-HGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAV 96
                          90       100
                  ....*....|....*....|....*.
gi 2053295504 291 YSKQ---WQDVVQNKENSRYKNWFYI 313
Cdd:PRK14511   97 GGPDnpwWWDVLEWGRSSPYADFFDI 122
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
218-311 1.76e-16

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: 82.93  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 218 VIEHLDYLSDLGINGIYFCPITI---GKTnHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQ 294
Cdd:cd11336    16 AAALVPYLADLGISHLYASPILTarpGST-HGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVSGAE 94
                          90       100
                  ....*....|....*....|
gi 2053295504 295 ---WQDVVQNKENSRYKNWF 311
Cdd:cd11336    95 npwWWDVLENGPDSPYAGFF 114
TreY COG3280
Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];
220-313 3.07e-16

Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];


Pssm-ID: 442511 [Multi-domain]  Cd Length: 915  Bit Score: 82.55  E-value: 3.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 220 EHLDYLSDLGINGIYFCPI---TIGKTnHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYS--KQ 294
Cdd:COG3280    23 ALVPYLARLGISHLYASPIlkaRPGST-HGYDVVDHNRINPELGGEEGFERLVAALRAHGMGLILDIVPNHMAVGPdnPW 101
                          90
                  ....*....|....*....
gi 2053295504 295 WQDVVQNKENSRYKNWFYI 313
Cdd:COG3280   102 WWDVLENGPASPYADFFDI 120
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
222-549 7.02e-15

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: 77.74  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 222 LDYLSDLGINGIYFCPI----------TIGKTNHRYDTVDYM---------EVDPTLGDKEtLKKLIEEAHKRNIKIMLD 282
Cdd:TIGR02104 170 LDYLKELGVTHVQLLPVfdfagvdeedPNNAYNWGYDPLNYNvpegsystnPYDPATRIRE-LKQMIQALHENGIRVIMD 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 283 AVFNHigyyskqwqdvVQNKENSRYK----NWFYikdmskidtpieQIDEKNIPYETFGC------EKYMpklntenseV 352
Cdd:TIGR02104 249 VVYNH-----------TYSREESPFEktvpGYYY------------RYNEDGTLSNGTGVgndtasEREM---------M 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 353 IKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIWHGSLPwLMGDQFDSVMN-YLMS---- 427
Cdd:TIGR02104 297 RKFIVDSVLYWVKEYNIDGFRFDLMGIHDIETMNEIRKALNKIDPNILLYGEGWDLGTP-LPPEQKATKANaYQMPgiaf 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 428 --------------EAMKKFFCTDEINAEE-FKYMI-----NDVMVSYPIQVSEVIfNLLGSHDTTRI---LTYANGN-- 482
Cdd:TIGR02104 376 fndefrdalkgsvfHLKKKGFVSGNPGTEEiVKKGIlgsieLDAVKPSALDPSQSI-NYVECHDNHTLwdkLSLANPDet 454
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2053295504 483 ----IDRFKLAYMFMFVQTGCPCIYYGDEI-----GMEGEL-SSISEGQrkcMEWNEEKWNKDIFDFMKKIIRLRKE 549
Cdd:TIGR02104 455 eeqlKKRQKLATAILLLSQGIPFLHAGQEFmrtkqGDENSYnSPDSINQ---LDWDRKATFKDDVNYIKGLIALRKA 528
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
220-513 3.24e-14

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 75.31  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 220 EHLDYLSDLGINGIYFCPITIGkTNHR----YDTVDYM---EVD-----PT-LGDKETLKKLIEEAHKRNIKIMLDAVFN 286
Cdd:PRK09441   26 ERAPELAEAGITAVWLPPAYKG-TSGGydvgYGVYDLFdlgEFDqkgtvRTkYGTKEELLNAIDALHENGIKVYADVVLN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 287 H-IGYYSKQWQDVVQNKENSRYK--------------------------NWFYiKDMSKID-------TPIEQIDEKNIP 332
Cdd:PRK09441  105 HkAGADEKETFRVVEVDPDDRTQiisepyeiegwtrftfpgrggkysdfKWHW-YHFSGTDydenpdeSGIFKIVGDGKG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 333 YET-----FGCEKY--MPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKKVKP-DIYILGE 404
Cdd:PRK09441  184 WDDqvddeNGNFDYlmGADIDFRHPEVREELKYWAKWYMETTGFDGFRLDAVKHIDAWFIKEWIEHVREVAGkDLFIVGE 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 405 IWHGSLPWLMG---------DQFDSVMNYLMSEAMKKffctdeinAEEF--KYMINDVMVSY-PIQVseVIFnlLGSHDT 472
Cdd:PRK09441  264 YWSHDVDKLQDyleqvegktDLFDVPLHYNFHEASKQ--------GRDYdmRNIFDGTLVEAdPFHA--VTF--VDNHDT 331
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2053295504 473 TRILTYANGNIDRFK-LAYMF-MFVQTGCPCIYYGDEIGMEGE 513
Cdd:PRK09441  332 QPGQALESPVEPWFKpLAYALiLLREEGYPCVFYGDYYGASGY 374
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
208-287 2.62e-13

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: 72.60  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 208 DNFtGGDLQGVIEHLDYLSDLGINGIYFCPITI---GKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAV 284
Cdd:cd11324    79 DLF-AGDLKGLAEKIPYLKELGVTYLHLMPLLKppeGDNDGGYAVSDYREVDPRLGTMEDLRALAAELRERGISLVLDFV 157

                  ...
gi 2053295504 285 FNH 287
Cdd:cd11324   158 LNH 160
AmyAc_Pullulanase_LD-like cd11341
Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin ...
222-416 3.17e-13

Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins; Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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: 200480 [Multi-domain]  Cd Length: 406  Bit Score: 71.77  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 222 LDYLSDLGINGIYFCPI----TIGKTNHR--------YDTVDYM--E-------VDPTLGDKEtLKKLIEEAHKRNIKIM 280
Cdd:cd11341    46 LDYLKELGVTHVQLLPVfdfaSVDEDKSRpednynwgYDPVNYNvpEgsystdpYDPYARIKE-FKEMVQALHKNGIRVI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 281 LDAVFNHIGYYSKQW-QDVVqnkensryKNWFYikdmskidtpieQIDEKNIPYETFGC------EKYMpklntenseVI 353
Cdd:cd11341   125 MDVVYNHTYDSENSPfEKIV--------PGYYY------------RYNADGGFSNGSGCgndtasERPM---------VR 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053295504 354 KYLLDVGKYWIQEFDIDAWR------LDVS--NEVdhvfwrkfREEVKKVKPDIYILGEiwhgslPWLMGD 416
Cdd:cd11341   176 KYIIDSLKYWAKEYKIDGFRfdlmglHDVEtmNEI--------REALDKIDPNILLYGE------GWDFGT 232
pullulan_Gpos TIGR02102
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ...
164-406 3.44e-13

pullulanase, extracellular, Gram-positive; 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. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.


Pssm-ID: 273973 [Multi-domain]  Cd Length: 1111  Bit Score: 72.97  E-value: 3.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  164 IDIPKVPNWVK--DTVWYQIFPDRFANgDPSINPEGVDKWGaipTRDNFtggdlqgvIEHLDYLSDLGINGIYFCPI--- 238
Cdd:TIGR02102  438 LDFAKIENFKKreDAIIYEAHVRDFTS-DPAIAGDLTAQFG---TFAAF--------VEKLDYLQDLGVTHIQLLPVlsy 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  239 ---------------TIGKTNHR--YDTVDYMEV---------DPTLGDKEtLKKLIEEAHKRNIKIMLDAVFNHIGYyS 292
Cdd:TIGR02102  506 ffvnefknkermldyASSNTNYNwgYDPQNYFALsgmysedpkDPELRIAE-FKNLINEIHKRGMGVILDVVYNHTAK-V 583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  293 KQWQDVVQNkensryknwfYIKDMskidtpieqiDEKNIPYETFGCEKympkLNTENSEVIKYLLDVGKYWIQEFDIDAW 372
Cdd:TIGR02102  584 YIFEDLEPN----------YYHFM----------DADGTPRTSFGGGR----LGTTHEMSRRILVDSIKYLVDEFKVDGF 639
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2053295504  373 RLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIW 406
Cdd:TIGR02102  640 RFDMMGDHDAASIEIAYKEAKAINPNIIMIGEGW 673
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
179-289 3.00e-12

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: 69.25  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 179 YQIFPDRFANGDPSINPEGVDKWGAIPTRDNF-TGGDLQGVIEHLDYLSDLGINGIYFC--P-ITIGKTNHRYDTVDYME 254
Cdd:cd11323    59 YTIFLDRFVNGDPTNDDANGTVFEQDIYETQLrHGGDIVGLVDSLDYLQGMGIKGIYIAgtPfINMPWGADGYSPLDFTL 138
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2053295504 255 VDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIG 289
Cdd:cd11323   139 LDHHFGTIADWRAAIDEIHRRGMYVVLDNTVATMG 173
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
204-289 9.61e-12

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: 66.69  E-value: 9.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 204 IPTRDNFTG-GDLQGVIEHLDYLSDLGINGIYFCPITIGKTNHRyDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLD 282
Cdd:cd11345    21 IGDLQAFSEaGGLKGVEGKLDYLSQLKVKGLVLGPIHVVQADQP-GELNLTEIDPDLGTLEDFTSLLTAAHKKGISVVLD 99

                  ....*..
gi 2053295504 283 AVFNHIG 289
Cdd:cd11345   100 LTPNYRG 106
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
245-405 1.02e-11

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: 66.92  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 245 HRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYYSKQWQDVVQNKENSRYKN--WFYikdmskidTP 322
Cdd:cd11315    50 YRYQPTDYRIGNNQLGTEDDFKALCAAAHKYGIKIIVDVVFNHMANEGSAIEDLWYPSADIELFSpeDFH--------GN 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 323 IEQIDEKNIPYETFGCEKYMPKLNTENSEV----IKYLLDVGKYWIQEFDIDAWR---LDVSNEVDHVFWRKFREevKKV 395
Cdd:cd11315   122 GGISNWNDRWQVTQGRLGGLPDLNTENPAVqqqqKAYLKALVALGVDGFRFDAAKhieLPDEPSKASDFWTNILN--NLD 199
                         170
                  ....*....|
gi 2053295504 396 KPDIYILGEI 405
Cdd:cd11315   200 KDGLFIYGEV 209
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
222-313 8.78e-10

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 62.04  E-value: 8.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504  222 LDYLSDLGINGIYFCPITIGK--TNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIGYY---SKQWQ 296
Cdd:PRK14507   764 LPYLAALGISHVYASPILKARpgSTHGYDIVDHSQINPEIGGEEGFERFCAALKAHGLGQLLDIVPNHMGVGgadNPWWL 843
                           90
                   ....*....|....*..
gi 2053295504  297 DVVQNKENSRYKNWFYI 313
Cdd:PRK14507   844 DVLENGPASPAADAFDI 860
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
220-513 9.46e-10

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: 60.99  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 220 EHLDYLSDLGINGIYFCPITIGKTNHR------YDTVDYMEVD-----PT-LGDKETLKKLIEEAHKRNIKIMLDAVFNH 287
Cdd:cd11318    24 EDAPELAELGITAVWLPPAYKGASGTEdvgydvYDLYDLGEFDqkgtvRTkYGTKEELLEAIKALHENGIQVYADAVLNH 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 288 -IGYYSKQWQDVVQNKENSRYKNwfyIKDMSKIDTP---------------------------IEQIDEKNIPYETFGCE 339
Cdd:cd11318   104 kAGADETETVKAVEVDPNDRNKE---ISEPYEIEAWtkftfpgrggkysdfkwnwqhfsgvdyDQKTKKKGIFKINFEGK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 340 KYMPKLNTENS---------------EVIKYLLDVGKYWIQEFDIDAWRLDVSNEVDHVFWRKFREEVKK-VKPDIYILG 403
Cdd:cd11318   181 GWDEDVDDENGnydylmgadidysnpEVREELKRWGKWYINTTGLDGFRLDAVKHISASFIKDWIDHLRReTGKDLFAVG 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 404 EIWHGSLPWL------MGDQ---FDSVMNYLMSEAMKKffctdeinAEEF---KYMINDVMVSYPIQ-VSEVifnllGSH 470
Cdd:cd11318   261 EYWSGDLEALedyldaTDGKmslFDVPLHYNFHEASKS--------GGNYdlrKIFDGTLVQSRPDKaVTFV-----DNH 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053295504 471 DTTRiltyanGN------IDRFK-LAYMF-MFVQTGCPCIYYGDEIGMEGE 513
Cdd:cd11318   328 DTQP------GQsleswvEPWFKpLAYALiLLRKDGYPCVFYGDYYGIPGE 372
AmyAc_Sucrose_phosphorylase cd11355
Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose ...
212-311 3.83e-09

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: 200492  Cd Length: 433  Bit Score: 59.17  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 212 GGDLQGVIEHLD-YLSDLgINGIYFCPITIGKTNHRYDTVDYMEVDPTLGDKETLKKLIEeahkrNIKIMLDAVFNHIGY 290
Cdd:cd11355    14 GGNLKDLNTVLDtYFKGV-FGGVHILPFFPSSDDRGFDPIDYTEVDPRFGTWDDIEALGE-----DYELMADLMVNHISA 87
                          90       100
                  ....*....|....*....|.
gi 2053295504 291 YSKQWQDVVQNKENSRYKNWF 311
Cdd:cd11355    88 QSPYFQDFLAKGDASEYADLF 108
AmyAc_Sucrose_phosphorylase-like cd11343
Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose ...
250-405 8.49e-09

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: 58.28  E-value: 8.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 250 VDYMEVDPTLGDKETLKKLieeahKRNIKIMLDAVFNHIGYYSKQWQDVVQNKEnsRYKNWFyikdmskiDTPIEQIDEK 329
Cdd:cd11343    56 IDYTEVDPRLGDWDDIEAL-----AEDYDLMFDLVINHISSQSPWFQDFLAGGD--PSKDYF--------IEADPEEDLS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 330 NI----------PYETFGCEKYM--------PKLNTENSEVIKYLLDVGKYWIqEFDIDAWRLD----VSNEVD------ 381
Cdd:cd11343   121 KVvrprtsplltEFETAGGTKHVwttfsedqIDLNFRNPEVLLEFLDILLFYA-ANGARIIRLDavgyLWKELGtscfhl 199
                         170       180
                  ....*....|....*....|....*..
gi 2053295504 382 ---HVFWRKFREEVKKVKPDIYILGEI 405
Cdd:cd11343   200 petHEIIKLLRALLDALAPGVELLTET 226
AmyAc_Glg_debranch cd11326
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ...
217-550 5.05e-08

Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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: 200465 [Multi-domain]  Cd Length: 433  Bit Score: 55.55  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 217 GVIEH--LDYLSDLGINGIYFCPI----------TIGKTNH-RYDTVDYMEVDP-------TLGDKETLKKLIEEAHKRN 276
Cdd:cd11326    43 GLAEPakIPYLKELGVTAVELLPVhafddeehlvERGLTNYwGYNTLNFFAPDPryasddaPGGPVDEFKAMVKALHKAG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 277 IKIMLDAVFNHIG------------------YYSkqwqdvvQNKENSRYKNWfyikdmskidTpieqideknipyetfGC 338
Cdd:cd11326   123 IEVILDVVYNHTAeggelgptlsfrgldnasYYR-------LDPDGPYYLNY----------T---------------GC 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 339 EKympKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLD----VSNEVDHVFWRK---FRE-----EVKKVK---------P 397
Cdd:cd11326   171 GN---TLNTNHPVVLRLILDSLRYWVTEMHVDGFRFDlasvLGRDPDGFPDPNpplLEAiaqdpVLSGVKliaepwdigG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 398 DIYILGEIWHGSLPWlmGDQF-DSVmnylmseamKKFFCTDEINAEEFKYMINDvmvsypiqvSEVIF-----------N 465
Cdd:cd11326   248 GGYQVGNFPPGWAEW--NDRYrDDV---------RRFWRGDGGLVGDFATRLAG---------SSDLFghdgrspsasvN 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 466 LLGSHD--TTRILT-Y------ANG--------------------------NIDRFKLAYMFM---FVQTGCPCIYYGDE 507
Cdd:cd11326   308 FITAHDgfTLADLVsYnekhneANGennrdghndnlswncgvegptddpeiLALRRRQMRNLLatlLLSQGTPMLLAGDE 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053295504 508 IG--MEG---------ELSsisegqrkCMEWNEEKWNKDIFDFMKKIIRLRKEN 550
Cdd:cd11326   388 FGrtQQGnnnaycqdnEIS--------WLDWDLLEADSDLFRFVRRLIALRKAH 433
AmyAc_MTase_N cd11335
Alpha amylase catalytic domain found in maltosyltransferase; Maltosyltransferase (MTase), a ...
155-405 5.65e-08

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: 55.78  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 155 FFGYPYLNYIDIPKVPNWVKDTVWYQIFPdRFA-----NGD---PSINPEGVdkwgaiptRDNftgGDLQGVIEHLDYLS 226
Cdd:cd11335    25 AVKYYKLSKLKGASKGDWIKSSSVYSLFV-RTTtawdhDGDgalEPENLYGF--------RET---GTFLKMIALLPYLK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 227 DLGINGIYFCPIT-IGKTNHR------YDTVDYMEVDPTLGD--------KETLKKLIEEAHKRNIKIMLDAVFNhigyy 291
Cdd:cd11335    93 RMGINTIYLLPITkISKKFKKgelgspYAVKNFFEIDPLLHDpllgdlsvEEEFKAFVEACHMLGIRVVLDFIPR----- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 292 skqwqdvVQNKENSRYK---NWFY-IKdmskidtpieqIDEKNIPYETFGCEKYMPKLNTENSEVIKYLLDVgkywiQEF 367
Cdd:cd11335   168 -------TAARDSDLILehpEWFYwIK-----------VDELNNYHPPKVPGLGFVLPSQETLPLIYESEDV-----KEH 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2053295504 368 dIDAWRLDvSNEVDHVFWRKFREEVKKVKPDiyILGEI 405
Cdd:cd11335   225 -LKLFRWS-PNKIDPEKWRNFFKENPKPEGD--FLGEI 258
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
220-375 3.10e-07

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: 53.15  E-value: 3.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 220 EHLDYLSDLGING-IYFCPItigktnhrYDTvdymEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIgyySKQWQDV 298
Cdd:cd11329    83 EHVEAISKLGAKGvIYELPA--------DET----YLNNSYGVESDLKELVKTAKQKDIKVILDLTPNHS---SKQHPLF 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 299 VQNKE-NSRYKNwFYIKDMSKIDTPI------------EQIDEKNIPYETFGCEKymPKLNTENSEVIKYLLDVGKYWIq 365
Cdd:cd11329   148 KDSVLkEPPYRS-AFVWADGKGHTPPnnwlsvtggsawKWVEDRQYYLHQFGPDQ--PDLNLNNPAVVDELKDVLKHWL- 223
                         170
                  ....*....|
gi 2053295504 366 EFDIDAWRLD 375
Cdd:cd11329   224 DLGVRGFRLA 233
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
176-410 4.44e-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: 200487 [Multi-domain]  Cd Length: 456  Bit Score: 52.68  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 176 TVWYQIFPDRFAN--------GDPSINpeGVDKWGAIPT------RDN-FTGGDLQGVIEH---LDYlSDLGIngiyfcP 237
Cdd:cd11349     1 IIIYQLLPRLFGNknttnipnGTIEEN--GVGKFNDFDDtalkeiKSLgFTHVWYTGVIRHatqTDY-SAYGI------P 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 238 -----ITIGKTNHRYDTVDYMEVDPTLGDK-----ETLKKLIEEAHKRNIKIMLDAVFNHIG--YYSKQWQDVVQN---- 301
Cdd:cd11349    72 pddpdIVKGRAGSPYAIKDYYDVDPDLATDptnrmEEFEALVERTHAAGLKVIIDFVPNHVArqYHSDAKPEGVKDfgan 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 302 ----KENSRYKNWFYIKDMS-KIDTPIEQIDEKNIPYETF-------GCEKYMPKLNtENSEVIK------YLLDVGKY- 362
Cdd:cd11349   152 ddtsKAFDPSNNFYYLPGEPfVLPFSLNGSPATDGPYHESpakatgnDCFSAAPSIN-DWYETVKlnygvdYDGGGSFHf 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053295504 363 ------WIQEFDI---------DAWRLDVSNEVDHVFWRKFREEVKKVKPDIYILGEIWHGSL 410
Cdd:cd11349   231 dpipdtWIKMLDIllfwaakgvDGFRCDMAEMVPVEFWHWAIPEIKARYPELIFIAEIYNPGL 293
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
208-571 5.51e-07

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


Pssm-ID: 440065 [Multi-domain]  Cd Length: 625  Bit Score: 52.83  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 208 DNFTGGDLQGVIEHL-DYLSDLGINGIYFCPIT-------IGktnhrYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKI 279
Cdd:COG0296   158 EGGRFLTYRELAERLvPYLKELGFTHIELMPVAehpfdgsWG-----YQPTGYFAPTSRYGTPDDFKYFVDACHQAGIGV 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 280 MLDAVFNHIGyyskqwqdvvqnkensryknwfyiKD---MSKID-TPIeqideknipYETfgcEKYMPKLNTE-NS---- 350
Cdd:COG0296   233 ILDWVPNHFP------------------------PDghgLARFDgTAL---------YEH---ADPRRGEHTDwGTlifn 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 351 ----EVIKYLLDVGKYWIQEFDIDAWRLD-----------------VSNE---------VDhvFWRKFREEVKKVKPDIY 400
Cdd:COG0296   277 ygrnEVRNFLISNALYWLEEFHIDGLRVDavasmlyldysreegewIPNKyggrenleaIH--FLRELNETVYERFPGVL 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 401 ILGE-----------IWHG----SLPWLMGdqfdsVMNylmseAMKKFFCTDEINAeefKYMINDVMVSYPIQVSE-VIF 464
Cdd:COG0296   355 TIAEestawpgvtrpTELGglgfDAKWNMG-----WMH-----DTLRYMTKDPIYR---KYHHNELTFSLVYAFSEnFVL 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 465 NLlgSHD-----TTRILTYANGN----IDRFKLAYMFMFVQTGCPCIYYGDEIGMEGelssisegqrkcmEWNEEK---- 531
Cdd:COG0296   422 PL--SHDevvhgKGSLLGKMPGDrwqkFANLRLLYAYMWTHPGKKLLFMGQEFGQWR-------------EWNYDEpldw 486
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053295504 532 ------WNKDIFDFMKKIIRLRKENKELRSISN-----EWVLADKENGTII 571
Cdd:COG0296   487 hlldypPHAGLQRLVRDLNRLYREEPALHELDFdpegfEWIDADDAENSVL 537
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
225-504 1.27e-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: 50.68  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 225 LSDLGINGIYFCPITIGKT--NHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHigyyskqwqdvvqnk 302
Cdd:cd11314    27 LAAAGFTAIWLPPPSKSVSgsSMGYDPGDLYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINH--------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 303 ensryknwfyikdMSKIDTpieqideknipYETFGcekYMPKLNTENSEVIKYLLDVGKYWIQEFDIDAWRLDVSnevdH 382
Cdd:cd11314    92 -------------RSGPDT-----------GEDFG---GAPDLDHTNPEVQNDLKAWLNWLKNDIGFDGWRFDFV----K 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 383 VFWRKF-REEVKKVKPDIYIlGEIWHGsLPWLMGDQ------------------FDSVMNYLMSEAMkkffctdeiNAEE 443
Cdd:cd11314   141 GYAPSYvKEYNEATSPSFSV-GEYWDG-LSYENQDAhrqrlvdwidatgggsaaFDFTTKYILQEAV---------NNNE 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2053295504 444 FKYMINDVMVS------YPiQVSeVIFnlLGSHDTTRILTYANGNIDRFKLAYMFMFVQTGCPCIYY 504
Cdd:cd11314   210 YWRLRDGQGKPpgligwWP-QKA-VTF--VDNHDTGSTQGHWPFPTDNVLQGYAYILTHPGTPCVFW 272
AmyAc_GlgE_like cd11344
Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan: ...
178-286 1.46e-06

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: 50.68  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 178 WYQIFPdRFANGDPsinpegvdkwgaiptrdnFTGGDLQGVIEHLDYLSDLGINGIYFCPI-TIGKTNH--RYDTVD--- 251
Cdd:cd11344     4 WYEFFP-RSAGADP------------------GRHGTFRDAEARLPRIAAMGFDVLYLPPIhPIGRTNRkgKNNALVagp 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2053295504 252 ---------------YMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFN 286
Cdd:cd11344    65 gdpgspwaigseeggHDAIHPELGTLEDFDRLVAEARELGIEVALDIALQ 114
AmyAc_Glg_debranch_2 cd11327
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ...
220-295 3.82e-06

Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities, 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. The catalytic triad (DED), which is highly conserved in other debranching enzymes, is not present in this group. 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: 200466  Cd Length: 478  Bit Score: 49.93  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 220 EHLDYLSDLGINGIYFCPI-TIGKTNHRYDTVDYMEVDPTL---GDKET---LKKLIEEAHKR-NIKIMLDAVFNHIGYY 291
Cdd:cd11327    40 ERLRVAKELGYNMIHFTPLqELGESNSPYSIADQLELNPDFfpdGKKKTfedVEELVKKLEKEwGLLSITDVVLNHTANN 119

                  ....
gi 2053295504 292 SKqW 295
Cdd:cd11327   120 SP-W 122
AmyAc_Sucrose_phosphorylase-like_1 cd11356
Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called ...
250-375 5.08e-06

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: 49.43  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 250 VDYMEVDPTLGDKETLKKLieeahKRNIKIMLDAVFNHIgyySKQ--WqdvVQN--KENSRYKNWFYIK----DMSKI-- 319
Cdd:cd11356    58 IDYRQVNPELGDWEDIEAL-----AKDFRLMFDLVINHV---SSSspW---FQQflAGEPPYKDYFIEAdpdtDLSQVvr 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2053295504 320 --DTPIEQidekniPYETFGCEKYM--------PKLNTENSEVIKYLLDVGKYWIQEfDIDAWRLD 375
Cdd:cd11356   127 prTSPLLT------PFETADGTKHVwttfspdqVDLNFRNPEVLLEFLDILLFYLER-GARIIRLD 185
AmyAc_plant_IsoA cd11346
Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching ...
213-370 7.25e-05

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: 45.54  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 213 GDLQGVIEHLDYLSDLGINGIYFCPITIGKTNHRYDT--------VDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAV 284
Cdd:cd11346    29 GTFLGVLEKVDHLKSLGVNTVLLQPIFAFARVKGPYYppsffsapDPYGAGDSSLSASAELRAMVKGLHSNGIEVLLEVV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053295504 285 FNHIGyyskQWQDVVQNKE------NSRYknwfYIKDMSKIDTPiEQIDEKNIpyetfgcekympkLNTENSEVIKYLLD 358
Cdd:cd11346   109 LTHTA----EGTDESPESEslrgidAASY----YILGKSGVLEN-SGVPGAAV-------------LNCNHPVTQSLILD 166
                         170
                  ....*....|..
gi 2053295504 359 VGKYWIQEFDID 370
Cdd:cd11346   167 SLRHWATEFGVD 178
AmyAc_1 cd11347
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
247-289 1.22e-04

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: 44.92  E-value: 1.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2053295504 247 YDTVDYmEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNHIG 289
Cdd:cd11347    87 YAITDY-TVNPDLGGEDDLAALRERLAARGLKLMLDFVPNHVA 128
PLN02784 PLN02784
alpha-amylase
223-287 5.57e-03

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 39.99  E-value: 5.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053295504 223 DYLSDLGINGIYFCPITIGKTNHRYDTVDYMEVDPTLGDKETLKKLIEEAHKRNIKIMLDAVFNH 287
Cdd:PLN02784  528 AELSSLGFTVVWLPPPTESVSPEGYMPKDLYNLNSRYGTIDELKDLVKSFHEVGIKVLGDAVLNH 592
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH