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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   1 EYEVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLYHSRGIGEGFSGDYNEYFGLNVDTDALNYLGLDNHMLHTLDPKIITI 80
Cdd:cd11321   152 KWEVLRFLLSNLRWWLEEYRFDGFRFDGVTSMLYHHHGLGTGFSGDYGEYFGLNVDEDALVYLMLANDLLHELYPNAITI 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676322701  81 AEDVSGMPTLCRPVSEGGIGFDYRLGMAIPDKWIELLKEQSDDEWDMGNLVHTLTNRRWMESTVAYAESHDQALVGDKT 159
Cdd:cd11321   232 AEDVSGMPGLCRPVSEGGIGFDYRLAMAIPDKWIKLLKEKKDEDWNMGNIVHTLTNRRYGEKTIAYAESHDQALVGDKT 310

Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   1 EYEVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLYHSRGIGEGFSGDYNEYFGLNVDTDALNYLGLDNHMLHTLDPKIITI 80
Cdd:cd11321   152 KWEVLRFLLSNLRWWLEEYRFDGFRFDGVTSMLYHHHGLGTGFSGDYGEYFGLNVDEDALVYLMLANDLLHELYPNAITI 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676322701  81 AEDVSGMPTLCRPVSEGGIGFDYRLGMAIPDKWIELLKEQSDDEWDMGNLVHTLTNRRWMESTVAYAESHDQALVGDKT 159
Cdd:cd11321   232 AEDVSGMPGLCRPVSEGGIGFDYRLAMAIPDKWIKLLKEKKDEDWNMGNIVHTLTNRRYGEKTIAYAESHDQALVGDKT 310

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   3 EVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLY--HSRGIGEGFsgdYNEYfGLNVDTDALNYLGLDNHMLHTLDPKIITI 80
Cdd:COG0296   281 EVRNFLISNALYWLEEFHIDGLRVDAVASMLYldYSREEGEWI---PNKY-GGRENLEAIHFLRELNETVYERFPGVLTI 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676322701  81 AEDVSGMPTLCRPVSEGGIGFDYRlgmaipdkwiellkeqsddeWDMGnlvhtltnrrWMESTVAYAESHD 151
Cdd:COG0296   357 AEESTAWPGVTRPTELGGLGFDAK--------------------WNMG----------WMHDTLRYMTKDP 397

Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   1 EYEVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLYHSRGIGEGFSGDYNEYFGLNVDTDALNYLGLDNHMLHTLDPKIITI 80
Cdd:cd11321   152 KWEVLRFLLSNLRWWLEEYRFDGFRFDGVTSMLYHHHGLGTGFSGDYGEYFGLNVDEDALVYLMLANDLLHELYPNAITI 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676322701  81 AEDVSGMPTLCRPVSEGGIGFDYRLGMAIPDKWIELLKEQSDDEWDMGNLVHTLTNRRWMESTVAYAESHDQALVGDKT 159
Cdd:cd11321   232 AEDVSGMPGLCRPVSEGGIGFDYRLAMAIPDKWIKLLKEKKDEDWNMGNIVHTLTNRRYGEKTIAYAESHDQALVGDKT 310

alpha-amylase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   3 EVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLYHSRGIGEgFSGDYNEYFGLNVDTDALNYLGLDNHMLHTLDPKIITIAE 82
Cdd:PLN03244  507 DVLHFLISNLNWWITEYQIDGFQFHSLASMIYTHNGFAS-FNGDLDDYCNQYVDKDALMYLILANEILHALHPKIITIAE 585

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676322701  83 DVSGMPTLCRPVSEGGIGFDYRLGMAIPDKWIELLKEQSDDEWDMGNLVHTLT-NRRWMESTVAYAESHDQALVGDKT 159
Cdd:PLN03244  586 DATYYPGLCEPTSQGGLGFDYYVNLSAPDMWLDFLDNIPDHEWSMSKIVSTLIaNKEYADKMLSYAENHNQSISGGRS 663

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   3 EVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLY--HSRGIGEGFSgdyNEYfGLNVDTDALNYLGLDNHMLHTLDPKIITI 80
Cdd:cd11322   173 EVRSFLISNALYWLEEYHIDGLRVDAVSSMLYldYDRGPGEWIP---NIY-GGNENLEAIEFLKELNTVIHKRHPGVLTI 248

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676322701  81 AEDVSGMPTLCRPVSEGGIGFDYRlgmaipdkwiellkeqsddeWDMGnlvhtltnrrWMESTVAY 146
Cdd:cd11322   249 AEESTAWPGVTAPVEEGGLGFDYK--------------------WNMG----------WMNDTLDY 284

1,4-alpha-glucan branching protein GlgB;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   3 EVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLYhsRGIGEGFSGDYNEYfGLNVDTDALNYLGLDNHMLHTLDPKIITIAE 82
Cdd:PRK12313  285 EVRSFLISSALFWLDEYHLDGLRVDAVSNMLY--LDYDEEGEWTPNKY-GGRENLEAIYFLQKLNEVVYLEHPDVLMIAE 361

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676322701  83 DVSGMPTLCRPVSEGGIGFDYRlgmaipdkwiellkeqsddeWDMGnlvhtltnrrWMESTVAYAE 148
Cdd:PRK12313  362 ESTAWPKVTGPVEVGGLGFDYK--------------------WNMG----------WMNDTLRYFE 397

glycogen branching enzyme; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701    3 EVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLY--HSRGIGEGFSGDyneyFGLNVDTDALNYLGLDNHMLHTLDPKIITI 80
Cdd:PRK14705   880 EVRNFLVANALYWLDEFHIDGLRVDAVASMLYldYSREEGQWRPNR----FGGRENLEAISFLQEVNATVYKTHPGAVMI 955

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   81 AEDVSGMPTLCRPVSEGGIGFDYRLGMAipdkWI-ELLKEQSDDEwdmgnlvhtlTNRRWMESTV------AYAE----- 148
Cdd:PRK14705   956 AEESTAFPGVTAPTSHGGLGFGLKWNMG----WMhDSLKYASEDP----------INRKWHHGTItfslvyAFTEnfllp 1021

                   ....*....
gi 1676322701  149 -SHDQALVG 156
Cdd:PRK14705  1022 iSHDEVVHG 1030

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   2 YEVLRFLLSNLRWWHDEYNFDGYRFDGVTSMlyhsrgigegfsgdyneyfglnVDTDALNYLGLDNHMLHTL--DPKIIT 79
Cdd:cd11325   163 DEVRQFFIDNALYWLREYHVDGLRLDAVHAI----------------------RDDSGWHFLQELAREVRAAaaGRPAHL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701  80 IAEDVSGMPTLCRPVSEGGIGFD---------------------YRLGMAIPDKWIELLKE----QSDDEWDMGNLVHTL 134
Cdd:cd11325   221 IAEDDRNDPRLVRPPELGGAGFDaqwnddfhhalhvaltgeregYYADFGPAEDLARALAEgfvyQGQYSPFRGRRHGRP 300

                         170
                  ....*....|....*....
gi 1676322701 135 TNRRWMESTVAYAESHDQA 153
Cdd:cd11325   301 SADLPPTRFVVFLQNHDQV 319

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701   7 FLLSNLRWWHDEYNFDGYRFDgvtsmlyHSRGIGEGFSGDYNEYfglNVDTDALNYLGLDNHMLHTLDPKIITIAEDVSG 86
Cdd:cd11350   156 FVDDVNRYWLEEYHIDGFRFD-------LTKGFTQKPTGGGAWG---GYDAARIDFLKRYADEAKAVDKDFYVIAEHLPD 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676322701  87 MPTLCRPVSEG----GIGFDYRLGMAIPDKWIELLKEQSDDEWDMGNLVHTltnrrwmeSTVAYAESHDQ 152
Cdd:cd11350   226 NPEETELATYGmslwGNSNYSFSQAAMGYQGGSLLLDYSGDPYQNGGWSPK--------NAVNYMESHDE 287