Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 506 CQVPTTVSVTFAVKATTVYGESIKIVGSISQLGSWNPSSATALNADSYTTDNPLWTGTINLPAGQSFEYKFIRVQ-NGAV 584
Cdd:cd05811   1 CATATTVAVTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKEsDGSV 80

                        90       100
                ....*....|....*....|....*..
gi 94730359 585 TWESDPNRKYTVPSTCGVkSAVQSDVW 611
Cdd:cd05811  81 TWESDPNRSYTVPSGCGT-TATVDDSW 106

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 506 CQVPTTVSVTFAVKATTVYGESIKIVGSISQLGSWNPSSATALNADSYTTDNPLWTGTINLPAGQSFEYKFIRVQ-NGAV 584
Cdd:cd05811   1 CATATTVAVTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKEsDGSV 80

                        90       100
                ....*....|....*....|....*..
gi 94730359 585 TWESDPNRKYTVPSTCGVkSAVQSDVW 611
Cdd:cd05811  81 TWESDPNRSYTVPSGCGT-TATVDDSW 106

Starch binding domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359    512 VSVTFAVK-ATTVYGESIKIVGSISQLGSWNPSSATALNADsyTTDNPLWTGTINLP-AGQSFEYKFIRVQN-GAVTWES 588
Cdd:smart01065   1 VSVTFKVRnGYTQPGESVYVVGSVPELGNWNPKKAVPLSPD--TDGYPLWKGTVSLPpAGTTIEYKYVKVDEdGSVTWES 78

                           90
                   ....*....|
gi 94730359    589 DPNRKYTVPS 598
Cdd:smart01065  79 GPNRRLTVPE 88

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 506 CQVPTTVSVTFAVKATTVYGESIKIVGSISQLGSWNPSSATALNADSYTTDNPLWTGTINLPAGQSFEYKFIRVQ-NGAV 584
Cdd:cd05811   1 CATATTVAVTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKEsDGSV 80

                        90       100
                ....*....|....*....|....*..
gi 94730359 585 TWESDPNRKYTVPSTCGVkSAVQSDVW 611
Cdd:cd05811  81 TWESDPNRSYTVPSGCGT-TATVDDSW 106

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 512 VSVTFAVKATTVYGESIKIVGSISQLGSWNPSSATALNADSYttdnPLWTGTINLPAGQSFEYKFIRVQ-NGAVTWESDP 590
Cdd:cd05808   1 VAVTFNVTATTVWGQNVYVVGNVPELGNWSPANAVALSAATY----PVWSGTVDLPAGTAIEYKYIKKDgSGTVTWESGP 76

                        90       100
                ....*....|....*....|..
gi 94730359 591 NRKYTVPSTCgvkSAVQSDVWR 612
Cdd:cd05808  77 NRTATTPASG---TLTLNDTWR 95

Starch binding domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359    512 VSVTFAVK-ATTVYGESIKIVGSISQLGSWNPSSATALNADsyTTDNPLWTGTINLP-AGQSFEYKFIRVQN-GAVTWES 588
Cdd:smart01065   1 VSVTFKVRnGYTQPGESVYVVGSVPELGNWNPKKAVPLSPD--TDGYPLWKGTVSLPpAGTTIEYKYVKVDEdGSVTWES 78

                           90
                   ....*....|
gi 94730359    589 DPNRKYTVPS 598
Cdd:smart01065  79 GPNRRLTVPE 88

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 513 SVTFAVKATTVY-GESIKIVGSISQLGSWNPSSATALNAdsytTDNPLWTGTINLPAGQ-SFEYKFIRVQN--GAVTWES 588
Cdd:cd05816   1 VVQFKILCPYVPkGQSVYVTGSSPELGNWDPQKALKLSD----VGFPIWEADIDISKDSfPFEYKYIIANKdsGVVSWEN 76

                        90
                ....*....|....*...
gi 94730359 589 DPNRKYTVPSTCGVKSAV 606
Cdd:cd05816  77 GPNRELSAPSLKGESSTL 94

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 514 VTFAVKATTVYGESIKIVGSISQLGSWNPSSATALNadsyTTDNPLWTGTINLPAGQSFEYK-----FIRVQNgaVTWES 588
Cdd:cd05817   2 VTFKIHYPTQFGEAVYISGNCNQLGNWNPSKAKRMQ----WNEGDLWTVDVGIPESVYIEYKyfvsnYDDPNT--VLWES 75

                        90
                ....*....|.
gi 94730359 589 DPNRKYTVPST 599
Cdd:cd05817  76 GPNRVLRTNHQ 86

Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 510 TTVSVTFAVKAT--TVYGESIKIVGSISQLGSWNPSSATALnADSYTTDNPLWTGTINLPAGQSFEYKFIRVQ-NGAVTW 586
Cdd:cd05820   1 KQIPVIFTVQNTpeTAPGEFLYLTGSVPELGNWSTSTDQAV-GPLLCPNWPDWFVVASVPAGTYIEFKFLKAPaDGTGTW 79

                        90
                ....*....|..
gi 94730359 587 ESDPNRKYTVPS 598
Cdd:cd05820  80 EGGSNHAYTTPS 91

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 512 VSVTFAVKATTVYGESIKIVGSISQLGSWNPSSATalnadSYTTDNplWTGTINLPAGQSFEYKFIRVQN-GAVTWESDP 590
Cdd:cd05818   2 VKLQVRLDHQVKFGEHVAILGSTKELGSWKKKVPM-----NWTENG--WVCDLELDGGELVEYKFVIVKRdGSVIWEGGN 74

                ....*..
gi 94730359 591 NRKYTVP 597
Cdd:cd05818  75 NRVLELP 81

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 512 VSVTFAVKATTVYgesikIVGSISQLGSWNPSSATALNADS---YTTDNPLWTGTINLPAGQS---FEYKFIRVQNGAVT 585
Cdd:cd05806   7 VVLTFADRDTELL-----VLGSRPELGSWDPQRAVPMRPARkalSPQEPSLWLGEVELSEPGSedtFWYKFLKREAGALI 81

                ..
gi 94730359 586 WE 587
Cdd:cd05806  82 WE 83

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359 512 VSVTFAVKATTVYGES-IKIVGSISQLGSWNPSSATALNADSYttdnplWTGTINLPAGQSFEYKFIRVQNGAVT-WESD 589
Cdd:cd05813   1 VNVTFRVHYITHSDAQlVAVTGDHEELGSWHSYIPLQYVKDGF------WSASVSLPVDTHVEWKFVLVENGQVTrWEEC 74

                ...
gi 94730359 590 PNR 592
Cdd:cd05813  75 SNR 77

4-alpha-glucanotransferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730359  525 GESIKIVGSISQLGSWNPSSATALNadsyTTDNPLWTGTINLPAGQ-SFEYKF-IRVQNGAVTWESDPNRKYTVPSTCGV 602
Cdd:PLN02950 167 GTSVYVTGSIAQLGNWQVDDGLKLN----YTGDSIWEADCLVPKSDfPIKYKYaLQTAEGLVSLELGVNRELSLDSSSGK 242

                         90
                 ....*....|....*...
gi 94730359  603 KSAV--------QSDVWR 612
Cdd:PLN02950 243 PPSYivasdgafREMPWR 260