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Conserved domains on  [gi|489000892|ref|WP_002911554|]
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MULTISPECIES: alpha-amylase [Klebsiella]

Protein Classification

alpha-amylase( domain architecture ID 11484173)

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

CATH:  3.20.20.80
CAZY:  GH13
EC:  3.2.1.-
Gene Ontology:  GO:0004556|GO:0005509|GO:0005975
SCOP:  4003138

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
1-490 0e+00

cytoplasmic alpha-amylase; Reviewed


:

Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 852.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   1 MKNPTLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSVGYDTYDLFDLGEFDQKGSVATKYGDK 80
Cdd:PRK09441   1 MRNGTMMQYFEWYLPNDGKLWNRLAERAPELAEAGITAVWLPPAYKGTSGGYDVGYGVYDLFDLGEFDQKGTVRTKYGTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  81 AQLLAAINALKEHNIAVLLDVVVNHKMGADEKESLRVQRVDEQDRTQIDEEIIECEAWTRYTFPVRAGQYSQFVWDYKCF 160
Cdd:PRK09441  81 EELLNAIDALHENGIKVYADVVLNHKAGADEKETFRVVEVDPDDRTQIISEPYEIEGWTRFTFPGRGGKYSDFKWHWYHF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 161 SGIDHIENPTEDGVFKIvnDYTGEGWNEQVDDELGNFDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHI 240
Cdd:PRK09441 161 SGTDYDENPDESGIFKI--VGDGKGWDDQVDDENGNFDYLMGADIDFRHPEVREELKYWAKWYMETTGFDGFRLDAVKHI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 241 PAWFYKAWIEHVQEVAPQPLFIVAEYWSHEVEKLQQYIDLVEGKTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVEAD 320
Cdd:PRK09441 239 DAWFIKEWIEHVREVAGKDLFIVGEYWSHDVDKLQDYLEQVEGKTDLFDVPLHYNFHEASKQGRDYDMRNIFDGTLVEAD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 321 PFHAVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYADLFGASYEDTggdgetyaiEMPVIEQLHELID 400
Cdd:PRK09441 319 PFHAVTFVDNHDTQPGQALESPVEPWFKPLAYALILLREEGYPCVFYGDYYGASGYYI---------DMPFKEKLDKLLL 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 401 ARQRFAHGVQTLWFDHPNCIAFSRSGTDDDPGCVVIMSNGDEGEKTLTLGENYGNKRWRDFLGNREEIVETDGEGCATFT 480
Cdd:PRK09441 390 ARKNFAYGEQTDYFDHPNCIGWTRSGDEENPGLAVVISNGDAGEKTMEVGENYAGKTWRDYTGNRQETVTIDEDGWGTFP 469
                        490
                 ....*....|
gi 489000892 481 CNGGSVSVWV 490
Cdd:PRK09441 470 VNGGSVSVWV 479
 
Name Accession Description Interval E-value
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
1-490 0e+00

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 852.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   1 MKNPTLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSVGYDTYDLFDLGEFDQKGSVATKYGDK 80
Cdd:PRK09441   1 MRNGTMMQYFEWYLPNDGKLWNRLAERAPELAEAGITAVWLPPAYKGTSGGYDVGYGVYDLFDLGEFDQKGTVRTKYGTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  81 AQLLAAINALKEHNIAVLLDVVVNHKMGADEKESLRVQRVDEQDRTQIDEEIIECEAWTRYTFPVRAGQYSQFVWDYKCF 160
Cdd:PRK09441  81 EELLNAIDALHENGIKVYADVVLNHKAGADEKETFRVVEVDPDDRTQIISEPYEIEGWTRFTFPGRGGKYSDFKWHWYHF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 161 SGIDHIENPTEDGVFKIvnDYTGEGWNEQVDDELGNFDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHI 240
Cdd:PRK09441 161 SGTDYDENPDESGIFKI--VGDGKGWDDQVDDENGNFDYLMGADIDFRHPEVREELKYWAKWYMETTGFDGFRLDAVKHI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 241 PAWFYKAWIEHVQEVAPQPLFIVAEYWSHEVEKLQQYIDLVEGKTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVEAD 320
Cdd:PRK09441 239 DAWFIKEWIEHVREVAGKDLFIVGEYWSHDVDKLQDYLEQVEGKTDLFDVPLHYNFHEASKQGRDYDMRNIFDGTLVEAD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 321 PFHAVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYADLFGASYEDTggdgetyaiEMPVIEQLHELID 400
Cdd:PRK09441 319 PFHAVTFVDNHDTQPGQALESPVEPWFKPLAYALILLREEGYPCVFYGDYYGASGYYI---------DMPFKEKLDKLLL 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 401 ARQRFAHGVQTLWFDHPNCIAFSRSGTDDDPGCVVIMSNGDEGEKTLTLGENYGNKRWRDFLGNREEIVETDGEGCATFT 480
Cdd:PRK09441 390 ARKNFAYGEQTDYFDHPNCIGWTRSGDEENPGLAVVISNGDAGEKTMEVGENYAGKTWRDYTGNRQETVTIDEDGWGTFP 469
                        490
                 ....*....|
gi 489000892 481 CNGGSVSVWV 490
Cdd:PRK09441 470 VNGGSVSVWV 479
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
3-404 0e+00

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: 647.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   3 NPTLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSVGYDTYDLFDLGEFDQKGSVATKYGDKAQ 82
Cdd:cd11318    1 NGTMMQYFEWYLPADGQHWKRLAEDAPELAELGITAVWLPPAYKGASGTEDVGYDVYDLYDLGEFDQKGTVRTKYGTKEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  83 LLAAINALKEHNIAVLLDVVVNHKMGADEKESLRVQRVDEQDRTQIDEEIIECEAWTRYTFPVRAGQYSQFVWDYKCFSG 162
Cdd:cd11318   81 LLEAIKALHENGIQVYADAVLNHKAGADETETVKAVEVDPNDRNKEISEPYEIEAWTKFTFPGRGGKYSDFKWNWQHFSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 163 IDHIENPTEDGVFKIVNDytGEGWNEQVDDELGNFDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHIPA 242
Cdd:cd11318  161 VDYDQKTKKKGIFKINFE--GKGWDEDVDDENGNYDYLMGADIDYSNPEVREELKRWGKWYINTTGLDGFRLDAVKHISA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 243 WFYKAWIEHVQEVAPQPLFIVAEYWSHEVEKLQQYIDLVEGKTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVEADPF 322
Cdd:cd11318  239 SFIKDWIDHLRRETGKDLFAVGEYWSGDLEALEDYLDATDGKMSLFDVPLHYNFHEASKSGGNYDLRKIFDGTLVQSRPD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 323 HAVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYADLFGASYEDtggdgetyaIEMPVIEQLHELIDAR 402
Cdd:cd11318  319 KAVTFVDNHDTQPGQSLESWVEPWFKPLAYALILLRKDGYPCVFYGDYYGIPGED---------PIPPKKELLDKLLKAR 389

                 ..
gi 489000892 403 QR 404
Cdd:cd11318  390 KL 391
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
31-382 3.08e-23

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 101.48  E-value: 3.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKGAsGGYSvGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkmGAD 110
Cdd:COG0366   40 LKDLGVDAIWLSPFFPSP-MSDH-GYDISDYRD---------VDPRFGTLADFDELVAEAHARGIKVILDLVLNH--TSD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 111 E----KESLRVQRVDEQDR-----------TQIDEEIIECEAWTRYTfpvRAGQYsqfvwdykcfsgidhienptedgvf 175
Cdd:COG0366  107 EhpwfQEARAGPDSPYRDWyvwrdgkpdlpPNNWFSIFGGSAWTWDP---EDGQY------------------------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 176 kivndYTGEGWNEQVDdelgnfdylmganIDFRNHAVTEEIKYWARWVMEQtGCDGFRLDAVKHI------------PAW 243
Cdd:COG0366  159 -----YLHLFFSSQPD-------------LNWENPEVREELLDVLRFWLDR-GVDGFRLDAVNHLdkdeglpenlpeVHE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 244 FYKAWIEHVQEVAPQpLFIVAEYWSHEVEKLQQYIDLVEGkTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVE-ADPF 322
Cdd:COG0366  220 FLRELRAAVDEYYPD-FFLVGEAWVDPPEDVARYFGGDEL-DMAFNFPLMPALWDALAPEDAAELRDALAQTPALyPEGG 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489000892 323 HAVTLVTNHDTQ---PLQALEAPVEpWFKpLAYALIL-LRenGVPSVFYAD---LFGASYED-TGGDG 382
Cdd:COG0366  298 WWANFLRNHDQPrlaSRLGGDYDRR-RAK-LAAALLLtLP--GTPYIYYGDeigMTGDKLQDpEGRDG 361
Aamy smart00642
Alpha-amylase domain;
5-108 5.49e-18

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 81.22  E-value: 5.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892     5 TLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSvgydtYDLFDLGEFDQKGsvaTKYGDKAQLL 84
Cdd:smart00642   2 IYPDRFADGNGDGGGDLQGIIEKLDYLKDLGVTAIWLSPIFESPQGYPS-----YHGYDISDYKQID---PRFGTMEDFK 73
                           90       100
                   ....*....|....*....|....
gi 489000892    85 AAINALKEHNIAVLLDVVVNHKMG 108
Cdd:smart00642  74 ELVDAAHARGIKVILDVVINHTSD 97
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
31-369 3.98e-16

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: 79.32  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   31 LNEIGINMVWLPPAYKgaSGGYSVGYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkMGad 110
Cdd:pfam00128  13 LKELGVTAIWLSPIFD--SPQADHGYDIADYY---------KIDPHYGTMEDFKELISKAHERGIKVILDLVVNH-TS-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  111 ekeslrvqrvDEQdrtqideeiieceAWTRYTFPVRAGQYSQFvWDYKcfsgidHIENPTEDGVFKIVNDYTGEGWNEQV 190
Cdd:pfam00128  79 ----------DEH-------------AWFQESRSSKDNPYRDY-YFWR------PGGGPIPPNNWRSYFGGSAWTYDEKG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  191 DDELGNFDYLMGANIDFRNHAVTEEIK----YWARwvmeqTGCDGFRLDAVKHIP----------AWFYKAWIEHVQEVA 256
Cdd:pfam00128 129 QEYYLHLFVAGQPDLNWENPEVRNELYdvvrFWLD-----KGIDGFRIDVVKHISkvpglpfennGPFWHEFTQAMNETV 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  257 --PQPLFIVAEYWSHEVEKLQQYIDLVEGK-TMLFDAPLqMKFHEASRQgrDYDMSQIFSGTLVE--ADPFH-------- 323
Cdd:pfam00128 204 fgYKDVMTVGEVFHGDGEWARVYTTEARMElEMGFNFPH-NDVALKPFI--KWDLAPISARKLKEmiTDWLDalpdtngw 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 489000892  324 AVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRenGVPSVFYAD 369
Cdd:pfam00128 281 NFTFLGNHDQPRFLSRFGDDRASAKLLAVFLLTLR--GTPYIYQGE 324
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
31-111 2.61e-03

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: 40.38  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   31 LNEIGINMVWLPPAYKGASG-------GYSVGYDTYdLFDLGEfdqkGSVATKYGDKAQ----LLAAINALKEHNIAVLL 99
Cdd:TIGR02104 173 LKELGVTHVQLLPVFDFAGVdeedpnnAYNWGYDPL-NYNVPE----GSYSTNPYDPATrireLKQMIQALHENGIRVIM 247
                          90
                  ....*....|..
gi 489000892  100 DVVVNHKMGADE 111
Cdd:TIGR02104 248 DVVYNHTYSREE 259
 
Name Accession Description Interval E-value
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
1-490 0e+00

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 852.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   1 MKNPTLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSVGYDTYDLFDLGEFDQKGSVATKYGDK 80
Cdd:PRK09441   1 MRNGTMMQYFEWYLPNDGKLWNRLAERAPELAEAGITAVWLPPAYKGTSGGYDVGYGVYDLFDLGEFDQKGTVRTKYGTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  81 AQLLAAINALKEHNIAVLLDVVVNHKMGADEKESLRVQRVDEQDRTQIDEEIIECEAWTRYTFPVRAGQYSQFVWDYKCF 160
Cdd:PRK09441  81 EELLNAIDALHENGIKVYADVVLNHKAGADEKETFRVVEVDPDDRTQIISEPYEIEGWTRFTFPGRGGKYSDFKWHWYHF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 161 SGIDHIENPTEDGVFKIvnDYTGEGWNEQVDDELGNFDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHI 240
Cdd:PRK09441 161 SGTDYDENPDESGIFKI--VGDGKGWDDQVDDENGNFDYLMGADIDFRHPEVREELKYWAKWYMETTGFDGFRLDAVKHI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 241 PAWFYKAWIEHVQEVAPQPLFIVAEYWSHEVEKLQQYIDLVEGKTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVEAD 320
Cdd:PRK09441 239 DAWFIKEWIEHVREVAGKDLFIVGEYWSHDVDKLQDYLEQVEGKTDLFDVPLHYNFHEASKQGRDYDMRNIFDGTLVEAD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 321 PFHAVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYADLFGASYEDTggdgetyaiEMPVIEQLHELID 400
Cdd:PRK09441 319 PFHAVTFVDNHDTQPGQALESPVEPWFKPLAYALILLREEGYPCVFYGDYYGASGYYI---------DMPFKEKLDKLLL 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 401 ARQRFAHGVQTLWFDHPNCIAFSRSGTDDDPGCVVIMSNGDEGEKTLTLGENYGNKRWRDFLGNREEIVETDGEGCATFT 480
Cdd:PRK09441 390 ARKNFAYGEQTDYFDHPNCIGWTRSGDEENPGLAVVISNGDAGEKTMEVGENYAGKTWRDYTGNRQETVTIDEDGWGTFP 469
                        490
                 ....*....|
gi 489000892 481 CNGGSVSVWV 490
Cdd:PRK09441 470 VNGGSVSVWV 479
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
3-404 0e+00

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: 647.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   3 NPTLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSVGYDTYDLFDLGEFDQKGSVATKYGDKAQ 82
Cdd:cd11318    1 NGTMMQYFEWYLPADGQHWKRLAEDAPELAELGITAVWLPPAYKGASGTEDVGYDVYDLYDLGEFDQKGTVRTKYGTKEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  83 LLAAINALKEHNIAVLLDVVVNHKMGADEKESLRVQRVDEQDRTQIDEEIIECEAWTRYTFPVRAGQYSQFVWDYKCFSG 162
Cdd:cd11318   81 LLEAIKALHENGIQVYADAVLNHKAGADETETVKAVEVDPNDRNKEISEPYEIEAWTKFTFPGRGGKYSDFKWNWQHFSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 163 IDHIENPTEDGVFKIVNDytGEGWNEQVDDELGNFDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHIPA 242
Cdd:cd11318  161 VDYDQKTKKKGIFKINFE--GKGWDEDVDDENGNYDYLMGADIDYSNPEVREELKRWGKWYINTTGLDGFRLDAVKHISA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 243 WFYKAWIEHVQEVAPQPLFIVAEYWSHEVEKLQQYIDLVEGKTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVEADPF 322
Cdd:cd11318  239 SFIKDWIDHLRRETGKDLFAVGEYWSGDLEALEDYLDATDGKMSLFDVPLHYNFHEASKSGGNYDLRKIFDGTLVQSRPD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 323 HAVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYADLFGASYEDtggdgetyaIEMPVIEQLHELIDAR 402
Cdd:cd11318  319 KAVTFVDNHDTQPGQSLESWVEPWFKPLAYALILLRKDGYPCVFYGDYYGIPGED---------PIPPKKELLDKLLKAR 389

                 ..
gi 489000892 403 QR 404
Cdd:cd11318  390 KL 391
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
6-406 6.28e-55

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: 185.89  E-value: 6.28e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   6 LLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGgYSVGYDTYDLFDLGefdqkgsvaTKYGDKAQLLA 85
Cdd:cd11314    2 MLQGFYWDSPKDGTWWNHLESKAPELAAAGFTAIWLPPPSKSVSG-SSMGYDPGDLYDLN---------SRYGSEAELRS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  86 AINALKEHNIAVLLDVVVNHKMGADekeslrvqrvdeqdrtqideeiieceawtrytfpvragqysqfvwdykcfsgidh 165
Cdd:cd11314   72 LIAALHAKGIKVIADIVINHRSGPD------------------------------------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 166 ienptedgvfkivndyTGEgwneqvddelgnfDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHIPAWFY 245
Cdd:cd11314   97 ----------------TGE-------------DFGGAPDLDHTNPEVQNDLKAWLNWLKNDIGFDGWRFDFVKGYAPSYV 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 246 KAWIEhvqevAPQPLFIVAEYWS--------HEVEKLQQYIDLVEGKTMLFDAPLQMKFHEA--SRQGRDYDMSQIFSGT 315
Cdd:cd11314  148 KEYNE-----ATSPSFSVGEYWDglsyenqdAHRQRLVDWIDATGGGSAAFDFTTKYILQEAvnNNEYWRLRDGQGKPPG 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 316 LVEADPFHAVTLVTNHDTQPLQALEAPVePWFKPLAYALILLREnGVPSVFYADlfgasYEDTGgdgetyaiempVIEQL 395
Cdd:cd11314  223 LIGWWPQKAVTFVDNHDTGSTQGHWPFP-TDNVLQGYAYILTHP-GTPCVFWDH-----YYDWG-----------LKDEI 284
                        410
                 ....*....|.
gi 489000892 396 HELIDARQRFA 406
Cdd:cd11314  285 KALIAARKRAG 295
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
31-382 3.08e-23

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 101.48  E-value: 3.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKGAsGGYSvGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkmGAD 110
Cdd:COG0366   40 LKDLGVDAIWLSPFFPSP-MSDH-GYDISDYRD---------VDPRFGTLADFDELVAEAHARGIKVILDLVLNH--TSD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 111 E----KESLRVQRVDEQDR-----------TQIDEEIIECEAWTRYTfpvRAGQYsqfvwdykcfsgidhienptedgvf 175
Cdd:COG0366  107 EhpwfQEARAGPDSPYRDWyvwrdgkpdlpPNNWFSIFGGSAWTWDP---EDGQY------------------------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 176 kivndYTGEGWNEQVDdelgnfdylmganIDFRNHAVTEEIKYWARWVMEQtGCDGFRLDAVKHI------------PAW 243
Cdd:COG0366  159 -----YLHLFFSSQPD-------------LNWENPEVREELLDVLRFWLDR-GVDGFRLDAVNHLdkdeglpenlpeVHE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 244 FYKAWIEHVQEVAPQpLFIVAEYWSHEVEKLQQYIDLVEGkTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVE-ADPF 322
Cdd:COG0366  220 FLRELRAAVDEYYPD-FFLVGEAWVDPPEDVARYFGGDEL-DMAFNFPLMPALWDALAPEDAAELRDALAQTPALyPEGG 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489000892 323 HAVTLVTNHDTQ---PLQALEAPVEpWFKpLAYALIL-LRenGVPSVFYAD---LFGASYED-TGGDG 382
Cdd:COG0366  298 WWANFLRNHDQPrlaSRLGGDYDRR-RAK-LAAALLLtLP--GTPYIYYGDeigMTGDKLQDpEGRDG 361
PLN02784 PLN02784
alpha-amylase
6-372 2.93e-18

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 88.14  E-value: 2.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   6 LLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASggySVGYDTYDLFDLGefdqkgsvaTKYGDKAQLLA 85
Cdd:PLN02784 505 LCQGFNWESHKSGRWYMELGEKAAELSSLGFTVVWLPPPTESVS---PEGYMPKDLYNLN---------SRYGTIDELKD 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  86 AINALKEHNIAVLLDVVVNHKmgadekeslrvqrvdeqdrtqideeiieCEawtryTFPVRAGQYSQF----VWDYKCfs 161
Cdd:PLN02784 573 LVKSFHEVGIKVLGDAVLNHR----------------------------CA-----HFQNQNGVWNIFggrlNWDDRA-- 617
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 162 gidhienptedgvfkIVND---YTGEGwNEQVDDelgNFDylMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVK 238
Cdd:PLN02784 618 ---------------VVADdphFQGRG-NKSSGD---NFH--AAPNIDHSQDFVRKDLKEWLCWMRKEVGYDGWRLDFVR 676
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 239 HIPAWFYKAWIEhvqevAPQPLFIVAEYW---------------SHEvEKLQQYIDLVEGKTMLFDAPLQMKFHEA---S 300
Cdd:PLN02784 677 GFWGGYVKDYME-----ASEPYFAVGEYWdslsytygemdynqdAHR-QRIVDWINATNGTAGAFDVTTKGILHSAlerC 750
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489000892 301 RQGRDYDMSQIFSGtLVEADPFHAVTLVTNHDTQPLQAleapvePWFKPL-----AYALILLREnGVPSVFYADLFG 372
Cdd:PLN02784 751 EYWRLSDQKGKPPG-VVGWWPSRAVTFIENHDTGSTQG------HWRFPEgkemqGYAYILTHP-GTPAVFYDHIFS 819
PLN02361 PLN02361
alpha-amylase
6-404 4.29e-18

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 86.02  E-value: 4.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   6 LLQCFHWYyPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASggySVGYDTYDLFDLGefdqkgsvaTKYGDKAQLLA 85
Cdd:PLN02361  14 LLQAFNWE-SHKHDWWRNLEGKVPDLAKSGFTSAWLPPPSQSLA---PEGYLPQNLYSLN---------SAYGSEHLLKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  86 AINALKEHNIAVLLDVVVNHKMGADEKESLRVQRVDeqdrtqideeiieceawtryTFPVRagqysqfvWDykcfsgidh 165
Cdd:PLN02361  81 LLRKMKQYNVRAMADIVINHRVGTTQGHGGMYNRYD--------------------GIPLP--------WD--------- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 166 iENPTEDGVFKIVNDYTGEgwneqvddelgNFDYLmgANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHIPAWFY 245
Cdd:PLN02361 124 -EHAVTSCTGGLGNRSTGD-----------NFNGV--PNIDHTQHFVRKDIIGWLIWLRNDVGFQDFRFDFAKGYSAKFV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 246 KAWIEhvqevAPQPLFIVAEYW-----------------SHEvEKLQQYIDLVEGKTMLFDAPLQMKFHEASR------- 301
Cdd:PLN02361 190 KEYIE-----AAKPLFSVGEYWdscnysgpdyrldynqdSHR-QRIVNWIDGTGGLSAAFDFTTKGILQEAVKgqwwrlr 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 302 --QGRDYDMSQIFsgtlveadPFHAVTLVTNHDTQPLQALeapvepWFKPL-----AYALILLREnGVPSVFYADLFgas 374
Cdd:PLN02361 264 daQGKPPGVMGWW--------PSRAVTFIDNHDTGSTQAH------WPFPSdhimeGYAYILTHP-GIPTVFYDHFY--- 325
                        410       420       430
                 ....*....|....*....|....*....|
gi 489000892 375 yeDTGGDgetyaiempVIEQLHELIDARQR 404
Cdd:PLN02361 326 --DWGGS---------IHDQIVKLIDIRKR 344
Aamy smart00642
Alpha-amylase domain;
5-108 5.49e-18

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 81.22  E-value: 5.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892     5 TLLQCFHWYYPTGGELWPEVEALAPSLNEIGINMVWLPPAYKGASGGYSvgydtYDLFDLGEFDQKGsvaTKYGDKAQLL 84
Cdd:smart00642   2 IYPDRFADGNGDGGGDLQGIIEKLDYLKDLGVTAIWLSPIFESPQGYPS-----YHGYDISDYKQID---PRFGTMEDFK 73
                           90       100
                   ....*....|....*....|....
gi 489000892    85 AAINALKEHNIAVLLDVVVNHKMG 108
Cdd:smart00642  74 ELVDAAHARGIKVILDVVINHTSD 97
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
21-367 1.06e-16

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: 79.91  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  21 WPEVEALAPSLNEIGINMVWLPPAYKGASGGYSVGYDTYDLFDlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLD 100
Cdd:cd00551   24 LKGIIDKLDYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLDYY--------EIDPRLGTEEDFKELVKAAHKRGIKVILD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 101 VVVNHKMgadekeslrvqrvdeqdrtqideeiieceawtrytfpvragqysqfvwdykcfsgidhienptedgvfkivnd 180
Cdd:cd00551   96 LVFNHDI------------------------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 181 ytgegwneqvddelgnfdylmganidfrnhavteeIKYWARwvmeqTGCDGFRLDAVKHI----PAWFYKAWIEHVQEVA 256
Cdd:cd00551  103 -----------------------------------LRFWLD-----EGVDGFRLDAAKHVpkpePVEFLREIRKDAKLAK 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 257 PqPLFIVAEYWSHEVEKLQQYidlveGKTMLFDAPLQMKFHEASRQ---GRDYDMSQIFSGTLVEADPFHAVTLVTNHDT 333
Cdd:cd00551  143 P-DTLLLGEAWGGPDELLAKA-----GFDDGLDSVFDFPLLEALRDalkGGEGALAILAALLLLNPEGALLVNFLGNHDT 216
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 489000892 334 QPLQALEAPVEPWFKP----LAYALILLReNGVPSVFY 367
Cdd:cd00551  217 FRLADLVSYKIVELRKarlkLALALLLTL-PGTPMIYY 253
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
31-369 3.98e-16

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: 79.32  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   31 LNEIGINMVWLPPAYKgaSGGYSVGYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkMGad 110
Cdd:pfam00128  13 LKELGVTAIWLSPIFD--SPQADHGYDIADYY---------KIDPHYGTMEDFKELISKAHERGIKVILDLVVNH-TS-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  111 ekeslrvqrvDEQdrtqideeiieceAWTRYTFPVRAGQYSQFvWDYKcfsgidHIENPTEDGVFKIVNDYTGEGWNEQV 190
Cdd:pfam00128  79 ----------DEH-------------AWFQESRSSKDNPYRDY-YFWR------PGGGPIPPNNWRSYFGGSAWTYDEKG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  191 DDELGNFDYLMGANIDFRNHAVTEEIK----YWARwvmeqTGCDGFRLDAVKHIP----------AWFYKAWIEHVQEVA 256
Cdd:pfam00128 129 QEYYLHLFVAGQPDLNWENPEVRNELYdvvrFWLD-----KGIDGFRIDVVKHISkvpglpfennGPFWHEFTQAMNETV 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  257 --PQPLFIVAEYWSHEVEKLQQYIDLVEGK-TMLFDAPLqMKFHEASRQgrDYDMSQIFSGTLVE--ADPFH-------- 323
Cdd:pfam00128 204 fgYKDVMTVGEVFHGDGEWARVYTTEARMElEMGFNFPH-NDVALKPFI--KWDLAPISARKLKEmiTDWLDalpdtngw 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 489000892  324 AVTLVTNHDTQPLQALEAPVEPWFKPLAYALILLRenGVPSVFYAD 369
Cdd:pfam00128 281 NFTFLGNHDQPRFLSRFGDDRASAKLLAVFLLTLR--GTPYIYQGE 324
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
202-403 2.65e-14

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: 74.21  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 202 GANIDFRNHAVTEEIKYWARWVMEqTGCDGFRLDAVKHIPAWFYKAWIEHVQEVAPQP-LFIVAEYWSHEVEKLQQYIDL 280
Cdd:cd11339  124 TGDLNTENPEVVDYLIDAYKWWID-TGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPdFFMFGEVYDGDPSYIAPYTTT 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 281 VEGKTMLfDAPLQMKFHEA-SRQGRDYDMSQIFSGTLVEADPFHAVTLVTNHDTQPLQALEA---PVEPWFKPLAYALI- 355
Cdd:cd11339  203 AGGDSVL-DFPLYGAIRDAfAGGGSGDLLQDLFLSDDLYNDATELVTFLDNHDMGRFLSSLKdgsADGTARLALALALLf 281
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489000892 356 LLRenGVPSVFYAD---------------LFGASYEDTGGDGETYAIEMPVIEQLHELIDARQ 403
Cdd:cd11339  282 TSR--GIPCIYYGTeqgftgggdpdngrrNMFASTGDLTSADDNFDTDHPLYQYIARLNRIRR 342
PLN00196 PLN00196
alpha-amylase; Provisional
6-410 1.76e-12

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 69.18  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   6 LLQCFHW--YYPTGGE---LWPEVEALApslnEIGINMVWLPPAYKGASggySVGYDTYDLFDLGefdqkgsvATKYGDK 80
Cdd:PLN00196  27 LFQGFNWesWKQNGGWynfLMGKVDDIA----AAGITHVWLPPPSHSVS---EQGYMPGRLYDLD--------ASKYGNE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  81 AQLLAAINALKEHNIAVLLDVVVNHKMgADEKESlrvqrvdeqdrtqideeiieceawtrytfpvrAGQYSQFvwdykcf 160
Cdd:PLN00196  92 AQLKSLIEAFHGKGVQVIADIVINHRT-AEHKDG--------------------------------RGIYCLF------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 161 sgidhiENPTEDGVFK-----IVNDytgegwNEQVDDELGNF----DYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDG 231
Cdd:PLN00196 132 ------EGGTPDSRLDwgphmICRD------DTQYSDGTGNLdtgaDFAAAPDIDHLNKRVQRELIGWLLWLKSDIGFDA 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 232 FRLDAVKHIPAWFYKAWIEhvqevAPQPLFIVAEYWSHEV---------------EKLQQYIDLVEGKT---MLFDAPLQ 293
Cdd:PLN00196 200 WRLDFAKGYSAEVAKVYID-----GTEPSFAVAEIWTSMAyggdgkpeydqnahrQELVNWVDRVGGAAspaTVFDFTTK 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 294 MKFHEASrQGRDYDM--SQIFSGTLVEADPFHAVTLVTNHDTQPLQAL-EAPVEPWFKPLAYaliLLRENGVPSVFYADL 370
Cdd:PLN00196 275 GILNVAV-EGELWRLrgADGKAPGVIGWWPAKAVTFVDNHDTGSTQHMwPFPSDKVMQGYAY---ILTHPGNPCIFYDHF 350
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 489000892 371 FgasyeDTGgdgetyaiempVIEQLHELIDARQRfaHGVQ 410
Cdd:PLN00196 351 F-----DWG-----------LKEEIAALVSIRNR--NGIT 372
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
12-389 1.99e-12

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


Pssm-ID: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 68.85  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  12 WYYPTGGElWPEVEALAPSLNEIGINMVWLPPAYK--------GASGGYSvGYDTYDLFDLGEFdqkgsvatkYGDKAQL 83
Cdd:cd11320   38 LKKYWGGD-WQGIIDKLPYLKDLGVTAIWISPPVEninspiegGGNTGYH-GYWARDFKRTNEH---------FGTWEDF 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  84 LAAINALKEHNIAVLLDVVVNHKMGADEKESLRvqrvdeqdrtqideeiieceawtRYTFPVRAGQYSQFVwdykcfSGI 163
Cdd:cd11320  107 DELVDAAHANGIKVIIDFVPNHSSPADYAEDGA-----------------------LYDNGTLVGDYPNDD------NGW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 164 DHIENPTEDgvfkivndytgegWNEQVDDE---LGNFDYLMGANIDFRNHaVTEEIKYWArwvmeQTGCDGFRLDAVKHI 240
Cdd:cd11320  158 FHHNGGIDD-------------WSDREQVRyknLFDLADLNQSNPWVDQY-LKDAIKFWL-----DHGIDGIRVDAVKHM 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 241 PAWFYKAWIEHVQevAPQPLFIVAEYW-SHEVEKLQQYIDLVEGKTM-LFDAPLQMKFHE--ASRQGRDYDMSQIFSGTL 316
Cdd:cd11320  219 PPGWQKSFADAIY--SKKPVFTFGEWFlGSPDPGYEDYVKFANNSGMsLLDFPLNQAIRDvfAGFTATMYDLDAMLQQTS 296
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489000892 317 VEAD-PFHAVTLVTNHDTQPLQALEAPVEPWfkPLAYALIL-LRenGVPSVFYAD---LFGasyeDTGGDGETYAIEM 389
Cdd:cd11320  297 SDYNyENDLVTFIDNHDMPRFLTLNNNDKRL--HQALAFLLtSR--GIPVIYYGTeqyLHG----GTQVGGDPYNRPM 366
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
31-333 3.29e-10

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes 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: 61.83  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKGASggYSvGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkmgad 110
Cdd:cd11316   32 LNDLGVNGIWLMPIFPSPS--YH-GYDVTDYYA---------IEPDYGTMEDFERLIAEAHKRGIKVIIDLVINH----- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 111 ekeslrvqrvdeqdrTQIDEEIIEcEAWTRYTFPVRagqysqfvwDYKCFSGIDHIENptedgvfkivNDYTGEGWNEQV 190
Cdd:cd11316   95 ---------------TSSEHPWFQ-EAASSPDSPYR---------DYYIWADDDPGGW----------SSWGGNVWHKAG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 191 DDE--LGNFDYLMgANIDFRNHAVTEEIKYWARWVMEQtGCDGFRLDAVKHI----PAW--------FYKAWIEHVQEVA 256
Cdd:cd11316  140 DGGyyYGAFWSGM-PDLNLDNPAVREEIKKIAKFWLDK-GVDGFRLDAAKHIyengEGQadqeenieFWKEFRDYVKSVK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 257 PqPLFIVAEYWSHEvEKLQQYIDlvEGKTMLFDAPLQMKFHEASRQGRDYD-----MSQIFSGTLVEADPFHAVTLVTNH 331
Cdd:cd11316  218 P-DAYLVGEVWDDP-STIAPYYA--SGLDSAFNFDLAEAIIDSVKNGGSGAglakaLLRVYELYAKYNPDYIDAPFLSNH 293

                 ..
gi 489000892 332 DT 333
Cdd:cd11316  294 DQ 295
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
31-382 5.43e-08

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


Pssm-ID: 200479 [Multi-domain]  Cd Length: 407  Bit Score: 54.91  E-value: 5.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKGASGGYSV-GYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkMGA 109
Cdd:cd11340   54 LQDLGVTAIWLTPLLENDMPSYSYhGYAATDFY---------RIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNH-CGS 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 110 ------DEKESLRVQRVDEQDRTQIDEEIIeceawtrytFPVRAGQYSqfvwdykcfsgidhienptedgvFKIVNDytg 183
Cdd:cd11340  124 ehwwmkDLPTKDWINQTPEYTQTNHRRTAL---------QDPYASQAD-----------------------RKLFLD--- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 184 eGWneqvddelgnFDYLMgANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHIPAWFYKAWIEHVQEVAPQpLFIV 263
Cdd:cd11340  169 -GW----------FVPTM-PDLNQRNPLVARYLIQNSIWWIEYAGLDGIRVDTYPYSDKDFMSEWTKAIMEEYPN-FNIV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 264 AEYWSHEVEKL---QQYIDLVEGKT----MLFDAPLQMKFHEA--SRQGRDYDMSQIFSgTL----VEADPFHAVTLVTN 330
Cdd:cd11340  236 GEEWSGNPAIVaywQKGKKNPDGYDshlpSVMDFPLQDALRDAlnEEEGWDTGLNRLYE-TLandfLYPDPNNLVIFLDN 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489000892 331 HDTQplQALEAPVEPW--FKpLAYALIL-LRenGVPSVFYADLFGASYEDTGGDG 382
Cdd:cd11340  315 HDTS--RFYSQVGEDLdkFK-LALALLLtTR--GIPQLYYGTEILMKGTKKKDDG 364
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
17-267 9.58e-08

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


Pssm-ID: 200477 [Multi-domain]  Cd Length: 389  Bit Score: 54.03  E-value: 9.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  17 GGELWPEVEALaPSLNEIGINMVWLPPAYKGASggySVGYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIA 96
Cdd:cd11338   52 GGDLQGIIEKL-DYLKDLGVNAIYLNPIFEAPS---NHKYDTADYF---------KIDPHLGTEEDFKELVEEAHKRGIR 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  97 VLLDVVVNHkMGADEKESLRVQRVDEQDRTQiDEEIIECEAWTRYTFPvragqysqfvWDYKCFSGIDHIenPTedgvfk 176
Cdd:cd11338  119 VILDGVFNH-TGDDSPYFQDVLKYGESSAYQ-DWFSIYYFWPYFTDEP----------PNYESWWGVPSL--PK------ 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 177 ivndytgegWNEqvddelgnfdylmgANIDFRNH--AVteeIKYWarwvMEQTGCDGFRLDAVKHIPAWFYKAWIEHVQE 254
Cdd:cd11338  179 ---------LNT--------------ENPEVREYldSV---ARYW----LKEGDIDGWRLDVADEVPHEFWREFRKAVKA 228
                        250
                 ....*....|...
gi 489000892 255 VAPQPLfIVAEYW 267
Cdd:cd11338  229 VNPDAY-IIGEVW 240
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
24-333 1.02e-07

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: 53.71  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  24 VEALAPSLNEIGINMVWLPPAY----KGASGGYSVGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLL 99
Cdd:cd11313   24 VTKDLPRLKDLGVDILWLMPIHpigeKNRKGSLGSPYAVKDYRA---------VNPEYGTLEDFKALVDEAHDRGMKVIL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 100 DVVVNHkmgadekeslrvqrvdeqdrTQIDEEIIEceawTRYTFpvragqysqFVWDykcfsgidhienptEDGvfKIVN 179
Cdd:cd11313   95 DWVANH--------------------TAWDHPLVE----EHPEW---------YLRD--------------SDG--NITN 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 180 DYTgeGWNEQVDdelgnFDYlmgANIDFRNHaVTEEIKYWARwvmeQTGCDGFRLDAVKHIPAWFYKAWIEHVQEVAPqP 259
Cdd:cd11313  126 KVF--DWTDVAD-----LDY---SNPELRDY-MIDAMKYWVR----EFDVDGFRCDVAWGVPLDFWKEARAELRAVKP-D 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 260 LFIVAEYWSHEVEKLQQYIDlvegktMLFDAPLQMKFHEASRQGRDYDmsqifsgTLVEAD-------PFHAVTL--VTN 330
Cdd:cd11313  190 VFMLAEAEPRDDDELYSAFD------MTYDWDLHHTLNDVAKGKASAS-------DLLDALnaqeagyPKNAVKMrfLEN 256

                 ...
gi 489000892 331 HDT 333
Cdd:cd11313  257 HDE 259
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
31-240 1.37e-07

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: 53.77  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKgaSGGYSVGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHkmGAD 110
Cdd:cd11328   39 FKDIGIDAIWLSPIFK--SPMVDFGYDISDFTD---------IDPIFGTMEDFEELIAEAKKLGLKVILDFVPNH--SSD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 111 E----KESlrVQRVDEqdrtqideeiieceawtrytfpvragqYSQF-VWdykcfsgidhiENPTEDGVFKI------VN 179
Cdd:cd11328  106 EhewfQKS--VKRDEP---------------------------YKDYyVW-----------HDGKNNDNGTRvppnnwLS 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 180 DYTGEGWneQVDDELGNFdYL-----MGANIDFRNHAVTEEIK----YWARwvmeqTGCDGFRLDAVKHI 240
Cdd:cd11328  146 VFGGSAW--TWNEERQQY-YLhqfavKQPDLNYRNPKVVEEMKnvlrFWLD-----KGVDGFRIDAVPHL 207
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
78-381 1.64e-07

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: 53.05  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  78 GDKAQLLAAINALKEHNIAVLLDVVVNHkMGAdekeslrvqrvdeqdrtqideeiiecEAWTRYTFpvragQYSQFVWDY 157
Cdd:cd11315   65 GTEDDFKALCAAAHKYGIKIIVDVVFNH-MAN--------------------------EGSAIEDL-----WYPSADIEL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 158 KCFSgiDHienptedgvfkiVNDYTGEGWN--EQV--DDELGNFDylmganIDFRNHAVTEEIK-YWARwvMEQTGCDGF 232
Cdd:cd11315  113 FSPE--DF------------HGNGGISNWNdrWQVtqGRLGGLPD------LNTENPAVQQQQKaYLKA--LVALGVDGF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 233 RLDAVKHI--PAWFYKA---WIEHVQEVAPQPLFIVAEYWSHEVEKLQQYIDLVEGKTMLFDA---PLQMKFHEASRQGR 304
Cdd:cd11315  171 RFDAAKHIelPDEPSKAsdfWTNILNNLDKDGLFIYGEVLQDGGSRDSDYASYLSLGGVTASAygfPLRGALKNAFLFGG 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489000892 305 DYDMSQIFSGtlveADPFHAVTLVTNHDTQPLQALEAPV-EPWFKPLAYALILLRENGVPsVFYADLFGASYED-TGGD 381
Cdd:cd11315  251 SLDPASYGQA----LPSDRAVTWVESHDTYNNDGFESTGlDDEDERLAWAYLAARDGGTP-LFFSRPNGSGGTNpQIGD 324
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
35-332 1.66e-07

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: 53.34  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  35 GINMVWLPPAYK------GASGGYSvGYDTYDLFDLGEfdqkgsvatKYGDKAQLLAAINALKEHNIAVLLDVVVNHkMG 108
Cdd:cd11319   56 GFDAIWISPIVKniegntAYGEAYH-GYWAQDLYSLNP---------HFGTADDLKALSKALHKRGMYLMVDVVVNH-MA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 109 adekeslrvqrvdeqdrtqideeiieceawtrYTFPVRAGQYSQFVwdykCFSGIDHIENptedgvFKIVNDYTGEgwnE 188
Cdd:cd11319  125 --------------------------------SAGPGSDVDYSSFV----PFNDSSYYHP------YCWITDYNNQ---T 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 189 QVDD-ELGNfDYLMGANIDFRNHAVTEEIKYWARWVMEQTGCDGFRLDAVKHIPAWFYKAWIEHVQevapqpLFIVAEYW 267
Cdd:cd11319  160 SVEDcWLGD-DVVALPDLNTENPFVVSTLNDWIKNLVSNYSIDGLRIDTAKHVRKDFWPGFVEAAG------VFAIGEVF 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489000892 268 SHEVEKLQQYIDLVEGktmLFDAPLQMKFHEA--SRQGrdyDMSQIFSGTLVEA----DPFHAVTLVTNHD 332
Cdd:cd11319  233 DGDPNYVCPYQNYLDG---VLNYPLYYPLVDAfqSTKG---SMSALVDTINSVQssckDPTLLGTFLENHD 297
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
31-332 3.99e-06

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: 49.10  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYK--GASGGYSVGyDTYdlfdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHKmg 108
Cdd:cd11334   36 LQWLGVTAIWLLPFYPspLRDDGYDIA-DYY------------GVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHT-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 109 ADEKESLRVQRVDEQDRtqideeiieceaWTRYtfpvragqysqFVWDykcfsgiDHI-ENPTEDGVFKIVNDYTGEgWN 187
Cdd:cd11334  101 SDQHPWFQAARRDPDSP------------YRDY-----------YVWS-------DTPpKYKDARIIFPDVEKSNWT-WD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 188 EQVDDELGNFDYLMGANIDFRNHAVTEEIK----YWArwvmeQTGCDGFRLDAVKHI-------------PAWFYKAWIE 250
Cdd:cd11334  150 EVAGAYYWHRFYSHQPDLNFDNPAVREEILrimdFWL-----DLGVDGFRLDAVPYLieregtncenlpeTHDFLKRLRA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 251 HVQEVAPQPLFIvAEYwSHEVEKLQQYIDLVEGKTMLFDAPLQMKFHEASRQGRDYDMSQIFSGTLVEADPFHAVTLVTN 330
Cdd:cd11334  225 FVDRRYPDAILL-AEA-NQWPEEVREYFGDGDELHMAFNFPLNPRLFLALAREDAFPIIDALRQTPPIPEGCQWANFLRN 302

                 ..
gi 489000892 331 HD 332
Cdd:cd11334  303 HD 304
AmyAc_GTHase cd11325
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called ...
29-290 4.41e-06

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: 49.08  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  29 PSLNEIGINMVWLPPAykgAS--GGYSVGYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHk 106
Cdd:cd11325   62 DYLADLGVTAIELMPV---AEfpGERNWGYDGVLPF---------APESSYGGPDDLKRLVDAAHRRGLAVILDVVYNH- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 107 MGADekeslrvqrvdeqdrtqideeiieceawtrytfpvraGQY-SQFVWDYkcFSgiDHIENPTEDGvfkiVNDYtgeG 185
Cdd:cd11325  129 FGPD-------------------------------------GNYlWQFAGPY--FT--DDYSTPWGDA----INFD---G 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 186 WNEQVDDelgnFdylmganidFRNHAVteeikYWarwvMEQTGCDGFRLDAVKHI----PAWFYKAWIEHVQEVAPQP-L 260
Cdd:cd11325  161 PGDEVRQ----F---------FIDNAL-----YW----LREYHVDGLRLDAVHAIrddsGWHFLQELAREVRAAAAGRpA 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 489000892 261 FIVAEYWSHEveklQQYIDLVEGKTMLFDA 290
Cdd:cd11325  219 HLIAEDDRND----PRLVRPPELGGAGFDA 244
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
31-375 6.72e-06

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The 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: 48.46  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYkgASGGYSVGYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHKmgAD 110
Cdd:cd11348   31 IKSLGCNAIWLNPCF--DSPFKDAGYDVRDYY---------KVAPRYGTNEDLVRLFDEAHKRGIHVLLDLVPGHT--SD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 111 E----KESLRVQRVDEQDRTqideeiieceAWTRYTFPVRAGqysqfvwdYKCFSGIdhienPTEDGVFkIVN------- 179
Cdd:cd11348   98 EhpwfKESKKAENNEYSDRY----------IWTDSIWSGGPG--------LPFVGGE-----AERNGNY-IVNffscqpa 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 180 -DY-----TGEGWNEQVDDElgnfdylmGAnidfrnHAVTEEIKYWARWVMEQtGCDGFRLDA----VKHIP--AWFYKA 247
Cdd:cd11348  154 lNYgfahpPTEPWQQPVDAP--------GP------QATREAMKDIMRFWLDK-GADGFRVDMadslVKNDPgnKETIKL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 248 WIE---HVQEVAPQPLFiVAEyWSHEVEKLQQyidlveGKTMLF------DAPLQMKFHEASRQGRDYDMSqIFS----G 314
Cdd:cd11348  219 WQEiraWLDEEYPEAVL-VSE-WGNPEQSLKA------GFDMDFllhfggNGYNSLFRNLNTDGGHRRDNC-YFDasgkG 289
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489000892 315 TLVE-ADPFHA----------VTLVT-NHDTQPLQALEAPVEpwfKPLAYALILLREnGVPSVFYADLFGASY 375
Cdd:cd11348  290 DIKPfVDEYLPqyeatkgkgyISLPTcNHDTPRLNARLTEEE---LKLAFAFLLTMP-GVPFIYYGDEIGMRY 358
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
31-240 1.28e-05

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: 47.74  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKgaSGGYSVGYDTYDLFDLGEFdqkgsvatkYGDKAQLLAAINALKEHNIAVLLDVVVNHKmgAD 110
Cdd:cd11359   37 LKYLGVKTVWLSPIYK--SPMKDFGYDVSDFTDIDPM---------FGTMEDFERLLAAMHDRGMKLIMDFVPNHT--SD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 111 EKESLRVQRVDEQDRTqideeiieceawtrytfpvragqySQFVWdykcfsgidhiENPTEDGVFKIVND----YTGEGW 186
Cdd:cd11359  104 KHEWFQLSRNSTNPYT------------------------DYYIW-----------ADCTADGPGTPPNNwvsvFGNSAW 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489000892 187 neQVDDELGNFdYLMG-----ANIDFRNHAVTEE----IKYWarwvMEQtGCDGFRLDAVKHI 240
Cdd:cd11359  149 --EYDEKRNQC-YLHQflkeqPDLNFRNPDVQQEmddvLRFW----LDK-GVDGFRVDAVKHL 203
malS PRK09505
alpha-amylase; Reviewed
209-381 4.75e-05

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 45.81  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 209 NHAVTEEIKYW-ARWVMEqTGCDGFRLDAVKHI--PAWF---------YKAWIEHVQEVAP--QPLFIVAEYWSHEVEKL 274
Cdd:PRK09505 435 GYTPRDYLTHWlSQWVRD-YGIDGFRVDTAKHVelPAWQqlkqeasaaLAEWKKANPDKALddAPFWMTGEAWGHGVMKS 513
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 275 QQYIDlvegktmLFDAPLQMKFHEASRQGRDYdMSQI------FSGTLVEadpFHAVTLVTNHDTQPLQALEAPVePWFK 348
Cdd:PRK09505 514 DYYRH-------GFDAMINFDYQEQAAKAVDC-LAQMdptyqqMAEKLQD---FNVLSYLSSHDTRLFFEGGQSY-AKQR 581
                        170       180       190
                 ....*....|....*....|....*....|...
gi 489000892 349 PLAYALiLLRENGVpSVFYADLFGASYEDTGGD 381
Cdd:PRK09505 582 RAAELL-LLAPGAV-QIYYGDESARPFGPTGSD 612
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
31-105 1.13e-04

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: 44.37  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489000892  31 LNEIGINMVWLPPAYKgaSGGYSVGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNH 105
Cdd:cd11333   34 LKDLGVDAIWLSPIYP--SPQVDNGYDISDYRA---------IDPEFGTMEDFDELIKEAHKRGIKIIMDLVVNH 97
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
22-110 2.02e-04

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 44.32  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   22 PEVEALAPSLNEIGINMVWLPPAYKgASGGYSVGYDTYDlfdlgefdqKGSVATKYGDKAQLLAAINALKEHNIAVLLDV 101
Cdd:PRK14507  758 ADAEAILPYLAALGISHVYASPILK-ARPGSTHGYDIVD---------HSQINPEIGGEEGFERFCAALKAHGLGQLLDI 827
                          90
                  ....*....|.
gi 489000892  102 VVNHK--MGAD 110
Cdd:PRK14507  828 VPNHMgvGGAD 838
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
24-237 5.02e-04

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: 42.56  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  24 VEALAPSLNEIGINMVWLPPAYK---GAS-GGYSVG-YDTydlfdlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVL 98
Cdd:cd11324   88 LAEKIPYLKELGVTYLHLMPLLKppeGDNdGGYAVSdYRE--------------VDPRLGTMEDLRALAAELRERGISLV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  99 LDVVVNHKmgADEKE-SLRVQRVDEQ---------DRTQIDEEiiecEAWTRYTFPVRA-GqysQFVWDykcfsgidhie 167
Cdd:cd11324  154 LDFVLNHT--ADEHEwAQKARAGDPEyqdyyymfpDRTLPDAY----ERTLPEVFPDTApG---NFTWD----------- 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489000892 168 npTEDG--VFKIVNDYtgegwneQVDdelgnfdylmganIDFRNHAV----TEEIKYWArwvmeQTGCDGFRLDAV 237
Cdd:cd11324  214 --EEMGkwVWTTFNPF-------QWD-------------LNYANPAVfnemLDEMLFLA-----NQGVDVLRLDAV 262
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
31-268 7.52e-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: 200489 [Multi-domain]  Cd Length: 443  Bit Score: 41.92  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  31 LNEIGINMVWLPPAYKGASGGYSV-GYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNHKmG- 108
Cdd:cd11352   59 LKRLGVTALWLSPVFKQRPELETYhGYGIQNFLD---------VDPRFGTREDLRDLVDAAHARGIYVILDIILNHS-Gd 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 109 -----ADEKESLRVQRVDEQDRTQIDEEIIEceawtrytfpvrAGQYSQFVWDYkcfsgidhienptEDGV----FKIVN 179
Cdd:cd11352  129 vfsydDDRPYSSSPGYYRGFPNYPPGGWFIG------------GDQDALPEWRP-------------DDAIwpaeLQNLE 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892 180 DYTGEG----WNEQVDDELGNFDYLMganiDFRN------HAV----TEEIKYWarwvMEQTGCDGFRLDAVKHI-PAW- 243
Cdd:cd11352  184 YYTRKGrirnWDGYPEYKEGDFFSLK----DFRTgsgsipSAAldilARVYQYW----IAYADIDGFRIDTVKHMePGAa 255
                        250       260
                 ....*....|....*....|....*..
gi 489000892 244 --FYKAWIEHVQEVAPQPLFIVAEYWS 268
Cdd:cd11352  256 ryFCNAIKEFAQSIGKDNFFLFGEITG 282
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
29-105 8.86e-04

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: 41.88  E-value: 8.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489000892  29 PSLNEIGINMVWLPPAYKgaSGGYSVGYDTYDLFDlgefdqkgsVATKYGDKAQLLAAINALKEHNIAVLLDVVVNH 105
Cdd:cd11332   35 PYLAALGVDAIWLSPFYP--SPMADGGYDVADYRD---------VDPLFGTLADFDALVAAAHELGLRVIVDIVPNH 100
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
415-492 2.55e-03

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 37.32  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  415 DHPNCIAFSRSGtDDDPGCVVIMSNGDEGEKTLTLGENYGNKrWRDFLG---------NREEIVETDGEG---CATFTCN 482
Cdd:pfam02806   7 AENNVIAFERGD-DGGKLLVVFNFTPSVSYTDYRTGLPEAGT-YCEVLNtddeeyggsNTGEVVTVDGPGhpnSLTLTLP 84
                          90
                  ....*....|
gi 489000892  483 GGSVSVWVLE 492
Cdd:pfam02806  85 PLSALVLKVE 94
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
31-111 2.61e-03

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: 40.38  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892   31 LNEIGINMVWLPPAYKGASG-------GYSVGYDTYdLFDLGEfdqkGSVATKYGDKAQ----LLAAINALKEHNIAVLL 99
Cdd:TIGR02104 173 LKELGVTHVQLLPVFDFAGVdeedpnnAYNWGYDPL-NYNVPE----GSYSTNPYDPATrireLKQMIQALHENGIRVIM 247
                          90
                  ....*....|..
gi 489000892  100 DVVVNHKMGADE 111
Cdd:TIGR02104 248 DVVYNHTYSREE 259
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
23-105 8.43e-03

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: 38.31  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489000892  23 EVEALAPSLNEIGINMVWLPPAYKgaSGGYsvGYDTYDLFdlgefdqkgSVATKYGDKAQLLAAINALKEHNIAVLLDVV 102
Cdd:cd11353   31 KLEDWIPHLKKLGINAIYFGPVFE--SDSH--GYDTRDYY---------KIDRRLGTNEDFKAVCKKLHENGIKVVLDGV 97

                 ...
gi 489000892 103 VNH 105
Cdd:cd11353   98 FNH 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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