1DTU,1CYG,1A47


Conserved Protein Domain Family
CBM20_CGTase

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cd05807: CBM20_CGTase 
Click on image for an interactive view with Cn3D
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. 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.
Statistics
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PSSM-Id: 99882
View PSSM: cd05807
Aligned: 6 rows
Threshold Bit Score: 183.146
Threshold Setting Gi: 118073811
Created: 10-Sep-2007
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
starch-bindingstarch-binding
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:starch-binding site 1 [chemical binding site]
Evidence:
  • Comment:Site 1 is small relative to site 2 and exhibits minimal structural changes upon ligand binding. It acts as an initial starch recognition site.
  • Structure:1DTU_A; Bacillus circulans CGTase CBM20 domain starch binding site 1 binds maltopentaose inhibitor; defined at 4A contacts.
    View structure with Cn3D
  • Citation:PMID 8672460

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                      #                                  #           ##
1DTU_A      585 DQVSVRFVVNNATTALGQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEFKFLKKQg-STVTWE 663 Bacillus circulans
1CYG_A      578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDsqGNVTWE 657 Geobacillus stea...
1A47_A      582 NQICVRFVVNNASTVYGENVYLTGNVAELGNWDTSKAIGPMFNQVVYQYPTWYYDVSVPAGTTIQFKFIKKNg-NTITWE 660 Thermoanaerobact...
ABN14270    613 DQVTVRFIIDNAETKLGENVFLVGNVHELGNWDPEQSVGKFFNQIVYQYPTWYYDVNVPANTDLEFKFIKIDqdNNVTWQ 692 Bacillus sp. BL-31
CAI46245    612 DQISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVHEYPNWYYDVNLPAGTDIEFKFVKIAsdGTVTWE 691 Haloferax medite...
ZP_01541987 604 PQKSVRFILENGYTQWGEAIYLVGNTPELGSWDPNKAIGPFYNQVVEQYPNWYQDVSVPTNTQLQFKFIKKNg-NQVIWE 682 Shewanella woody...
Feature 1          #                 
1DTU_A      664 GGSNHTFTAPSsGTATINVNW 684 Bacillus circulans
1CYG_A      658 SGSNHVYTTPTnTTGKIIVDW 678 Geobacillus stearothermophilus
1A47_A      661 GGSNHTYTVPSsSTGTVIVNW 681 Thermoanaerobacterium
ABN14270    693 SGANQTYSSPEsGTGIIRVDW 713 Bacillus sp. BL-31
CAI46245    692 SGSNRQYTTPTdSTGEYSGTW 712 Haloferax mediterranei
ZP_01541987 683 SGSNHQLSAGS-TDSSIRVNW 702 Shewanella woodyi ATCC 51908

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