Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.

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gi 1360775892 23 GPGHSVALAGSFNDWDPDTaPMKDadGSGCYRCTVSLQAGSYEYKFVVDDEWILDEENPnFAPNDFGTLNSVLSV 97
Cdd:pfam16561  9 GGGKKVYVTGSFDNWKKKI-PLQK--SGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLP-TATDDMGNLNNYIEV 79

N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins; E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase.

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gi 1360775892 18 FTLTAGPGH-SVALAGSFNDWDPDTAPMKdADGSGCYRCTVSLQAG-SYEYKFVVD-DEWILDEENPNFAPNDFGTLNSV 94
Cdd:cd07184    5 FELPAEQGAdSVSLVGDFNDWDPQATPMK-KLKNGTFSATLDLPAGrEYQFRYLIDgERWVNDPEADAYAPNGFGEENSV 83

                 ...
gi 1360775892 95 LSV 97
Cdd:cd07184   84 VSV 86

X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2.1.41) cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. BaPul is used industrially in the production of high fructose corn syrup, high maltose content syrups and low calorie and ''light'' beers. Pullulanases, in addition to the catalytic domain, include several carbohydrate-binding domains (CBMs) as well as domains of unknown function (termed ''X'' modules). X25 was identified in Bacillus acidopullulyticus pullulanase, and splits another domain of unknown function (X45). X25 is present in multiple copy in some pullulanases. It has been suggested that X25 and X45 are CBMs which target mixed alpha-1,6/alpha-1,4 linked D-glucan polysaccharides.

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gi 1360775892 27 SVALAGSFN-------DWDPD--TAPMKDADGSGCYRCTVSLQAGSYEYKFVVDDEW 74
Cdd:cd12962    1 SVTLVGSFQselgcagDWDPDclATQLTDDGNDGVYTFTTTLPAGDYEYKVALNGSW 57

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.

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gi 1360775892 18 FTLTAGPGHSVALAGSFNDWDPDTAPMKDADGSGCYRCTVSLQAGSYEYKFVVDD-EWILDEENPNFAPNDFGTLNSVL 95
Cdd:cd02688    4 FRIFAPGAKSVYLIGSFNGWWQAQALPMTKNGGGVWSATIPLPLGTYEYKYVIDGgKNVLPYFDPYYVAGDGNSGASIV 82

Early set domain associated with the catalytic domain of pullulanase-like proteins; E or "early" set domains are associated with the catalytic domain of pullulanase at either the N-terminal or C-terminal end, and in a few instances at both ends. Pullulanase (also called dextrinase or alpha-dextrin endo-1,6-alpha glucosidase) is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. The E set domain of pullulanase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.

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gi 1360775892 24 PGHSVALAGSFNDWDPDTApMKDAdGSGCYRCTVSLQAGSYEYKfVVDDEW 74
Cdd:cd02861    9 GGTTVYVRGSMNGWGEDDA-LTYQ-GNGVYSVTITLAAGSYEFK-VASADW 56

Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.

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gi 1360775892 32 GSFNDWDPDTAP-MKDADGSGCYRCTVSLQAGSyEYKFVVDDEWILDEENpnfAPNDFGTLNS 93
Cdd:cd12967    6 GNYQGWNPATAPaLYSPNGDGKYEGYVYLPGNF-EFKFTTAPNWDGDYGG---DGGGGGLLDG 64